ZA200302907B - Medicament containing activated antithrombin III. - Google Patents

Medicament containing activated antithrombin III. Download PDF

Info

Publication number: ZA200302907B
Authority: ZA; South Africa
Prior art keywords: idaat; tsp; antithrombin; thrombospondin; cells
Prior art date: 2000-09-12

Application number

ZA200302907A

Other languages

English (en)

Inventor

Martin Brodde

Beate Kehrel

Original Assignee

Beate Kehrel

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

2000-09-12

Filing date

2003-04-14

Publication date

2003-09-15

2003-04-14 Application filed by Beate Kehrel filed Critical Beate Kehrel

2003-09-15 Publication of ZA200302907B publication Critical patent/ZA200302907B/en

Links

108090000935 Antithrombin III Proteins 0.000 title claims description 22
102000004411 Antithrombin III Human genes 0.000 title claims description 13
229960005348 antithrombin iii Drugs 0.000 title claims description 13
239000003814 drug Substances 0.000 title description 9
210000001772 blood platelet Anatomy 0.000 claims description 100
238000000034 method Methods 0.000 claims description 44
239000004019 antithrombin Substances 0.000 claims description 41
239000000825 pharmaceutical preparation Substances 0.000 claims description 19
230000008569 process Effects 0.000 claims description 19
108090000765 processed proteins & peptides Proteins 0.000 claims description 19
239000000126 substance Substances 0.000 claims description 18
208000015181 infectious disease Diseases 0.000 claims description 15
238000002360 preparation method Methods 0.000 claims description 15
206010061218 Inflammation Diseases 0.000 claims description 14
230000004054 inflammatory process Effects 0.000 claims description 14
230000003993 interaction Effects 0.000 claims description 14
210000004369 blood Anatomy 0.000 claims description 12
239000008280 blood Substances 0.000 claims description 12
102000004196 processed proteins & peptides Human genes 0.000 claims description 12
206010040047 Sepsis Diseases 0.000 claims description 8
208000032852 chronic lymphocytic leukemia Diseases 0.000 claims description 6
238000011321 prophylaxis Methods 0.000 claims description 6
230000029663 wound healing Effects 0.000 claims description 6
230000001154 acute effect Effects 0.000 claims description 5
230000007812 deficiency Effects 0.000 claims description 5
208000010839 B-cell chronic lymphocytic leukemia Diseases 0.000 claims description 4
208000031886 HIV Infections Diseases 0.000 claims description 4
208000031422 Lymphocytic Chronic B-Cell Leukemia Diseases 0.000 claims description 4
101710178510 Defensin-2 Proteins 0.000 claims description 3
206010020751 Hypersensitivity Diseases 0.000 claims description 3
206010027476 Metastases Diseases 0.000 claims description 3
230000023555 blood coagulation Effects 0.000 claims description 3
230000001684 chronic effect Effects 0.000 claims description 3
230000003902 lesion Effects 0.000 claims description 3
208000032839 leukemia Diseases 0.000 claims description 3
210000000653 nervous system Anatomy 0.000 claims description 3
210000000056 organ Anatomy 0.000 claims description 3
239000000546 pharmaceutical excipient Substances 0.000 claims description 3
238000002054 transplantation Methods 0.000 claims description 3
230000004614 tumor growth Effects 0.000 claims description 3
206010010356 Congenital anomaly Diseases 0.000 claims description 2
208000004221 Multiple Trauma Diseases 0.000 claims description 2
208000023637 Multiple injury Diseases 0.000 claims description 2
208000030852 Parasitic disease Diseases 0.000 claims description 2
230000000172 allergic effect Effects 0.000 claims description 2
239000003242 anti bacterial agent Substances 0.000 claims description 2
229940088710 antibiotic agent Drugs 0.000 claims description 2
230000010100 anticoagulation Effects 0.000 claims description 2
208000010668 atopic eczema Diseases 0.000 claims description 2
238000002512 chemotherapy Methods 0.000 claims description 2
230000035987 intoxication Effects 0.000 claims description 2
231100000566 intoxication Toxicity 0.000 claims description 2
238000007912 intraperitoneal administration Methods 0.000 claims description 2
238000001990 intravenous administration Methods 0.000 claims description 2
201000004792 malaria Diseases 0.000 claims description 2
230000009401 metastasis Effects 0.000 claims description 2
230000010410 reperfusion Effects 0.000 claims description 2
238000002560 therapeutic procedure Methods 0.000 claims description 2
230000000451 tissue damage Effects 0.000 claims description 2
231100000827 tissue damage Toxicity 0.000 claims description 2
230000023597 hemostasis Effects 0.000 claims 2
208000027205 Congenital disease Diseases 0.000 claims 1
208000029767 Congenital, Hereditary, and Neonatal Diseases and Abnormalities Diseases 0.000 claims 1
208000037357 HIV infectious disease Diseases 0.000 claims 1
208000037919 acquired disease Diseases 0.000 claims 1
208000033519 human immunodeficiency virus infectious disease Diseases 0.000 claims 1
238000007918 intramuscular administration Methods 0.000 claims 1
102100036034 Thrombospondin-1 Human genes 0.000 description 75
101710159964 Tail sheath protein Proteins 0.000 description 59
101710168563 Tail spike protein Proteins 0.000 description 59
210000004027 cell Anatomy 0.000 description 57
210000001616 monocyte Anatomy 0.000 description 53
108060008245 Thrombospondin Proteins 0.000 description 41
102000002938 Thrombospondin Human genes 0.000 description 40
108090000623 proteins and genes Proteins 0.000 description 27
235000018102 proteins Nutrition 0.000 description 26
102000004169 proteins and genes Human genes 0.000 description 26
108010045374 CD36 Antigens Proteins 0.000 description 24
230000001404 mediated effect Effects 0.000 description 24
102000049320 CD36 Human genes 0.000 description 23
239000000872 buffer Substances 0.000 description 23
239000011575 calcium Substances 0.000 description 21
230000001640 apoptogenic effect Effects 0.000 description 19
238000006243 chemical reaction Methods 0.000 description 18
239000002953 phosphate buffered saline Substances 0.000 description 18
238000002965 ELISA Methods 0.000 description 17
102100035140 Vitronectin Human genes 0.000 description 17
108010031318 Vitronectin Proteins 0.000 description 17
102000008186 Collagen Human genes 0.000 description 16
108010035532 Collagen Proteins 0.000 description 16
108010046722 Thrombospondin 1 Proteins 0.000 description 16
229920001436 collagen Polymers 0.000 description 16
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 15
201000010099 disease Diseases 0.000 description 13
101710112753 A-type inclusion protein A25 homolog Proteins 0.000 description 12
241000699670 Mus sp. Species 0.000 description 12
230000002776 aggregation Effects 0.000 description 12
238000004220 aggregation Methods 0.000 description 12
KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 12
230000000694 effects Effects 0.000 description 12
210000002889 endothelial cell Anatomy 0.000 description 12
MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 12
230000006870 function Effects 0.000 description 12
230000005764 inhibitory process Effects 0.000 description 12
241001465754 Metazoa Species 0.000 description 11
108010044426 integrins Proteins 0.000 description 11
102000006495 integrins Human genes 0.000 description 11
108010049003 Fibrinogen Proteins 0.000 description 10
102000008946 Fibrinogen Human genes 0.000 description 10
206010057249 Phagocytosis Diseases 0.000 description 10
230000015572 biosynthetic process Effects 0.000 description 10
229940012952 fibrinogen Drugs 0.000 description 10
230000008782 phagocytosis Effects 0.000 description 10
239000000243 solution Substances 0.000 description 10
102100022977 Antithrombin-III Human genes 0.000 description 9
HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 9
102000046299 Transforming Growth Factor beta1 Human genes 0.000 description 9
101800002279 Transforming growth factor beta-1 Proteins 0.000 description 9
208000027418 Wounds and injury Diseases 0.000 description 9
238000002835 absorbance Methods 0.000 description 9
230000004913 activation Effects 0.000 description 9
229920000669 heparin Polymers 0.000 description 9
229960002897 heparin Drugs 0.000 description 9
241000894006 Bacteria Species 0.000 description 8
241000283707 Capra Species 0.000 description 8
108010065805 Interleukin-12 Proteins 0.000 description 8
102000013462 Interleukin-12 Human genes 0.000 description 8
102100032913 Leukocyte surface antigen CD47 Human genes 0.000 description 8
241000283973 Oryctolagus cuniculus Species 0.000 description 8
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
210000001744 T-lymphocyte Anatomy 0.000 description 8
238000010790 dilution Methods 0.000 description 8
239000012895 dilution Substances 0.000 description 8
229940117681 interleukin-12 Drugs 0.000 description 8
210000002540 macrophage Anatomy 0.000 description 8
102000005962 receptors Human genes 0.000 description 8
108020003175 receptors Proteins 0.000 description 8
230000019254 respiratory burst Effects 0.000 description 8
210000002966 serum Anatomy 0.000 description 8
210000001519 tissue Anatomy 0.000 description 8
208000000104 Arthus reaction Diseases 0.000 description 7
102000003886 Glycoproteins Human genes 0.000 description 7
108090000288 Glycoproteins Proteins 0.000 description 7
101000868279 Homo sapiens Leukocyte surface antigen CD47 Proteins 0.000 description 7
206010053614 Type III immune complex mediated reaction Diseases 0.000 description 7
206010052428 Wound Diseases 0.000 description 7
238000002474 experimental method Methods 0.000 description 7
238000011534 incubation Methods 0.000 description 7
239000000758 substrate Substances 0.000 description 7
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 6
241000699666 Mus <mouse, genus> Species 0.000 description 6
206010028980 Neoplasm Diseases 0.000 description 6
241000700605 Viruses Species 0.000 description 6
239000011324 bead Substances 0.000 description 6
230000002950 deficient Effects 0.000 description 6
229940079593 drug Drugs 0.000 description 6
230000007246 mechanism Effects 0.000 description 6
239000011859 microparticle Substances 0.000 description 6
101100208237 Bos taurus THBS2 gene Proteins 0.000 description 5
102100037904 CD9 antigen Human genes 0.000 description 5
108010088842 Fibrinolysin Proteins 0.000 description 5
108010067306 Fibronectins Proteins 0.000 description 5
102000016359 Fibronectins Human genes 0.000 description 5
241000713772 Human immunodeficiency virus 1 Species 0.000 description 5
108090000190 Thrombin Proteins 0.000 description 5
230000001419 dependent effect Effects 0.000 description 5
210000003714 granulocyte Anatomy 0.000 description 5
239000013642 negative control Substances 0.000 description 5
230000003448 neutrophilic effect Effects 0.000 description 5
244000045947 parasite Species 0.000 description 5
229940012957 plasmin Drugs 0.000 description 5
239000004033 plastic Substances 0.000 description 5
229920003023 plastic Polymers 0.000 description 5
230000028327 secretion Effects 0.000 description 5
238000012360 testing method Methods 0.000 description 5
229960004072 thrombin Drugs 0.000 description 5
229940099456 transforming growth factor beta 1 Drugs 0.000 description 5
238000011282 treatment Methods 0.000 description 5
101710205625 Capsid protein p24 Proteins 0.000 description 4
102000014150 Interferons Human genes 0.000 description 4
108010050904 Interferons Proteins 0.000 description 4
102000003992 Peroxidases Human genes 0.000 description 4
101710177166 Phosphoprotein Proteins 0.000 description 4
241000700159 Rattus Species 0.000 description 4
101710149279 Small delta antigen Proteins 0.000 description 4
102000004887 Transforming Growth Factor beta Human genes 0.000 description 4
108090001012 Transforming Growth Factor beta Proteins 0.000 description 4
230000003213 activating effect Effects 0.000 description 4
239000000556 agonist Substances 0.000 description 4
239000000427 antigen Substances 0.000 description 4
102000036639 antigens Human genes 0.000 description 4
108091007433 antigens Proteins 0.000 description 4
239000003795 chemical substances by application Substances 0.000 description 4
239000012153 distilled water Substances 0.000 description 4
238000000635 electron micrograph Methods 0.000 description 4
210000003979 eosinophil Anatomy 0.000 description 4
210000003743 erythrocyte Anatomy 0.000 description 4
229910052739 hydrogen Inorganic materials 0.000 description 4
230000002401 inhibitory effect Effects 0.000 description 4
229940079322 interferon Drugs 0.000 description 4
238000004519 manufacturing process Methods 0.000 description 4
244000052769 pathogen Species 0.000 description 4
210000005259 peripheral blood Anatomy 0.000 description 4
239000011886 peripheral blood Substances 0.000 description 4
210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 4
108040007629 peroxidase activity proteins Proteins 0.000 description 4
YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 4
210000002381 plasma Anatomy 0.000 description 4
239000013641 positive control Substances 0.000 description 4
ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 4
102000010834 Extracellular Matrix Proteins Human genes 0.000 description 3
108010037362 Extracellular Matrix Proteins Proteins 0.000 description 3
102000007625 Hirudins Human genes 0.000 description 3
108010007267 Hirudins Proteins 0.000 description 3
102000015696 Interleukins Human genes 0.000 description 3
108010063738 Interleukins Proteins 0.000 description 3
108010052285 Membrane Proteins Proteins 0.000 description 3
229910019093 NaOCl Inorganic materials 0.000 description 3
206010029113 Neovascularisation Diseases 0.000 description 3
239000004365 Protease Substances 0.000 description 3
239000012980 RPMI-1640 medium Substances 0.000 description 3
108010022999 Serine Proteases Proteins 0.000 description 3
102000012479 Serine Proteases Human genes 0.000 description 3
230000000996 additive effect Effects 0.000 description 3
238000004458 analytical method Methods 0.000 description 3
230000006907 apoptotic process Effects 0.000 description 3
239000006143 cell culture medium Substances 0.000 description 3
230000009918 complex formation Effects 0.000 description 3
238000004132 cross linking Methods 0.000 description 3
230000006378 damage Effects 0.000 description 3
231100000673 dose–response relationship Toxicity 0.000 description 3
230000003511 endothelial effect Effects 0.000 description 3
210000003038 endothelium Anatomy 0.000 description 3
229960001123 epoprostenol Drugs 0.000 description 3
KAQKFAOMNZTLHT-VVUHWYTRSA-N epoprostenol Chemical compound O1C(=CCCCC(O)=O)C[C@@H]2[C@@H](/C=C/[C@@H](O)CCCCC)[C@H](O)C[C@@H]21 KAQKFAOMNZTLHT-VVUHWYTRSA-N 0.000 description 3
230000012010 growth Effects 0.000 description 3
239000001963 growth medium Substances 0.000 description 3
229940006607 hirudin Drugs 0.000 description 3
WQPDUTSPKFMPDP-OUMQNGNKSA-N hirudin Chemical compound C([C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(OS(O)(=O)=O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]1NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H]2CSSC[C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@H](C(NCC(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N2)=O)CSSC1)C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)CSSC1)C(C)C)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 WQPDUTSPKFMPDP-OUMQNGNKSA-N 0.000 description 3
210000003630 histaminocyte Anatomy 0.000 description 3
208000014674 injury Diseases 0.000 description 3
239000004816 latex Substances 0.000 description 3
229920000126 latex Polymers 0.000 description 3
239000011159 matrix material Substances 0.000 description 3
230000003647 oxidation Effects 0.000 description 3
238000007254 oxidation reaction Methods 0.000 description 3
210000004303 peritoneum Anatomy 0.000 description 3
230000010118 platelet activation Effects 0.000 description 3
210000004623 platelet-rich plasma Anatomy 0.000 description 3
230000000770 proinflammatory effect Effects 0.000 description 3
238000002390 rotary evaporation Methods 0.000 description 3
239000011780 sodium chloride Substances 0.000 description 3
SUKJFIGYRHOWBL-UHFFFAOYSA-N sodium hypochlorite Chemical compound [Na+].Cl[O-] SUKJFIGYRHOWBL-UHFFFAOYSA-N 0.000 description 3
239000000725 suspension Substances 0.000 description 3
LKDMKWNDBAVNQZ-UHFFFAOYSA-N 4-[[1-[[1-[2-[[1-(4-nitroanilino)-1-oxo-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid Chemical compound OC(=O)CCC(=O)NC(C)C(=O)NC(C)C(=O)N1CCCC1C(=O)NC(C(=O)NC=1C=CC(=CC=1)[N+]([O-])=O)CC1=CC=CC=C1 LKDMKWNDBAVNQZ-UHFFFAOYSA-N 0.000 description 2
102000002260 Alkaline Phosphatase Human genes 0.000 description 2
108020004774 Alkaline Phosphatase Proteins 0.000 description 2
IYMAXBFPHPZYIK-BQBZGAKWSA-N Arg-Gly-Asp Chemical compound NC(N)=NCCC[C@H](N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(O)=O IYMAXBFPHPZYIK-BQBZGAKWSA-N 0.000 description 2
OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
102000005701 Calcium-Binding Proteins Human genes 0.000 description 2
108010045403 Calcium-Binding Proteins Proteins 0.000 description 2
102100027473 Cartilage oligomeric matrix protein Human genes 0.000 description 2
101710176668 Cartilage oligomeric matrix protein Proteins 0.000 description 2
108090000617 Cathepsin G Proteins 0.000 description 2
102000004173 Cathepsin G Human genes 0.000 description 2
102000019034 Chemokines Human genes 0.000 description 2
108010012236 Chemokines Proteins 0.000 description 2
241000223935 Cryptosporidium Species 0.000 description 2
102000004127 Cytokines Human genes 0.000 description 2
108090000695 Cytokines Proteins 0.000 description 2
102100038132 Endogenous retrovirus group K member 6 Pro protein Human genes 0.000 description 2
101800004490 Endothelin-1 Proteins 0.000 description 2
108010074860 Factor Xa Proteins 0.000 description 2
201000000584 Gray platelet syndrome Diseases 0.000 description 2
229920002971 Heparan sulfate Polymers 0.000 description 2
241000282412 Homo Species 0.000 description 2
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
108010028275 Leukocyte Elastase Proteins 0.000 description 2
102000016799 Leukocyte elastase Human genes 0.000 description 2
102000009112 Mannose-Binding Lectin Human genes 0.000 description 2
108010087870 Mannose-Binding Lectin Proteins 0.000 description 2
102000018697 Membrane Proteins Human genes 0.000 description 2
108010067372 Pancreatic elastase Proteins 0.000 description 2
102000016387 Pancreatic elastase Human genes 0.000 description 2
108091005804 Peptidases Proteins 0.000 description 2
229920001213 Polysorbate 20 Polymers 0.000 description 2
241000605862 Porphyromonas gingivalis Species 0.000 description 2
102100038567 Properdin Human genes 0.000 description 2
108010005642 Properdin Proteins 0.000 description 2
229920005654 Sephadex Polymers 0.000 description 2
239000012507 Sephadex™ Substances 0.000 description 2
102100036428 Spondin-1 Human genes 0.000 description 2
101710092167 Spondin-1 Proteins 0.000 description 2
241000191967 Staphylococcus aureus Species 0.000 description 2
239000007983 Tris buffer Substances 0.000 description 2
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 2
108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 2
RXSUFCOOZSGWSW-UHFFFAOYSA-M acetyloxy-(4-aminophenyl)mercury Chemical compound CC(=O)O[Hg]C1=CC=C(N)C=C1 RXSUFCOOZSGWSW-UHFFFAOYSA-M 0.000 description 2
239000000654 additive Substances 0.000 description 2
239000000853 adhesive Substances 0.000 description 2
230000001070 adhesive effect Effects 0.000 description 2
235000001014 amino acid Nutrition 0.000 description 2
150000001413 amino acids Chemical class 0.000 description 2
230000033115 angiogenesis Effects 0.000 description 2
230000001363 autoimmune Effects 0.000 description 2
102000052586 bactericidal permeability increasing protein Human genes 0.000 description 2
108010032816 bactericidal permeability increasing protein Proteins 0.000 description 2
230000033228 biological regulation Effects 0.000 description 2
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
230000020411 cell activation Effects 0.000 description 2
230000021164 cell adhesion Effects 0.000 description 2
238000004113 cell culture Methods 0.000 description 2
230000030833 cell death Effects 0.000 description 2
230000008859 change Effects 0.000 description 2
230000016396 cytokine production Effects 0.000 description 2
230000000254 damaging effect Effects 0.000 description 2
210000004443 dendritic cell Anatomy 0.000 description 2
230000030609 dephosphorylation Effects 0.000 description 2
238000006209 dephosphorylation reaction Methods 0.000 description 2
238000011161 development Methods 0.000 description 2
230000018109 developmental process Effects 0.000 description 2
208000035475 disorder Diseases 0.000 description 2
238000001493 electron microscopy Methods 0.000 description 2
239000002158 endotoxin Substances 0.000 description 2
210000002744 extracellular matrix Anatomy 0.000 description 2
230000020764 fibrinolysis Effects 0.000 description 2
230000006872 improvement Effects 0.000 description 2
238000000338 in vitro Methods 0.000 description 2
238000010348 incorporation Methods 0.000 description 2
230000001524 infective effect Effects 0.000 description 2
230000008595 infiltration Effects 0.000 description 2
238000001764 infiltration Methods 0.000 description 2
230000002757 inflammatory effect Effects 0.000 description 2
239000003112 inhibitor Substances 0.000 description 2
238000002347 injection Methods 0.000 description 2
239000007924 injection Substances 0.000 description 2
150000002500 ions Chemical class 0.000 description 2
JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
150000002632 lipids Chemical class 0.000 description 2
210000004072 lung Anatomy 0.000 description 2
239000002609 medium Substances 0.000 description 2
239000012528 membrane Substances 0.000 description 2
244000005700 microbiome Species 0.000 description 2
239000000203 mixture Substances 0.000 description 2
210000000822 natural killer cell Anatomy 0.000 description 2
230000014399 negative regulation of angiogenesis Effects 0.000 description 2
210000002241 neurite Anatomy 0.000 description 2
230000003472 neutralizing effect Effects 0.000 description 2
210000000440 neutrophil Anatomy 0.000 description 2
230000001717 pathogenic effect Effects 0.000 description 2
230000001575 pathological effect Effects 0.000 description 2
239000004417 polycarbonate Substances 0.000 description 2
229920000515 polycarbonate Polymers 0.000 description 2
239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
229920001184 polypeptide Polymers 0.000 description 2
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
230000035755 proliferation Effects 0.000 description 2
230000002685 pulmonary effect Effects 0.000 description 2
238000000746 purification Methods 0.000 description 2
230000009257 reactivity Effects 0.000 description 2
230000002829 reductive effect Effects 0.000 description 2
230000001105 regulatory effect Effects 0.000 description 2
230000003252 repetitive effect Effects 0.000 description 2
239000003001 serine protease inhibitor Substances 0.000 description 2
210000000329 smooth muscle myocyte Anatomy 0.000 description 2
239000011734 sodium Substances 0.000 description 2
239000006228 supernatant Substances 0.000 description 2
238000003786 synthesis reaction Methods 0.000 description 2
-1 tbrombospondin Proteins 0.000 description 2
230000008719 thickening Effects 0.000 description 2
IMRYETFJNLKUHK-UHFFFAOYSA-N traseolide Chemical compound CC1=C(C(C)=O)C=C2C(C(C)C)C(C)C(C)(C)C2=C1 IMRYETFJNLKUHK-UHFFFAOYSA-N 0.000 description 2
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
239000003656 tris buffered saline Substances 0.000 description 2
QDLHCMPXEPAAMD-QAIWCSMKSA-N wortmannin Chemical compound C1([C@]2(C)C3=C(C4=O)OC=C3C(=O)O[C@@H]2COC)=C4[C@@H]2CCC(=O)[C@@]2(C)C[C@H]1OC(C)=O QDLHCMPXEPAAMD-QAIWCSMKSA-N 0.000 description 2
QDLHCMPXEPAAMD-UHFFFAOYSA-N wortmannin Natural products COCC1OC(=O)C2=COC(C3=O)=C2C1(C)C1=C3C2CCC(=O)C2(C)CC1OC(C)=O QDLHCMPXEPAAMD-UHFFFAOYSA-N 0.000 description 2
KWPACVJPAFGBEQ-IKGGRYGDSA-N (2s)-1-[(2r)-2-amino-3-phenylpropanoyl]-n-[(3s)-1-chloro-6-(diaminomethylideneamino)-2-oxohexan-3-yl]pyrrolidine-2-carboxamide Chemical compound C([C@@H](N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)CCl)C1=CC=CC=C1 KWPACVJPAFGBEQ-IKGGRYGDSA-N 0.000 description 1
ITZMJCSORYKOSI-AJNGGQMLSA-N APGPR Enterostatin Chemical compound C[C@H](N)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N1[C@H](C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)CCC1 ITZMJCSORYKOSI-AJNGGQMLSA-N 0.000 description 1
102000011767 Acute-Phase Proteins Human genes 0.000 description 1
108010062271 Acute-Phase Proteins Proteins 0.000 description 1
108090000672 Annexin A5 Proteins 0.000 description 1
102000004121 Annexin A5 Human genes 0.000 description 1
101710163968 Antistasin Proteins 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
102400000687 Big endothelin-1 Human genes 0.000 description 1
101800001398 Big endothelin-1 Proteins 0.000 description 1
208000008439 Biliary Liver Cirrhosis Diseases 0.000 description 1
208000033222 Biliary cirrhosis primary Diseases 0.000 description 1
201000004569 Blindness Diseases 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
102100021943 C-C motif chemokine 2 Human genes 0.000 description 1
101710155857 C-C motif chemokine 2 Proteins 0.000 description 1
108010074051 C-Reactive Protein Proteins 0.000 description 1
102100032752 C-reactive protein Human genes 0.000 description 1
101150015687 CDA7 gene Proteins 0.000 description 1
108010076667 Caspases Proteins 0.000 description 1
102000011727 Caspases Human genes 0.000 description 1
102000000844 Cell Surface Receptors Human genes 0.000 description 1
108010001857 Cell Surface Receptors Proteins 0.000 description 1
102000001327 Chemokine CCL5 Human genes 0.000 description 1
108010055166 Chemokine CCL5 Proteins 0.000 description 1
QDHHCQZDFGDHMP-UHFFFAOYSA-N Chloramine Chemical compound ClN QDHHCQZDFGDHMP-UHFFFAOYSA-N 0.000 description 1
108090001069 Chymopapain Proteins 0.000 description 1
XXAXVMUWHZHZMJ-UHFFFAOYSA-N Chymopapain Chemical compound OC1=CC(S(O)(=O)=O)=CC(S(O)(=O)=O)=C1O XXAXVMUWHZHZMJ-UHFFFAOYSA-N 0.000 description 1
108010048623 Collagen Receptors Proteins 0.000 description 1
102000012422 Collagen Type I Human genes 0.000 description 1
108010022452 Collagen Type I Proteins 0.000 description 1
102000002734 Collagen Type VI Human genes 0.000 description 1
108010043741 Collagen Type VI Proteins 0.000 description 1
108010069112 Complement System Proteins Proteins 0.000 description 1
102000000989 Complement System Proteins Human genes 0.000 description 1
101710180978 D-alanine aminotransferase Proteins 0.000 description 1
102000000541 Defensins Human genes 0.000 description 1
108010002069 Defensins Proteins 0.000 description 1
206010051392 Diapedesis Diseases 0.000 description 1
208000017850 Diffuse alveolar hemorrhage Diseases 0.000 description 1
239000006144 Dulbecco’s modiﬁed Eagle's medium Substances 0.000 description 1
238000012286 ELISA Assay Methods 0.000 description 1
206010014025 Ear swelling Diseases 0.000 description 1
241000223932 Eimeria tenella Species 0.000 description 1
101100491399 Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) apsB gene Proteins 0.000 description 1
108050009340 Endothelin Proteins 0.000 description 1
102000002045 Endothelin Human genes 0.000 description 1
102400000686 Endothelin-1 Human genes 0.000 description 1
101710121417 Envelope glycoprotein Proteins 0.000 description 1
101710126496 Envelope glycoprotein I Proteins 0.000 description 1
108090000790 Enzymes Proteins 0.000 description 1
102000004190 Enzymes Human genes 0.000 description 1
208000009386 Experimental Arthritis Diseases 0.000 description 1
108010074105 Factor Va Proteins 0.000 description 1
102000015212 Fas Ligand Protein Human genes 0.000 description 1
108010039471 Fas Ligand Protein Proteins 0.000 description 1
108010087819 Fc receptors Proteins 0.000 description 1
102000009109 Fc receptors Human genes 0.000 description 1
108010073385 Fibrin Proteins 0.000 description 1
102000009123 Fibrin Human genes 0.000 description 1
BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
102000003974 Fibroblast growth factor 2 Human genes 0.000 description 1
108090000379 Fibroblast growth factor 2 Proteins 0.000 description 1
208000024869 Goodpasture syndrome Diseases 0.000 description 1
102000002268 Hexosaminidases Human genes 0.000 description 1
108010000540 Hexosaminidases Proteins 0.000 description 1
101000797762 Homo sapiens C-C motif chemokine 5 Proteins 0.000 description 1
101000917839 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor III-B Proteins 0.000 description 1
101000946889 Homo sapiens Monocyte differentiation antigen CD14 Proteins 0.000 description 1
241000725303 Human immunodeficiency virus Species 0.000 description 1
108700002232 Immediate-Early Genes Proteins 0.000 description 1
102100025305 Integrin alpha-2 Human genes 0.000 description 1
102100022337 Integrin alpha-V Human genes 0.000 description 1
108010002350 Interleukin-2 Proteins 0.000 description 1
201000008225 Klebsiella pneumonia Diseases 0.000 description 1
241000588747 Klebsiella pneumoniae Species 0.000 description 1
240000007839 Kleinhovia hospita Species 0.000 description 1
102000007330 LDL Lipoproteins Human genes 0.000 description 1
108010007622 LDL Lipoproteins Proteins 0.000 description 1
101710098610 Leukocyte surface antigen CD47 Proteins 0.000 description 1
102100029185 Low affinity immunoglobulin gamma Fc region receptor III-B Human genes 0.000 description 1
102000002274 Matrix Metalloproteinases Human genes 0.000 description 1
108010000684 Matrix Metalloproteinases Proteins 0.000 description 1
102000012750 Membrane Glycoproteins Human genes 0.000 description 1
108010090054 Membrane Glycoproteins Proteins 0.000 description 1
102000005741 Metalloproteases Human genes 0.000 description 1
108010006035 Metalloproteases Proteins 0.000 description 1
102100035877 Monocyte differentiation antigen CD14 Human genes 0.000 description 1
241001529936 Murinae Species 0.000 description 1
101500025613 Mus musculus Transforming growth factor beta-1 Proteins 0.000 description 1
201000009053 Neurodermatitis Diseases 0.000 description 1
101100202932 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) tsp-4 gene Proteins 0.000 description 1
102400001060 Neutrophil defensin 2 Human genes 0.000 description 1
101800000287 Neutrophil defensin 2 Proteins 0.000 description 1
102100039306 Nucleotide pyrophosphatase Human genes 0.000 description 1
206010030113 Oedema Diseases 0.000 description 1
229940116355 PI3 kinase inhibitor Drugs 0.000 description 1
229910019142 PO4 Inorganic materials 0.000 description 1
206010034277 Pemphigoid Diseases 0.000 description 1
241000721454 Pemphigus Species 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
241000312117 Phago Species 0.000 description 1
102000003993 Phosphatidylinositol 3-kinases Human genes 0.000 description 1
108090000430 Phosphatidylinositol 3-kinases Proteins 0.000 description 1
108010004729 Phycoerythrin Proteins 0.000 description 1
102000010752 Plasminogen Inactivators Human genes 0.000 description 1
108010077971 Plasminogen Inactivators Proteins 0.000 description 1
241000223960 Plasmodium falciparum Species 0.000 description 1
102100031574 Platelet glycoprotein 4 Human genes 0.000 description 1
101710202087 Platelet glycoprotein 4 Proteins 0.000 description 1
102100036851 Platelet glycoprotein IX Human genes 0.000 description 1
101710191888 Platelet glycoprotein IX Proteins 0.000 description 1
241000233872 Pneumocystis carinii Species 0.000 description 1
206010035664 Pneumonia Diseases 0.000 description 1
206010035717 Pneumonia klebsiella Diseases 0.000 description 1
206010036590 Premature baby Diseases 0.000 description 1
208000012654 Primary biliary cholangitis Diseases 0.000 description 1
108010050808 Procollagen Proteins 0.000 description 1
229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
108010067787 Proteoglycans Proteins 0.000 description 1
102000016611 Proteoglycans Human genes 0.000 description 1
239000012979 RPMI medium Substances 0.000 description 1
101100208249 Rattus norvegicus Thbs4 gene Proteins 0.000 description 1
230000010799 Receptor Interactions Effects 0.000 description 1
102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
206010063837 Reperfusion injury Diseases 0.000 description 1
208000017442 Retinal disease Diseases 0.000 description 1
206010038923 Retinopathy Diseases 0.000 description 1
102000008847 Serpin Human genes 0.000 description 1
108050000761 Serpin Proteins 0.000 description 1
OUUQCZGPVNCOIJ-UHFFFAOYSA-M Superoxide Chemical compound [O-][O] OUUQCZGPVNCOIJ-UHFFFAOYSA-M 0.000 description 1
101800000483 Surface protein gp120 Proteins 0.000 description 1
108010079274 Thrombomodulin Proteins 0.000 description 1
102100026966 Thrombomodulin Human genes 0.000 description 1
206010052779 Transplant rejections Diseases 0.000 description 1
239000013504 Triton X-100 Substances 0.000 description 1
229920004890 Triton X-100 Polymers 0.000 description 1
108090000704 Tubulin Proteins 0.000 description 1
102100031988 Tumor necrosis factor ligand superfamily member 6 Human genes 0.000 description 1
108050002568 Tumor necrosis factor ligand superfamily member 6 Proteins 0.000 description 1
208000035896 Twin-reversed arterial perfusion sequence Diseases 0.000 description 1
206010067584 Type 1 diabetes mellitus Diseases 0.000 description 1
208000024248 Vascular System injury Diseases 0.000 description 1
208000012339 Vascular injury Diseases 0.000 description 1
108010048673 Vitronectin Receptors Proteins 0.000 description 1
230000001594 aberrant effect Effects 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
206010064930 age-related macular degeneration Diseases 0.000 description 1
230000032683 aging Effects 0.000 description 1
IXELFRRANAOWSF-CYBMUJFWSA-N ajoene Natural products C=CCSSC=CC[S@](=O)CC=C IXELFRRANAOWSF-CYBMUJFWSA-N 0.000 description 1
230000007815 allergy Effects 0.000 description 1
102000003801 alpha-2-Antiplasmin Human genes 0.000 description 1
108090000183 alpha-2-Antiplasmin Proteins 0.000 description 1
210000001132 alveolar macrophage Anatomy 0.000 description 1
230000008485 antagonism Effects 0.000 description 1
210000000436 anus Anatomy 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
108010072041 arginyl-glycyl-aspartic acid Proteins 0.000 description 1
238000003556 assay Methods 0.000 description 1
208000006673 asthma Diseases 0.000 description 1
230000003305 autocrine Effects 0.000 description 1
230000005784 autoimmunity Effects 0.000 description 1
230000001580 bacterial effect Effects 0.000 description 1
229960002890 beraprost Drugs 0.000 description 1
CTPOHARTNNSRSR-APJZLKAGSA-N beraprost Chemical compound O([C@H]1C[C@@H](O)[C@@H]([C@@H]21)/C=C/[C@@H](O)C(C)CC#CC)C1=C2C=CC=C1CCCC(O)=O CTPOHARTNNSRSR-APJZLKAGSA-N 0.000 description 1
HZZGDPLAJHVHSP-GKHTVLBPSA-N big endothelin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(O)=O)NC(=O)[C@H]1NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@H](C(C)C)NC(=O)[C@@H]2CSSC[C@@H](C(N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N2)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CSSC1)C1=CN=CN1 HZZGDPLAJHVHSP-GKHTVLBPSA-N 0.000 description 1
230000005540 biological transmission Effects 0.000 description 1
239000003130 blood coagulation factor inhibitor Substances 0.000 description 1
208000014759 blood platelet disease Diseases 0.000 description 1
210000001124 body fluid Anatomy 0.000 description 1
239000010839 body fluid Substances 0.000 description 1
150000001669 calcium Chemical class 0.000 description 1
229910052791 calcium Inorganic materials 0.000 description 1
230000009460 calcium influx Effects 0.000 description 1
239000004202 carbamide Substances 0.000 description 1
210000000170 cell membrane Anatomy 0.000 description 1
PRQROPMIIGLWRP-BZSNNMDCSA-N chemotactic peptide Chemical compound CSCC[C@H](NC=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 PRQROPMIIGLWRP-BZSNNMDCSA-N 0.000 description 1
230000035605 chemotaxis Effects 0.000 description 1
RQFQJYYMBWVMQG-IXDPLRRUSA-N chitotriose Chemical compound O[C@@H]1[C@@H](N)[C@H](O)O[C@H](CO)[C@H]1O[C@H]1[C@H](N)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)N)[C@@H](CO)O1 RQFQJYYMBWVMQG-IXDPLRRUSA-N 0.000 description 1
238000005660 chlorination reaction Methods 0.000 description 1
WLNARFZDISHUGS-MIXBDBMTSA-N cholesteryl hemisuccinate Chemical compound C1C=C2C[C@@H](OC(=O)CCC(O)=O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 WLNARFZDISHUGS-MIXBDBMTSA-N 0.000 description 1
208000037976 chronic inflammation Diseases 0.000 description 1
230000006020 chronic inflammation Effects 0.000 description 1
IXELFRRANAOWSF-UHFFFAOYSA-N cis-ajoene Natural products C=CCSSC=CCS(=O)CC=C IXELFRRANAOWSF-UHFFFAOYSA-N 0.000 description 1
229940096422 collagen type i Drugs 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
238000010668 complexation reaction Methods 0.000 description 1
208000018631 connective tissue disease Diseases 0.000 description 1
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
230000034994 death Effects 0.000 description 1
230000003247 decreasing effect Effects 0.000 description 1
238000000432 density-gradient centrifugation Methods 0.000 description 1
238000001514 detection method Methods 0.000 description 1
206010012601 diabetes mellitus Diseases 0.000 description 1
XEYBRNLFEZDVAW-ARSRFYASSA-N dinoprostone Chemical compound CCCCC[C@H](O)\C=C\[C@H]1[C@H](O)CC(=O)[C@@H]1C\C=C/CCCC(O)=O XEYBRNLFEZDVAW-ARSRFYASSA-N 0.000 description 1
229960002986 dinoprostone Drugs 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
230000008034 disappearance Effects 0.000 description 1
238000009826 distribution Methods 0.000 description 1
230000005584 early death Effects 0.000 description 1
210000005069 ears Anatomy 0.000 description 1
108010067341 ectonucleotide pyrophosphatase phosphodiesterase 1 Proteins 0.000 description 1
230000004528 endothelial cell apoptotic process Effects 0.000 description 1
210000000871 endothelium corneal Anatomy 0.000 description 1
229940088598 enzyme Drugs 0.000 description 1
210000000222 eosinocyte Anatomy 0.000 description 1
210000000981 epithelium Anatomy 0.000 description 1
210000003617 erythrocyte membrane Anatomy 0.000 description 1
210000001508 eye Anatomy 0.000 description 1
229950003499 fibrin Drugs 0.000 description 1
238000000684 flow cytometry Methods 0.000 description 1
239000012530 fluid Substances 0.000 description 1
230000004907 flux Effects 0.000 description 1
125000000524 functional group Chemical group 0.000 description 1
YFHXZQPUBCBNIP-UHFFFAOYSA-N fura-2 Chemical compound CC1=CC=C(N(CC(O)=O)CC(O)=O)C(OCCOC=2C(=CC=3OC(=CC=3C=2)C=2OC(=CN=2)C(O)=O)N(CC(O)=O)CC(O)=O)=C1 YFHXZQPUBCBNIP-UHFFFAOYSA-N 0.000 description 1
239000007789 gas Substances 0.000 description 1
108010074717 glycosaminoglycan receptor Proteins 0.000 description 1
230000013595 glycosylation Effects 0.000 description 1
238000006206 glycosylation reaction Methods 0.000 description 1
229960000789 guanidine hydrochloride Drugs 0.000 description 1
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
230000026030 halogenation Effects 0.000 description 1
238000005658 halogenation reaction Methods 0.000 description 1
230000035876 healing Effects 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
108010038082 heparin proteoglycan Proteins 0.000 description 1
230000013632 homeostatic process Effects 0.000 description 1
102000045341 human CCL5 Human genes 0.000 description 1
229940040731 human interleukin-12 Drugs 0.000 description 1
QWPPOHNGKGFGJK-UHFFFAOYSA-N hypochlorous acid Chemical compound ClO QWPPOHNGKGFGJK-UHFFFAOYSA-N 0.000 description 1
230000001900 immune effect Effects 0.000 description 1
230000028993 immune response Effects 0.000 description 1
229960003444 immunosuppressant agent Drugs 0.000 description 1
239000003018 immunosuppressive agent Substances 0.000 description 1
230000001771 impaired effect Effects 0.000 description 1
238000001727 in vivo Methods 0.000 description 1
230000002779 inactivation Effects 0.000 description 1
208000027866 inflammatory disease Diseases 0.000 description 1
230000028709 inflammatory response Effects 0.000 description 1
208000030603 inherited susceptibility to asthma Diseases 0.000 description 1
230000019734 interleukin-12 production Effects 0.000 description 1
230000009545 invasion Effects 0.000 description 1
238000002372 labelling Methods 0.000 description 1
239000004310 lactic acid Substances 0.000 description 1
235000014655 lactic acid Nutrition 0.000 description 1
231100000518 lethal Toxicity 0.000 description 1
230000001665 lethal effect Effects 0.000 description 1
231100000225 lethality Toxicity 0.000 description 1
238000011694 lewis rat Methods 0.000 description 1
239000003446 ligand Substances 0.000 description 1
230000000670 limiting effect Effects 0.000 description 1
210000004924 lung microvascular endothelial cell Anatomy 0.000 description 1
206010025135 lupus erythematosus Diseases 0.000 description 1
230000002934 lysing effect Effects 0.000 description 1
230000002132 lysosomal effect Effects 0.000 description 1
208000002780 macular degeneration Diseases 0.000 description 1
238000013507 mapping Methods 0.000 description 1
230000035800 maturation Effects 0.000 description 1
238000005259 measurement Methods 0.000 description 1
210000004379 membrane Anatomy 0.000 description 1
MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
230000003641 microbiacidal effect Effects 0.000 description 1
210000003632 microfilament Anatomy 0.000 description 1
210000004925 microvascular endothelial cell Anatomy 0.000 description 1
230000005012 migration Effects 0.000 description 1
238000013508 migration Methods 0.000 description 1
210000004980 monocyte derived macrophage Anatomy 0.000 description 1
210000000214 mouth Anatomy 0.000 description 1
230000035772 mutation Effects 0.000 description 1
208000010125 myocardial infarction Diseases 0.000 description 1
210000004897 n-terminal region Anatomy 0.000 description 1
230000001338 necrotic effect Effects 0.000 description 1
210000004498 neuroglial cell Anatomy 0.000 description 1
GRZXCHIIZXMEPJ-HTLKCAKFSA-N neutrophil peptide-2 Chemical compound C([C@H]1C(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@H](C(N[C@@H](C)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=4C=CC(O)=CC=4)NC(=O)[C@@H](N)CSSC[C@H](NC2=O)C(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](C)C(=O)N3)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](C)C(=O)N1)[C@@H](C)CC)[C@@H](C)O)=O)[C@@H](C)CC)C1=CC=CC=C1 GRZXCHIIZXMEPJ-HTLKCAKFSA-N 0.000 description 1
108010067588 nucleotide pyrophosphatase Proteins 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
230000008520 organization Effects 0.000 description 1
125000000636 p-nitrophenyl group Chemical group [H]C1=C([H])C(=C([H])C([H])=C1*)[N+]([O-])=O 0.000 description 1
230000003076 paracrine Effects 0.000 description 1
239000002245 particle Substances 0.000 description 1
230000008506 pathogenesis Effects 0.000 description 1
230000007310 pathophysiology Effects 0.000 description 1
230000037361 pathway Effects 0.000 description 1
239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
CMFNMSMUKZHDEY-UHFFFAOYSA-N peroxynitrous acid Chemical compound OON=O CMFNMSMUKZHDEY-UHFFFAOYSA-N 0.000 description 1
230000002085 persistent effect Effects 0.000 description 1
206010034754 petechiae Diseases 0.000 description 1
230000002399 phagocytotic effect Effects 0.000 description 1
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
239000010452 phosphate Substances 0.000 description 1
239000002935 phosphatidylinositol 3 kinase inhibitor Substances 0.000 description 1
230000026731 phosphorylation Effects 0.000 description 1
238000006366 phosphorylation reaction Methods 0.000 description 1
239000002797 plasminogen activator inhibitor Substances 0.000 description 1
231100000614 poison Toxicity 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
229920000136 polysorbate Polymers 0.000 description 1
239000011148 porous material Substances 0.000 description 1
230000014773 positive regulation of hemostasis Effects 0.000 description 1
230000002265 prevention Effects 0.000 description 1
230000007112 pro inflammatory response Effects 0.000 description 1
239000000047 product Substances 0.000 description 1
230000001737 promoting effect Effects 0.000 description 1
XEYBRNLFEZDVAW-UHFFFAOYSA-N prostaglandin E2 Natural products CCCCCC(O)C=CC1C(O)CC(=O)C1CC=CCCCC(O)=O XEYBRNLFEZDVAW-UHFFFAOYSA-N 0.000 description 1
230000001681 protective effect Effects 0.000 description 1
230000002797 proteolythic effect Effects 0.000 description 1
230000006337 proteolytic cleavage Effects 0.000 description 1
230000009467 reduction Effects 0.000 description 1
230000008929 regeneration Effects 0.000 description 1
238000011069 regeneration method Methods 0.000 description 1
238000011160 research Methods 0.000 description 1
230000004044 response Effects 0.000 description 1
210000001525 retina Anatomy 0.000 description 1
230000004263 retinal angiogenesis Effects 0.000 description 1
206010039073 rheumatoid arthritis Diseases 0.000 description 1
210000003296 saliva Anatomy 0.000 description 1
238000009738 saturating Methods 0.000 description 1
102000014452 scavenger receptors Human genes 0.000 description 1
108010078070 scavenger receptors Proteins 0.000 description 1
208000021043 septic peritonitis Diseases 0.000 description 1
238000012163 sequencing technique Methods 0.000 description 1
230000001568 sexual effect Effects 0.000 description 1
230000019491 signal transduction Effects 0.000 description 1
239000002356 single layer Substances 0.000 description 1
210000002027 skeletal muscle Anatomy 0.000 description 1
208000010110 spontaneous platelet aggregation Diseases 0.000 description 1
230000006641 stabilisation Effects 0.000 description 1
238000011105 stabilization Methods 0.000 description 1
230000000638 stimulation Effects 0.000 description 1
230000001629 suppression Effects 0.000 description 1
239000003440 toxic substance Substances 0.000 description 1
230000001960 triggered effect Effects 0.000 description 1
GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
101150060219 tsp-1 gene Proteins 0.000 description 1
210000004881 tumor cell Anatomy 0.000 description 1
229960005356 urokinase Drugs 0.000 description 1
210000001215 vagina Anatomy 0.000 description 1
108010047303 von Willebrand Factor Proteins 0.000 description 1
102100036537 von Willebrand factor Human genes 0.000 description 1
229960001134 von willebrand factor Drugs 0.000 description 1
238000005406 washing Methods 0.000 description 1
230000037314 wound repair Effects 0.000 description 1

Classifications

- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/55—Protease inhibitors
- A61K38/57—Protease inhibitors from animals; from humans
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/18—Antivirals for RNA viruses for HIV
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
- A61P33/02—Antiprotozoals, e.g. for leishmaniasis, trichomoniasis, toxoplasmosis
- A61P33/06—Antimalarials
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/02—Antineoplastic agents specific for leukemia
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/04—Antineoplastic agents specific for metastasis
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/08—Antiallergic agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/04—Antihaemorrhagics; Procoagulants; Haemostatic agents; Antifibrinolytic agents
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Veterinary Medicine (AREA)
Pharmacology & Pharmacy (AREA)
Chemical & Material Sciences (AREA)
Public Health (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Animal Behavior & Ethology (AREA)
General Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Chemical Kinetics & Catalysis (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Immunology (AREA)
Oncology (AREA)
Communicable Diseases (AREA)
Hematology (AREA)
Tropical Medicine & Parasitology (AREA)
Diabetes (AREA)
Virology (AREA)
Epidemiology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Gastroenterology & Hepatology (AREA)
Zoology (AREA)
Transplantation (AREA)
Pain & Pain Management (AREA)
Rheumatology (AREA)
AIDS & HIV (AREA)
Molecular Biology (AREA)
Pulmonology (AREA)
Neurosurgery (AREA)
Neurology (AREA)
Biomedical Technology (AREA)
Dermatology (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Peptides Or Proteins (AREA)
Medicinal Preparation (AREA)

ZA200302907A 2000-09-12 2003-04-14 Medicament containing activated antithrombin III. ZA200302907B (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
DE10045047A DE10045047A1 (de)	2000-09-12	2000-09-12	Arzneimittel enthaltend aktiviertes Antithrombin III

Publications (1)

Publication Number	Publication Date
ZA200302907B true ZA200302907B (en)	2003-09-15

Family

ID=7655909

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
ZA200302907A ZA200302907B (en)	2000-09-12	2003-04-14	Medicament containing activated antithrombin III.

Country Status (14)

Country	Link
US (2)	US7388075B2 (da)
EP (1)	EP1435985B1 (da)
JP (1)	JP5517387B2 (da)
AP (1)	AP2049A (da)
AT (1)	ATE359085T1 (da)
AU (2)	AU8987601A (da)
CY (1)	CY1106657T1 (da)
DE (2)	DE10045047A1 (da)
DK (1)	DK1435985T3 (da)
ES (1)	ES2283432T3 (da)
NZ (1)	NZ525292A (da)
PT (1)	PT1435985E (da)
WO (1)	WO2002022150A2 (da)
ZA (1)	ZA200302907B (da)

Families Citing this family (11)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE10051983A1 (de) *	2000-10-20	2002-06-13	Beate Kehrel	Inhibierung der pathogenen Wirkung oxidierter Proteine
AU2002215032A1 (en) *	2000-10-20	2002-04-29	Beate Kehrel	Inhibition of the interaction between oxidized proteins and cd36 or the active mechanism thereof
DE10102048A1 (de) *	2001-01-17	2002-07-18	Aventis Behring Gmbh	Antithrombin III gegen durch Angiogenese verursachte Krankheiten
NZ535487A (en) *	2002-04-01	2008-12-24	Univ Texas Medical Branch	Administration of ATIII by inhalation provides more efficient treatment of lung disorders such as lung inflammation and injury than intravenous administration
AU2003232209A1 (en) *	2003-04-25	2004-11-23	Hamburger Stiftung Zur Forderung Von Wissenschaft Und Kultur	Treatment of hi-virus infections with oxidised blood proteins
CA2664844A1 (en) *	2006-10-06	2008-10-23	Celtaxsys, Inc.	Chemorepulsion of cells
JP2010235447A (ja) *	2007-07-30	2010-10-21	Igaku Seibutsugaku Kenkyusho:Kk	炎症性サイトカインの抑制剤
DE102011003936A1 (de)	2011-02-10	2012-08-16	Oxprotect Gmbh	Verwendung von Proteinen/Peptiden, welche an GRP78 (BIP) binden, in Labormethoden zum Monitoring von Thrombozyten-Aggregationshemmern
AR094778A1 (es)	2013-02-13	2015-08-26	Laboratoire Français Du Fractionnement Et Des Biotechnologies	Proteínas con glicosilación modificada y métodos para producirlas
WO2017149391A1 (en) *	2016-03-02	2017-09-08	Laboratoire Francais Du Fractionnement Et Des Biotechnologies	The use of antithrombin for coating organs during transplantation
EP4311556A1 (en) *	2022-07-28	2024-01-31	Grifols Worldwide Operations Limited	Antithrombin in stroke

Family Cites Families (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JP2739050B2 (ja) *	1988-01-28	1998-04-08	ヘキスト薬品工業株式会社	抗血液凝固剤
DE4311580C1 (de)	1993-04-12	1994-08-18	Werner Prof Dr Med Reutter	Glycoproteine, Verfahren zu ihrer Herstellung und sie enthaltende pharmazeutische Mittel
JP3820607B2 (ja)	1995-11-10	2006-09-13	三菱ウェルファーマ株式会社	アンチトロンビン−ｉｉｉの液状製剤およびその保存安定化方法
US6686303B1 (en) *	1998-11-13	2004-02-03	Kimberly-Clark Worldwide, Inc.	Bicomponent nonwoven webs containing splittable thermoplastic filaments and a third component
DE19852729A1 (de) *	1998-11-16	2000-05-18	Werner Reutter	Rekombinante Glycoproteine, Verfahren zu ihrer Herstellung, sie enthaltende Arzneimittel und ihre Verwendung
EP1027894A3 (en) *	1999-01-28	2001-01-24	Aventis Behring Gesellschaft mit beschränkter Haftung	Pharmaceutical preparation for the treatment of inflammatory processes
WO2002058638A2 (en)	2001-01-26	2002-08-01	The General Hospital Corporation	Serpin drugs for treatment of hiv infection and method of use thereof

2000
- 2000-09-12 DE DE10045047A patent/DE10045047A1/de not_active Ceased
2001
- 2001-09-12 JP JP2002526400A patent/JP5517387B2/ja not_active Expired - Fee Related
- 2001-09-12 EP EP01969710A patent/EP1435985B1/de not_active Expired - Lifetime
- 2001-09-12 ES ES01969710T patent/ES2283432T3/es not_active Expired - Lifetime
- 2001-09-12 AU AU8987601A patent/AU8987601A/xx active Pending
- 2001-09-12 AU AU2001289876A patent/AU2001289876B2/en not_active Ceased
- 2001-09-12 AP APAP/P/2003/002783A patent/AP2049A/en active
- 2001-09-12 DK DK01969710T patent/DK1435985T3/da active
- 2001-09-12 NZ NZ525292A patent/NZ525292A/en not_active IP Right Cessation
- 2001-09-12 AT AT01969710T patent/ATE359085T1/de active
- 2001-09-12 PT PT01969710T patent/PT1435985E/pt unknown
- 2001-09-12 US US10/380,274 patent/US7388075B2/en not_active Expired - Fee Related
- 2001-09-12 DE DE50112350T patent/DE50112350D1/de not_active Expired - Lifetime
- 2001-09-12 WO PCT/EP2001/010541 patent/WO2002022150A2/de active IP Right Grant
2003
- 2003-04-14 ZA ZA200302907A patent/ZA200302907B/en unknown
2007
- 2007-06-14 CY CY20071100791T patent/CY1106657T1/el unknown
2008
- 2008-06-11 US US12/137,239 patent/US8114840B2/en not_active Expired - Fee Related

Also Published As

Publication number	Publication date
AU2001289876B2 (en)	2006-09-07
JP5517387B2 (ja)	2014-06-11
ATE359085T1 (de)	2007-05-15
AP2003002783A0 (en)	2003-06-30
WO2002022150A2 (de)	2002-03-21
WO2002022150A3 (de)	2004-05-06
ES2283432T3 (es)	2007-11-01
AU8987601A (en)	2002-03-26
JP2004518625A (ja)	2004-06-24
US20040029799A1 (en)	2004-02-12
US20090036360A1 (en)	2009-02-05
US8114840B2 (en)	2012-02-14
EP1435985B1 (de)	2007-04-11
PT1435985E (pt)	2007-07-11
DE50112350D1 (de)	2007-05-24
CY1106657T1 (el)	2012-01-25
DE10045047A1 (de)	2002-03-21
EP1435985A2 (de)	2004-07-14
AP2049A (en)	2009-09-25
NZ525292A (en)	2005-08-26
DK1435985T3 (da)	2007-08-20
US7388075B2 (en)	2008-06-17

Publication	Publication Date	Title
US8114840B2 (en)	2012-02-14	Medicament containing activated antithrombin III
Opal et al.	2002	Bench-to-bedside review: functional relationships between coagulation and the innate immune response and their respective roles in the pathogenesis of sepsis
Mammen	1998	Antithrombin: its physiological importance and role in DIC
US20190161746A1 (en)	2019-05-30	Adamts13-containing compositions having thrombolytic activity
US8715672B2 (en)	2014-05-06	Treatment of diseases linked to pathological kinin formation
de Jonge et al.	1998	Current drug treatment strategies for disseminated intravascular coagulation
JP2006008704A (ja)	2006-01-12	組織因子経路インヒビター（ｔｆｐｉ）の低量投与による敗血症の処置
Morris et al.	1994	Thrombin in inflammation and healing: relevance to rheumatoid arthritis.
US20060252692A1 (en)	2006-11-09	Inhibitors for use in hemostasis
CA2139353C (en)	2006-11-07	Pharmaceutical composition containing il-6, their uses for the treatment of consumptive thrombo-hemorrhagic disorder
Nellenbach et al.	2017	Peptide mimetic drugs for modulating thrombosis and hemostasis
CA2124161C (en)	2008-11-18	Pharmaceuticals for treating sepsis and septic shock
KR20010006592A (ko)	2001-01-26	염증성 질환 치료용 약제학적 조성물
Gao et al.	2021	Multiple roles of histidine-rich glycoprotein in vascular homeostasis and angiogenesis
Chavakis et al.	2003	Potential pharmacological applications of the antithrombotic molecule high molecular weight kininogen
WO2002022112A2 (en)	2002-03-21	Pharmaceutical composition for preventing or treating a disease associated with an excess of il-12 production
Tervo et al.	1992	Experience with plasmin inhibitors
CA2312824A1 (en)	1999-06-10	Use of a fibrinogen receptor-antagonist for preventing disseminated intravascular coagulation
CN110051830A (zh)	2019-07-26	一种protease nexin II\KPI蛋白突变体的应用
Ricou	1996	A broader view of ARDS
AU2007202500A1 (en)	2007-06-21	Treatment of sepsis by low dose administration of tissue factor pathway inhibitor (TFPI)