WO2002036619A1 - Nouveau polypeptide, glucoproteine humaine 42, et polynucleotide codant ce polypeptide - Google Patents

Nouveau polypeptide, glucoproteine humaine 42, et polynucleotide codant ce polypeptide Download PDF

Info

Publication number
WO2002036619A1
WO2002036619A1 PCT/CN2001/001524 CN0101524W WO0236619A1 WO 2002036619 A1 WO2002036619 A1 WO 2002036619A1 CN 0101524 W CN0101524 W CN 0101524W WO 0236619 A1 WO0236619 A1 WO 0236619A1
Authority
WO
WIPO (PCT)
Prior art keywords
polypeptide
polynucleotide
human glycoprotein
sequence
seq
Prior art date
Application number
PCT/CN2001/001524
Other languages
English (en)
Chinese (zh)
Inventor
Yumin Mao
Yi Xie
Original Assignee
Shanghai Biowindow Gene Development Inc.
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.)
Filing date
Publication date
Application filed by Shanghai Biowindow Gene Development Inc. filed Critical Shanghai Biowindow Gene Development Inc.
Priority to AU2002221460A priority Critical patent/AU2002221460A1/en
Publication of WO2002036619A1 publication Critical patent/WO2002036619A1/fr

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
    • C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
    • 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
    • A61P37/00—Drugs for immunological or allergic disorders
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides

Definitions

  • polypeptide of the present invention was inferred and identified as a new human glycoprotein 42 (HGP42).
  • the present invention provides a new polypeptide, human glycoprotein 42, which basically consists of the amino acid sequence shown in SEQ ID NO: 2.
  • the polypeptide of the present invention may be a recombinant polypeptide, a natural polypeptide, or a synthetic polypeptide, and preferably a recombinant polypeptide.
  • the polypeptides of the present invention may be naturally purified products or chemically synthesized products, or produced using recombinant techniques from prokaryotic or eukaryotic hosts (e.g., bacteria, yeast, higher plants, insects, and mammalian cells). Depending on the host used in the recombinant production protocol, the polypeptide of the invention may be glycosylated, or it may be non-glycosylated. Polypeptides of the invention may also include or exclude starting methionine residues.
  • the invention also includes fragments, derivatives and analogs of human glycoprotein 42.
  • fragment refers to a polypeptide that substantially maintains the same biological function or activity of the human glycoprotein 42 of the present invention.
  • the polynucleotide encoding the mature polypeptide of SEQ ID NO: 2 includes: only the coding sequence of the mature polypeptide; the coding sequence of the mature polypeptide and various additional coding sequences; the coding sequence of the mature polypeptide (and optional additional coding sequences); Coding sequence.
  • polynucleotide encoding a polypeptide refers to a polynucleotide comprising the polypeptide and a polynucleotide comprising additional coding and / or non-coding sequences.
  • the present invention also relates to a polynucleotide that hybridizes to the sequence described above (having at least 50%, preferably 70% identity, between the two sequences).
  • the present invention particularly relates to polynucleotides that can hybridize to the polynucleotides of the present invention under stringent conditions.
  • “strict conditions” means: (1) hybridization and elution at lower ionic strength and higher temperature, such as 0.2xSSC, 0.1 ° / »SDS, 60 ° C; or ( 2) Add a denaturant during hybridization, such as 50% (v / v) formamide, 0.1% calf serum / 0.1% F i co ll, 42 ° C, etc .; or (3) only in two Sequences do not hybridize until they have at least 95% identity, and more preferably 97% or more.
  • the polypeptide encoded by the hybridizable polynucleotide has the same biological function and activity as the mature polypeptide shown in SEQ ID NO: 2.
  • a method (Saiki, et al. Science 1985; 230: 1350-1354) using PCR technology to amplify DNA / RNA is preferably used to obtain the gene of the present invention.
  • the RACE method RACE-Rapid Amplification of cDNA Ends
  • the primers used for PCR can be appropriately based on the polynucleotide sequence information of the present invention disclosed herein.
  • the amplified DNA / RNA fragments can be isolated and purified by conventional methods such as by gel electrophoresis.
  • polynucleotide sequence of the gene of the present invention or various DNA fragments and the like obtained as described above can be measured by a conventional method such as dideoxy chain termination method (Sanger et al. PNAS, 1977, 74: 5463-5467). Such polynucleotide sequences can also be determined using commercial sequencing kits and the like. In order to obtain the full-length cDNA sequence, sequencing must be repeated. Sometimes it is necessary to determine the cDNA sequence of multiple clones in order to splice into a full-length cDNA sequence.
  • a polynucleotide sequence encoding human glycoprotein 42 may be inserted into a vector to constitute a recombinant vector containing the polynucleotide of the present invention.
  • vector refers to bacterial plasmids, phages, yeast plasmids, plant cell viruses, mammalian cell viruses such as adenoviruses, retroviruses, or other vectors well known in the art.
  • Vectors suitable for use in the present invention include, but are not limited to: T7 promoter-based expression vectors (Rosenberg, et al.
  • DM sequence can be operably linked to an appropriate promoter in an expression vector to guide mRM synthesis.
  • promoters are: the lac or trp promoter of E.
  • Escherichia coli, Streptomyces bacterial cells such as Salmonella typhimurium
  • fungal cells such as yeast
  • plant cells insect cells
  • fly S2 or Sf 9 animal cells
  • animal cells such as CH0, COS or Bowes melanoma cells.
  • the medium used in the culture may be selected from various conventional mediums. Culture is performed under conditions suitable for host cell growth. After the host cells have grown to an appropriate cell density, the selected promoter is induced by a suitable method (such as temperature conversion or chemical induction), and the cells are cultured for a period of time.
  • a suitable method such as temperature conversion or chemical induction
  • polypeptides of the present invention as well as antagonists, agonists and inhibitors of the polypeptides, can be directly used in the treatment of diseases, for example, they can treat malignant tumors, adrenal deficiency, skin diseases, various types of inflammation, HIV infection, and immune diseases.
  • polypeptides of the present invention have important roles in the catalysis of reactions, the transmission of molecules inside and outside the membrane, the reception and transmission of intracellular signals, the membrane localization of enzyme substrates, and tissue identification marks, etc., so they can be directly used as drugs or vaccines for many Diagnosis and treatment of diseases, such as human acquired immune deficiency syndrome (AIDS), malignant tumors, immune diseases, endocrine system diseases, neurological diseases, etc.
  • diseases such as human acquired immune deficiency syndrome (AIDS), malignant tumors, immune diseases, endocrine system diseases, neurological diseases, etc.
  • Antibodies to the polypeptides of the present invention can act on malignant diseases, including leukemias and lymphomas; sarcomas of epithelial cell origin; tumors of interstitial origin, such as sarcomas; tumors of the central nervous system and the like.
  • the polypeptides and antibodies of the present invention also have effects on damage, defects or disorders of immune tissues, especially for hematopoietic diseases (such as malignant anemia), skin diseases (such as psoriasis), and autoimmune diseases (such as rheumatoid arthritis ), Radiation diseases and the production and regulation of immune lymphocytes are extremely closely related.
  • hematopoietic diseases such as malignant anemia
  • skin diseases such as psoriasis
  • autoimmune diseases such as rheumatoid arthritis
  • the invention also provides methods for screening compounds to identify agents that increase (agonist) or suppress (antagonist) human glycoprotein 42.
  • Agonists enhance biological functions such as human glycoprotein 42 to stimulate cell proliferation, while antagonists prevent and treat disorders related to excessive cell proliferation, such as various cancers.
  • mammalian cells or membrane preparations expressing human glycoprotein 42 can be cultured together with labeled human glycoprotein 42 in the presence of drugs. The ability of the drug to increase or block this interaction is then determined.
  • Antagonists of human glycoprotein 42 include antibodies, compounds, receptor deletions, and the like that have been screened. Antagonists of human glycoprotein 42 can bind to human glycoprotein 42 and eliminate its function, or inhibit the production of the polypeptide, or bind to the active site of the polypeptide so that the polypeptide cannot perform biological functions.
  • human glycoprotein 42 When screening compounds as antagonists, human glycoprotein 42 can be added to a bioanalytical assay to determine whether a compound is an antagonist by measuring the effect of the compound on the interaction between human glycoprotein 42 and its receptor. Receptor deletions and analogs that act as antagonists can be screened in the same manner as described above for screening compounds.
  • Polypeptide molecules capable of binding to human glycoprotein 42 can be obtained by screening a random peptide library composed of various possible combinations of amino acids bound to a solid phase. In screening, the molecule 42 of human glycoprotein should generally be labeled.
  • the present invention provides a method for producing an antibody using a polypeptide, a fragment, a derivative, an analog thereof, or a cell thereof as an antigen.
  • These antibodies can be polyclonal or monoclonal antibodies.
  • the invention also provides antibodies against human glycoprotein 42 epitopes. These antibodies include (but are not limited to): polyclonal antibodies, monoclonal antibodies, chimeric antibodies, single chain antibodies, Fab fragments, and fragments produced by Fab expression libraries.
  • Polyclonal antibodies can be produced by injecting human glycoprotein 42 directly into immunized animals (such as rabbits, mice, rats, etc.).
  • a variety of adjuvants can be used to enhance the immune response, including but not limited to Freund's adjuvant.
  • Techniques for preparing monoclonal antibodies to human glycoprotein 42 include, but are not limited to, hybridoma technology (Kohl er and Miste in. Nature, 1975, 256: 495-497), triple tumor technology, human B-cell hybridoma technology, EBV-hybridoma technology, etc.
  • Chimeric antibodies that bind human constant regions to non-human-derived variable regions can be produced using existing techniques (Morrison et al, PNAS, 1985, 81: 6851).
  • the existing technology for producing single chain antibodies (U.S. Pat No. 4946778) can also be used to produce single chain antibodies against human glycoprotein 42.
  • Anti-human glycoprotein 42 antibodies can be used in immunohistochemical techniques to detect human glycoprotein 42 in biopsy specimens.
  • Monoclonal antibodies that bind to human glycoprotein 42 can also be labeled with radioisotopes and injected into the body to track their location and distribution. This radiolabeled antibody can be used as a non-invasive diagnostic method to locate tumor cells and determine whether there is metastasis.
  • Antibodies can also be used to design immunotoxins against a specific bead site in the body.
  • human glycoprotein 42 high affinity monoclonal antibodies can covalently bind to bacterial or plant toxins (such as diphtheria toxin, ricin, ormosine, etc.).
  • a common method is to attack the amino group of the antibody with a thiol crosslinker such as SPDP, and toxin is bound to the antibody through the exchange of disulfide bonds.
  • This hybrid antibody can be used to kill human glycoprotein 42 positive cells.
  • the antibodies of the present invention can be used to treat or prevent diseases related to human glycoprotein 42. Administration of an appropriate dose of the antibody can stimulate or block the production or activity of human glycoprotein 42.
  • the invention also relates to a diagnostic test method for quantitative and localized detection of human glycoprotein 42 levels.
  • tests are well known in the art and include FISH assays and radioimmunoassays.
  • the level of human glycoprotein 42 detected in the test can be used to explain the importance of human glycoprotein 42 in various diseases and to diagnose diseases in which human glycoprotein 42 plays a role.
  • polypeptide of the present invention can also be used for peptide mapping analysis.
  • the polypeptide can be specifically cleaved by physical, chemical or enzymatic analysis, and subjected to one-dimensional or two-dimensional or three-dimensional gel electrophoresis analysis, and more preferably mass spectrometry analysis.
  • Polynucleotides encoding human glycoprotein 42 can also be used for a variety of therapeutic purposes. Gene therapy technology can be used to treat abnormal cell proliferation, development or metabolism caused by the non-expression or abnormal / inactive expression of human glycoprotein 42.
  • Recombinant gene therapy vectors (such as viral vectors) can be designed to express mutated human glycoprotein 42 to inhibit endogenous human glycoprotein 42 activity.
  • a mutated human glycoprotein 42 may be a shortened human glycoprotein 42 lacking a signaling domain, and although it can bind to downstream substrates, it lacks signaling activity. Therefore, recombinant gene therapy vectors can be used to treat human glycoprotein 42 expression or Disease caused by abnormal activity.
  • Virus-derived expression vectors such as retrovirus, adenovirus, adenovirus-associated virus, herpes simplex virus, parvovirus, etc. can be used to transfer a polynucleotide encoding human glycoprotein 42 into a cell.
  • a method for constructing a recombinant viral vector carrying a polynucleotide encoding human glycoprotein 42 can be found in the existing literature (Sambrook, et al.).
  • a recombinant polynucleotide encoding human glycoprotein 42 can be packaged into liposomes and transferred into cells.
  • Methods for introducing a polynucleotide into a tissue or cell include: directly injecting the polynucleotide into a tissue in vivo; or introducing the polynucleotide into a cell in vitro through a vector (such as a virus, phage, or plasmid), and then transplanting the cell Into the body and so on.
  • a vector such as a virus, phage, or plasmid
  • Oligonucleotides including antisense RNA and DNA
  • ribozymes that inhibit human glycoprotein 42 mRNA are also within the scope of the present invention.
  • a ribozyme is an enzyme-like RNA molecule that can specifically decompose specific RNA. Its mechanism of action is that the ribozyme molecule specifically hybridizes with a complementary target RNA and performs endonucleation.
  • Antisense RNA, DNA, and ribozymes can be obtained using any existing RNA or DNA synthesis techniques, such as solid-phase phosphate amide chemical synthesis to synthesize oligonucleotides.
  • Antisense RNA molecules can be obtained by in vitro or in vivo transcription of a DNA sequence encoding the MA.
  • This DM sequence has been integrated downstream of the RNA polymerase promoter of the vector.
  • it can be modified in a variety of ways, such as increasing the sequence length on both sides, and the phosphorothioate or peptide bond instead of the phosphodiester bond is used for the ribonucleoside linkage.
  • the polynucleotide encoding human glycoprotein 42 can be used for the diagnosis of diseases related to human glycoprotein 42.
  • the polynucleotide encoding human glycoprotein 42 can be used to detect the expression of human glycoprotein 42 or the abnormal expression of human glycoprotein 42 in a disease state.
  • a DNA sequence encoding human glycoprotein 42 can be used to hybridize biopsy specimens to determine the expression of human glycoprotein 42.
  • Hybridization techniques include Southern blotting, Nor thern blotting, and in situ hybridization. These techniques and methods are publicly available and mature, and the relevant kits are commercially available.
  • polynucleotides of the present invention can be used as probes to be fixed on a micro array (Mi croar ray) or a DNA chip (also known as a "gene chip") for analyzing differential expression analysis of genes and genetic diagnosis in tissues .
  • Human glycoprotein 42 specific primers can also be used to detect human glycoprotein 42 transcripts by in vitro amplification of RNA-polymerase chain reaction (RT-PCR).
  • Detection of mutations in the human glycoprotein 42 gene can also be used to diagnose human glycoprotein 42-related diseases.
  • Human glycoprotein 42 mutations include point mutations, translocations, deletions, recombinations, and any other abnormalities compared to the normal wild-type human glycoprotein 42 DNA sequence. Mutations can be detected using existing techniques such as Southern blotting, DNA sequence analysis, PCR and in situ hybridization. In addition, mutations may affect protein expression. Therefore, the Nor thern blotting and Western blotting can be used to indirectly determine whether a gene is mutated.
  • sequences of the invention are also valuable for chromosome identification. This sequence will specifically target a specific position on a human chromosome and can hybridize to it. At present, the specificity of each gene on the chromosome needs to be identified Site. Currently, only a few chromosome markers based on actual sequence data (repeating polymorphisms) are available for labeling chromosome positions. According to the present invention, in order to associate these sequences with disease-related genes, an important first step is to locate these DNA sequences on a chromosome.
  • PCR primers (preferably 15-35bp) are prepared from the cDNA, and the sequences can be located on the chromosomes. These primers were then used for PCR screening of somatic hybrid cells containing individual human chromosomes. Only those heterozygous cells containing the human gene corresponding to the primer will produce amplified fragments.
  • PCR localization of somatic hybrid cells is a quick way to localize DM to specific chromosomes.
  • oligonucleotide primers of the present invention in a similar manner, a set of fragments from a specific chromosome or a large number of genomic clones can be used to achieve sublocalization.
  • Other similar strategies that can be used for chromosomal localization include in situ hybridization, chromosome pre-screening with labeled flow sorting, and hybrid pre-selection to construct chromosome-specific cDM libraries.
  • Fluorescent in situ hybridization of cDNA clones with metaphase chromosomes allows precise chromosomal localization in one step.
  • FISH Fluorescent in situ hybridization
  • the difference in cDNA or genomic sequence between the affected and unaffected individuals needs to be determined. If a mutation is observed in some or all diseased individuals and the mutation is not observed in any normal individuals, the mutation may be the cause of the disease. Comparing affected and unaffected individuals usually involves first looking for structural changes in chromosomes, such as deletions or translocations that are visible at the chromosomal level or detectable with cDNA sequence-based PCR. According to the resolution capabilities of current physical mapping and gene mapping technology, the cDNA accurately mapped to the chromosomal region associated with the disease can be one of 50 to 500 potentially pathogenic genes (assuming 1 megabase mapping resolution) Capacity and each 20kb corresponds to a gene).
  • the polypeptides, polynucleotides and mimetics, agonists, antagonists and inhibitors of the present invention can be used in combination with a suitable pharmaceutical carrier.
  • suitable pharmaceutical carrier can be water, glucose, ethanol, salts, buffers, glycerol, and combinations thereof.
  • the composition comprises a safe and effective amount of the polypeptide or antagonist, and carriers and excipients which do not affect the effect of the drug. These compositions can be used as drugs for the treatment of diseases.
  • the present invention also provides a kit or kit containing one or more containers containing one or more ingredients of the pharmaceutical composition of the present invention.
  • containers there can be medicines manufactured, used or sold by Instructions given by the government regulatory agency for the product or biological product, which reflects the permission of the government regulatory agency for production, use, or sale to be administered to the human body.
  • the polypeptides of the invention can be used in combination with other therapeutic compounds.
  • the pharmaceutical composition can be administered in a convenient manner, such as by a topical, intravenous, intraperitoneal, intramuscular, subcutaneous, intranasal or intradermal route of administration.
  • Human glycoprotein 42 is administered in an amount effective to treat and / or prevent a particular indication.
  • the amount and dose range of human glycoprotein 42 to be administered to a patient will depend on many factors, such as the mode of administration, the health conditions of the person to be treated, and the judgment of the diagnostician. Examples
  • RNA Human fetal brain total RNA was extracted by one-step method with guanidine isothiocyanate / phenol / chloroform.
  • Poly (A) mRNA was isolated from total RNA using Quik raRNA Isolat ion Kit (product of Qiegene). 2ug poly (A) mRNA is reverse transcribed to form cDNA. Use Smart cDNA Cloning Kit (purchased from Clontech). The 0 fragment was inserted into the multiple cloning site of pBSK (+) vector (Clontech), and transformed into DH5a. The bacteria formed a cDNA library.
  • Dye terminate cycle reaction ion sequencing kit Perkin-Elmer
  • ABI 377 automatic sequencer Perkin-Elmer
  • the determined cDNA sequence was compared with the existing public A sequence database (Genebank), and it was found that the cDNA sequence of one of the clones 0437B10 was a new DM.
  • the inserted cDNA fragments contained in this clone were determined in both directions by synthesizing a series of primers.
  • CD was synthesized by reverse transcription reaction using total RNA from fetal brain cells as a template and ol igo-dT as a primer. After purification with Qiagene's kit, PCR was performed using the following primers:
  • Primer 1 5 a GGCGCTGGGGAACTCTGGCCTCGCTGCAC -3, (SEQ ID NO: 3)
  • Pr imer2 5,-TGGTATGTTTTTAAATTCTGAAAATTAACTG-3, (SEQ ID NO: 4)
  • Primerl is located at the 5th end of SEQ ID NO: 1, starting from the lbp of the end Forward sequence;
  • Pr imer2 is the 3, terminal reverse sequence of SEQ ID NO: 1.
  • Amplification reaction conditions 50 ⁇ l / L KCl, 10 mmol / L Tri s-HCl pH 8.50, 1.5 mmol / L MgCl 2 , 20 ⁇ / L dNTP, lOpmol primer, 1U in a 50 ⁇ 1 reaction volume Taq DNA polymerase (Clontech).
  • the reaction was performed on a PE9600 DM thermal cycler (Perkin-Elmer) under the following conditions for 25 cycles: 94 ° C 30sec; 55 ° C 30sec; 72 ° C 2min.
  • RT-PCR set ⁇ -act in as a positive control and template blank as a negative control.
  • Primer3 5'- GGATGAAGGGTCGTTGGTGGGAAA -3, (Seq ID No: 5)
  • the 5 'ends of these two primers contain BamHI and Xhol restriction sites, respectively, followed by the coding sequences of the 5' and 3 'ends of the target gene, respectively.
  • the BamHI and Xhol restriction sites correspond to the expression vector plasmid pET-28b ( +) (Novagen, Cat. No. 69865. 3) selective endonuclease site.
  • the PCR reaction was performed using the PBS-0437B10 plasmid containing the full-length target gene as a template.
  • the PCR reaction conditions were as follows: a total volume of 50 ⁇ 1 containing 10 pg of pBS-0437B10 plasmid, primers Primer-3 and Primer-4 were 1 Opmol, Advantage polymerase Mix (Clontech) 1 ⁇ 1, respectively. Cycle parameters: 94. C 20s, 60 ° C 30s, 68 ° C 2 min, a total of 25 cycles.
  • the amplified product and plasmid pET-28 (+) were digested with BamHI and Xhol, respectively, and large fragments were recovered and ligated with T4 ligase.
  • the ligated product was transformed into E. coli DH5 CC using the calcium chloride method.
  • NH2-Met-A 1 aA 1 a-Thr-Leu-G 1 y-Pro-Leu-G 1 y-Ser-Trp-G 1 nG 1 n-Trp-Arg-OH SEQ ID NO: 7
  • the polypeptide is coupled with hemocyanin and bovine serum albumin to form a complex, respectively.
  • hemocyanin and bovine serum albumin For methods, see: Avrameas, et al. Ilan unochemistry, 1969; 6: 43. Rabbits were immunized with 4 mg of the hemocyanin polypeptide complex plus complete Freund's adjuvant, and 15 days later, the hemocyanin polypeptide complex plus incomplete Freund's adjuvant was used to boost immunity once.
  • a titer plate coated with a 15 g / ml bovine serum albumin peptide complex was used as an ELISA to determine antibody titers in rabbit serum.
  • Total IgG was isolated from antibody-positive rabbit serum using protein A-Sepharose.
  • the peptide was bound to a cyanogen bromide-activated Se P harose 4B column, and anti-peptide antibodies were separated from the total IgG by affinity chromatography.
  • the immunoprecipitation method proved that the purified antibody could specifically bind to human glycoprotein 42.

Abstract

L'invention concerne un nouveau polypeptide, une glucoprotéine humaine 42, et un polynucléotide codant ce polypeptide ainsi qu'un procédé d'obtention de ce polypeptide par des techniques recombinantes d'ADN. L'invention concerne en outre les applications de ce polypeptide dans le traitement de maladies, notamment des tumeurs malignes, de l'hémopathie, de l'infection par VIH, de maladies immunitaires et de diverses inflammations. L'invention concerne aussi l'antagoniste agissant contre le polypeptide et son action thérapeutique ainsi que les applications de ce polynucléotide codant la glucoprotéine humaine 42.
PCT/CN2001/001524 2000-11-02 2001-11-01 Nouveau polypeptide, glucoproteine humaine 42, et polynucleotide codant ce polypeptide WO2002036619A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
AU2002221460A AU2002221460A1 (en) 2000-11-02 2001-11-01 A new polypeptide-human glycoprotein 42 and the polynucleotide encoding it

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
CN00127195.4 2000-11-02
CN00127195A CN1352087A (zh) 2000-11-02 2000-11-02 一种新的多肽——人糖蛋白42和编码这种多肽的多核苷酸

Publications (1)

Publication Number Publication Date
WO2002036619A1 true WO2002036619A1 (fr) 2002-05-10

Family

ID=4592214

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/CN2001/001524 WO2002036619A1 (fr) 2000-11-02 2001-11-01 Nouveau polypeptide, glucoproteine humaine 42, et polynucleotide codant ce polypeptide

Country Status (3)

Country Link
CN (1) CN1352087A (fr)
AU (1) AU2002221460A1 (fr)
WO (1) WO2002036619A1 (fr)

Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1990010651A1 (fr) * 1989-03-10 1990-09-20 Snow Brand Milk Products Co., Ltd. Glycoproteine humaine, facteur physiologiquement actif la contenant, et preparation pharmaceutique le contenant en tant qu'ingredient actif
JPH06205677A (ja) * 1991-06-18 1994-07-26 Nippon Koutai Kenkyusho:Kk 糖タンパク質１０遺伝子
EP0632055A1 (fr) * 1988-12-27 1995-01-04 Mochida Pharmaceutical Co., Ltd. Substance anticoagulante obtenue de l'urine
WO1995006727A2 (fr) * 1993-09-03 1995-03-09 Immulogic Pharmaceutical Corporation Utilisations de la glycoproteine de myeline d'oligodendrocytes et de portions peptidiques derivees de celle-ci dans des protocoles ayant trait a des maladies auto-immunes
WO1997040149A1 (fr) * 1996-04-18 1997-10-30 Akzo Nobel N.V. Auto-antigene et proteines lies de maniere structurelle et leur utilisation dans l'immunotherapie des maladies auto-immunes
WO1999053056A1 (fr) * 1998-04-10 1999-10-21 Snow Brand Milk Products Co., Ltd. Nouvelle proteine et ses procedes de production

Patent Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0632055A1 (fr) * 1988-12-27 1995-01-04 Mochida Pharmaceutical Co., Ltd. Substance anticoagulante obtenue de l'urine
WO1990010651A1 (fr) * 1989-03-10 1990-09-20 Snow Brand Milk Products Co., Ltd. Glycoproteine humaine, facteur physiologiquement actif la contenant, et preparation pharmaceutique le contenant en tant qu'ingredient actif
JPH06205677A (ja) * 1991-06-18 1994-07-26 Nippon Koutai Kenkyusho:Kk 糖タンパク質１０遺伝子
WO1995006727A2 (fr) * 1993-09-03 1995-03-09 Immulogic Pharmaceutical Corporation Utilisations de la glycoproteine de myeline d'oligodendrocytes et de portions peptidiques derivees de celle-ci dans des protocoles ayant trait a des maladies auto-immunes
WO1997040149A1 (fr) * 1996-04-18 1997-10-30 Akzo Nobel N.V. Auto-antigene et proteines lies de maniere structurelle et leur utilisation dans l'immunotherapie des maladies auto-immunes
WO1999053056A1 (fr) * 1998-04-10 1999-10-21 Snow Brand Milk Products Co., Ltd. Nouvelle proteine et ses procedes de production

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
SULSTON, J.E. AND WATERSTON, R.: "Toward a complete human genome sequence", GENOME RES., vol. 8, no. 11, November 1998 (1998-11-01), pages 1097 - 1108, XP002181292 *

Also Published As

Publication number Publication date
AU2002221460A1 (en) 2002-05-15
CN1352087A (zh) 2002-06-05

Similar Documents

Publication Publication Date Title
WO2001038522A1 (fr) Nouveau polypeptide, histone humaine h2a.21, et polynucleotide codant pour ce polypeptide
WO2001038371A1 (fr) Nouveau polypeptide glutamate arnt synthetase 58 d'origine humaine et polycnucleotide codant pour ce polypeptide
WO2001031030A1 (fr) Nouveau polypeptide, phosphodiesterase 21 humaine de type acide sphingomyelinase, et polynucleotide codant pour ce polypeptide
WO2002036619A1 (fr) Nouveau polypeptide, glucoproteine humaine 42, et polynucleotide codant ce polypeptide
WO2001029228A1 (fr) Nouveau polypeptide, caseine kinase humaine 48, et polynucleotide codant pour ce polypeptide
WO2001038540A1 (fr) Nouveau polypeptide, la methionyl arnt synthetase humaine de 29 kda, et polynucleotide codant pour ledit polypeptide
WO2001038379A1 (fr) Nouvelle proteine ribosomique humaine l23 a base d'un polypeptide et polynucleotide codant cette proteine
WO2001038545A1 (fr) Nouveau polypeptide, acetyle galactosyle transferase 45 humain et polynucleotide codant ce polypeptide
WO2001094529A2 (fr) Nouveau polypeptide, serine hydrolase humaine atp-dependante 21, et polynucleotide codant pour ce polypeptide
WO2001038389A1 (fr) Nouvelle proteine ribosomique l14.22 a base d'un polypeptide et polynucleotide codant cette proteine
WO2001031024A1 (fr) Nouveau polypeptide, threonine synthetase 71, et polynucleotide codant pour ce polypeptide
WO2001075125A1 (fr) Nouveau polypeptide, serine hydrolase humaine atp-dependante 31, et polynucleotide codant pour ce polypeptide
WO2001030837A1 (fr) Nouveau polypeptide, galectine 15, et polynucleotide codant pour ce polypeptide
WO2001046441A1 (fr) Nouveau polypeptide, proteine humaine shc 43, et polynucleotide codant pour ce polypeptide
WO2001030840A1 (fr) Nouveau polypeptide, une proteine 57 a doigt de zinc, et polynucleotide codant pour ce polypeptide
WO2001030818A1 (fr) Nouveau polypeptide, proteine de liaison 33 a l'arn, et polynucleotide codant pour ce polypeptide
WO2001072986A1 (fr) Nouveau polypeptide, serine hydrolase humaine atp-dependante 10, et polynucleotide codant pour ce polypeptide
WO2001032862A1 (fr) Nouveau polypeptide, proteine humaine 20 ribosome s4, et polynucleotide codant pour ce polypeptide
WO2001070956A1 (fr) Nouveau polypeptide, proteine humaine de reparation 8 du mesappariement de l'adn, et polynucleotide codant pour ce polypeptide
WO2001032698A1 (fr) Nouveau polypeptide, proteine humaine 16 associee aux maladies auto-immunes, et polynucleotide codant pour ce polypeptide
WO2001031032A1 (fr) Nouveau polypeptide, sous-unite 42 d'ht atpase c humaine vacuolaire, et polynucleotide codant pour ce polypeptide
WO2001079508A1 (fr) Nouveau polypeptide, proteine porteuse mitochondriale humaine 18, et polynucleotide codant pour ce polypeptide
WO2001029229A1 (fr) Nouveau polypeptide, proteine humaine 20 de liaison de retinoblastome et polynucleotide le codant
WO2001038520A1 (fr) Nouveau polypeptide, proteine humaine 36 liee au mouvement de la bicouche de phospholipide, et polynucleotide codant pour ce polypeptide
WO2001029077A1 (fr) NOUVEAU POLYPEPTIDE, FACTEUR REGULATEUR HUMAIN 34 DE LA β 2-MICROGLOBULINE, ET POLYNUCLEOTIDE CODANT POUR CE POLYPEPTIDE

Legal Events

Date Code Title Description
DFPE Request for preliminary examination filed prior to expiration of 19th month from priority date (pct application filed before 20040101)
121 Ep: the epo has been informed by wipo that ep was designated in this application
REG Reference to national code

Ref country code: DE

Ref legal event code: 8642

122 Ep: pct application non-entry in european phase
NENP Non-entry into the national phase

Ref country code: JP

WWW Wipo information: withdrawn in national office

Country of ref document: JP