JP2006262907A - B細胞リンパ腫の治療のためのヒトbリンパ球限定分化抗原に対するキメラ抗体と放射能標識抗体の療法利用 - Google Patents
B細胞リンパ腫の治療のためのヒトbリンパ球限定分化抗原に対するキメラ抗体と放射能標識抗体の療法利用 Download PDFInfo
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Abstract
【解決手段】抗−CD20抗体依存性細胞介在性細胞溶解をCD20+ 細胞に対して誘導し且つATCC寄託番号69119 のトランスフェクトーマにより生産されるキメラ抗体と実質的に同じB−細胞涸渇活性を有するキメラ抗CD20抗体、及びその利用。
【選択図】なし
Description
本発明は、B細胞表面抗原Bp35("CD20")に対する放射能標識抗体およびキメラ抗体を使ったB細胞リンパ腫の治療に向けられる。
「接合」抗体の代わりとして、「キメラ」抗体、即ち2以上の異なる種(例えばマウスとヒト)からの部分を含んで成る抗体が開発されている。例えば、Liu, A.Y. ら、"Production of a Mouse-Human Chimeric Monoclonal Antibody to CD20 with Potent Fc-Dependent Biologic Activity" J. Immun. 139/10:3521-3526 (1987) は、CD20抗原に対して向けられたマウス/ヒトキメラ抗体を記載している。PCT公報第WO 88/04936 号も参照のこと。しかしながら、B細胞障害の治療のためのそのようなキメラ抗体の能力、効力または実用性に関する情報は該文献中に全く与えられていない。
必要とされ且つ大きな技術進歩になると思われるものは、霊長類(ヒトを含むがそれに限定されない)におけるB細胞リンパ腫の治療のためにCD20抗原をターゲティングする治療法である。
1)免疫グロブリン重鎖の前のCMVプロモーター/エンハンサーは、−350 位の NheI部位から−16位の SstI部位まで、軽鎖の前のプロモーター/エンハンサーの先端が切り取られた変形である(41 Cell, 521, 1985を参照のこと)。
4)ヒト免疫グロブリン軽鎖および重鎖カセットは、転写解読枠を維持し且つ免疫グロブリン鎖の中に通常見つかるアミノ酸を変更しないような軽鎖および重鎖免疫グロブリン可変領域の挿入を考慮した特定のDNA制限部位を含有する。
6)NEO カセットは、それ自身の真核プロモーター(BETA)とポリアデニル化領域(SV40初期ポリアデニル化領域、"SV")を含んだ。
TCAE 8ベクターとNEO カセットに関しては、Kozak 領域は部分的に損傷された共通Kozak 配列(上流の ClaI部位を含む)であった:
当業者により認識されるように、TCAEベクターは、免疫学的に活性なキメラ抗C20 抗体を生産させる上で実質的に時間を削減することを考慮に入れる。非ヒト軽鎖および重鎖可変領域の調製と単離、次いでそれらをヒト軽鎖定常転写カセットとヒト重鎖定常転写カセット中に組み込むことは、免疫学的に活性なキメラ抗C20 抗体の生産に備える。
A.抗CD20モノクローナル抗体(マウス)産生("2B8" )
BALB/Cマウスを3〜4カ月の期間に渡る毎週の注射によりヒトリンパ芽球様細胞系SB(Adams, R.A. ら、"Direct implantation and serial transplantation of human acute lymphoblastic leukemia in hamsters, SB-2." Can. Res. 28:1121-1125 (1968) を参照のこと;この細胞系はATCC受入れ番号ATCC CCL 120のもとにthe American Tissue Culture Collection, Rockville, MD.から入手可能である)で繰り返し免疫処置した。
i.MX-DTPA
14Cで標識された1−イソチオシアネートベンジル−3−メチルジエチレントリアミンペンタ酢酸(" 14C標識MX-DTPA")を2B8 への放射能標識の接合のためのキレート化剤として使用した。無金属条件を維持するためにMX-DTPA の操作を行った。即ち、無金属試薬を使用し、そして可能な時には、Alconox で洗浄しMilli-Q 水で濯いだポリプロピレン製プラスチック容器(フラスコ、ビーカー、メスシリンダー、ピペットチップ)を同様に使用した。MX-DTPA をOtto Gansow 博士(National Institute of Health, Bethesda, MD)から乾燥固体形態として入手し、4℃で乾燥保存した(遮光下で)。Milli-Q 水中に2 〜5 mMの濃度の原液を調製し、−70℃で保存した。MX-DTPA は水中の二ナトリウム塩としてCoulter Immunology (Hialeah, Florida) からも得られ、これを−70℃で保存した。
CENTRICON 30TMスピンフィルター(30,000D, MWCO; Amicon )を使った繰り返し緩衝液交換を利用して、150mM NaClを含む無金属の50mMバイシン−NaOH, pH 8.6中に2B8 抗体を移すことにより、MX-DTPA との接合用の精製2B8 を調製した。一般に、該フィルター装置に50〜200 μlのタンパク質(10mg/nl)を加え、次いで2mlのバイシン緩衝液を加えた。Sorval SS-34ローター中で4℃で該フィルターを遠心した(6,000 rpm, 45 分)。滞留液容量は約50〜100 μlであった。同フィルターを使ってこの工程を2回繰り返した。滞留液をポリプロピレン製1.5 mlスクリューキャップ付試験管に移し、タンパク質について分析し、10.0mg/mlに希釈し、使用まで4℃で保存した。上述のプロトコールを使って同様に該タンパク質を150mM NaClと0.05%アジ化ナトリウムを含む50mMクエン酸ナトリウム, pH 5.5中に移した。
2B8 とMX-DTPA の接合は、周囲温度でポリプロピレン試験管中で実施した。凍結したMX-DTPA 原液を使用直前に解凍した。10mg/mlのタンパク質50〜200 mlを、4:1のMX-DTPA :2B8 のモル比においてMX-DTPA と反応させた。MX-DTPA 原液を添加しそして穏やかに混合することにより反応を開始した。接合は周囲温度で一晩(14〜20時間)進行させておいた。実施例I. B. ii. において上述したような0.05%アジ化ナトリウムを含む無金属生理的食塩水(0.9 %w/v )中への透析または反復限外濾過により、接合体から未反応のMX-DTPA を除去した。タンパク質濃度を10mg/mlに調整し、放射能標識するまでポリプロピレン試験管中に4℃で保存した。
シンチレーションカウンティングしそして精製接合体を使って得られた値を炭素[14]標識MX-DTPA の比活性と比較することにより、MX-DTPA の取り込みを測定した。非放射性MX-DTPA (Coulter Immunology)を使用した幾つかの研究には、該接合体を既知濃度と既知比活性のイットリウム[90]の過剰の放射性担体溶液と共にインキュベートすることにより、MX-DTPA 取り込みを評価した。
全細胞ELISA を使って接合2B8 の免疫反応性を評価した。対数期中期のSB細胞を遠心により培養物から収得し、1×HBSSで2回洗浄した。細胞をHBSS中1〜2×106 細胞/mlに希釈し、50,000〜100,000 細胞/ウエルになるように96ウエルのポリスチレンマイクロタイタープレート中にアリコートに分けた。プレートを40〜45℃にて2時間真空乾燥して細胞をプラスチックに固定させた。使用するまで該プレートを−20℃で保存した。アッセイ用に、使用直前にプレートを周囲温度に温め、次いで1% BSAを含有する 1×PBS, pH 7.2-7.4 でブロックした(2時間)。アッセイ用試料を 1×PBS /1% BSA中に希釈し、プレートに添加し、同緩衝液中に系列希釈(1:2)した。
無担体インジウム[111] を使って接合体を放射能標識した。0.05M HCl 中の同位体のアリコート(0.1 〜2 mCi /mg抗体)をポリプロピレン試験管に移し、約1/10容の無金属2M HClを加えた。5分間インキュベーション後、無金属2M酢酸ナトリウムを加え、該溶液をpH 4.0-4.4に調整した。生理的食塩水中、または0.05%アジ化ナトリウムを含む50mMクエン酸ナトリウム/150mM NaCl中の10.0mg/ml DTPA 原液から約0.5 mgの2B8-MX-DTPA を加え、次いで該溶液を即座に穏やかに混合した。pH試験紙で溶液のpHを調べ、4.0 〜4.5 の値であることを確認し、該混合物を周囲温度で15〜30分間インキュベートした。次いで、20mM EDTA を1 mMの最終濃度になるように加えることにより反応を失活させ、2M酢酸ナトリウムを使って反応混合物を約pH 6.0に調整した。
ある実験では、上述のものと同様であるがHPLCによる精製を実施しないプロトコールに従って、2B8-MX-DTPA をインジウム[111] で放射能標識した。これを「ミックス&シュート」プロトコールと名付けた。
2 ng HClを使用しないこと以外、I2B8の調製について記載したのと同じプロトコールに従ってイットリウム[90]標識2B8-MX-DTPA ("Y2B8")を調製した。イットリウム標識接合体の全調製物は上述のものと同じサイズ排除クロマトグラフィーにより精製した。
i.放射能標識2B8-MX-DTPA の生体内分布
I2B8を6〜8週齢のBALB/cマウスにおいて組織分布について評価した。上述の「ミックス&シュート」プロトコールに従って臨床用2B8-MX-DTPA を使って放射能標識接合体を調製した。該接合体の比活性は 2.3 mCi/mgであり、該接合体を50mg/ml HSAを含むPBS, pH 7.4 中に配合した。
線量計測のため、2B8-MX-DTPA を2.3 mCi /mgの比活性になるようにインジウム[111] で放射能標識し、そして約1.1 μCiを20匹のBALB/cマウスの各々に注射した。次いで、各々5匹のマウスから成るグループを1, 24, 48 および72時間目に犠牲にし、それらの器官を取り出し、分析用に調製した。加えて、皮膚、筋肉および骨の一部分を取り出し、分析用に処理し、尿と糞便も収集し、24〜74時間の時点で分析した。
放射能標識2B8-MX-DTPA の局在化は、ラモスB細胞腫を有する無胸腺症マウスにおいて測定した。6〜8週齢の無胸腺症マウスに、無胸腺症マウス中での増殖用に前に順応させておいた1.2 ×107 個のラモスB細胞腫を含む0.1 mlのRPMI-1640 を皮下注射(左後方側腹部)した。腫瘍は2週間以内に出現し、0.07〜1.1 グラムの重さに及んだ。マウスに100 μlのインジウム[111] 標識2B8-MX-DTPA (16.7μCi)を静注し、0, 24, 48 および72時間目に頸部脱臼により3匹のマウスのグループを犠牲にした。犠牲後、尾、心臓、肺、肝臓、腎臓、脾臓、筋肉、大腿および腫瘍を取り出し、洗浄し、重さを量った。分析用に血液試料も採取した。各標本に結合した放射能をγカウンティングにより測定し、%注入線量/g組織を測定した。
上述した予備的生体内分布実験(実施例I. B. viii. a. )に従って、接合2B8 をインジウム[111] で2.3 mCi /mgの比活性に放射能標識し、およそ1.1 μCiを20匹のBALB/cマウスの各々に注射して放射能標識物質の生体内分布を調べた。続いて、各々5匹から成るグループを1, 24, 48 および72時間目に犠牲にし、それらの器官と皮膚、筋肉および骨の一部分を取り出し、分析用に処理した。加えて、尿と糞便も収集し、24〜72時間の時点に渡り分析した。
i.2B8 と2B8-MX-DTPA :ヒト組織を使った免疫組織学的研究
アセトンで固定した32の異なるヒト組織のパネルを使ってマウスモノクローナル抗体 2B8の組織反応性を評価した。抗体2B8 は、非常に限定された組織分布パターンを有した抗CD20抗原と反応する。該抗原は、造血起源のものを含むリンパ系組織中の細胞のサブセットにおいてのみ観察される。
a.第I/II相臨床実験:単一線量療法研究
I2B8(画像診断)の第I/II相臨床分析に続くY2B8の単一治療線量での処置を目下実施している。単一線量研究では、次のスキームに従う:
1.灌流による末梢幹細胞(PSC) または骨髄(BM)の収得;
2.I2B8画像診断;
3.Y2B8治療(3つの線量レベル);および
4.PSC または自己BM移植(必要なら、連続3日間の500 /mm3 以下の絶体好中球数または20,000/mm3 以下の血小板数に基づいて、骨髄検査に関する骨髄回収の証拠なしで)
Y2B8の線量レベルは次の通りである:
画像診断実験が許容できれば、0.0 または1.0 mg/kg患者体重の2B8 を点滴静注により250 mg/時間を越えない速度で投与する。この後、Y2B8 (10, 20または40 mCi) を20 mCi/時間の点滴静注速度で投与する。
Y2B8の第I/II相臨床分析を現在実施している。複数線量研究の場合、次のスキームに従っている:
1.PSC またはBMの収得;
2.I2B8画像診断
3.4線量または80 mCiの全蓄積線量でのY2B8治療(3線量レベル);および
4.PSC または自己BM移植(臨床医の決定に基づく)
Y2B8の線量レベルは次の通りである:
画像診断(線量計測)実験を次の通り実施する:最初の2人の患者を使って未標識抗体(即ち2B8 )の好ましい画像診断線量を決定する。最初の2人の患者に250 ccの生理的食塩水中の100 mgの未標識2B8 を4時間に渡り投与し、次いで0.5 mCi のI2B8を投与する--t=0、t=10分、t=120 分、t=24時間およびt=48時間の時点で生体内分布データ用に血液をサンプリングする。t=2時間、t=24時間およびt=48時間の時点で患者を多領域γカメラ画像でスキャンする。t=48時間でスキャンした後、患者に上述と同様に250 mgの2B8 に次いで4.5 mCi のI2B8を投与する--- 次いで上述と同様に採血とスキャンニングを行う。
Y2B8での処置の前に、最初の4人を除く患者には、上述と同様に2B8 を投与し、次いで5 〜10分間に渡りY2B8を点滴静注により投与する。t=0、t=10分、t=120 分、t=24時間およびt=48時間の時点で生体内分布用に血液をサンプリングする。患者にほぼ6〜8週間毎にそれぞれの線量のYB28(第一の線量の場合と同じ線量を投与する)を4線量の最大値または80 mCiの全蓄積線量になるように投与する。患者のWBC が3,000 以上であり且つAGC が1000,000以上となるまで、患者に次の線量のY2B8を投与しないことが最も好ましい。
3線量レベル実験の完了の後、MTD の範囲を限定する。次いで追加の患者を実験に登録し、MTD を投与する。
A.キメラ抗CD20免疫グロブリンDNA発現ベクターの作製
2B8 マウスハイブリドーマ細胞からRNAを単離し(Chomczynki, P.ら、"Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction." Anal.Biochem. 162:156-159 (1987)に記載された通りに)、そしてそれからcDNAを調製した。5′末端においてマウス軽鎖シグナル配列と相同性を有するDNAプライマーと3′末端においてマウス軽鎖J領域と相同性を有するDNAプライマーのセットを使ったポリメラーゼ連鎖反応により、該cDNAからマウス免疫グロブリン軽鎖可変領域DNAを単離した。プライマー配列は次の通りであった:
5' ATC AC AGATCT CTC ACC ATG GAT TTT CAG GTG CAG ATT ATC AGC TTC 3'
(下線を引いた部分はBgl II部位であり、上に線を引いた部分は開始コドンである)
2.VL アンチセンス(配列番号4)
5' TGC AGC ATC CGTACG TTT GAT TTC CAG CTT 3'
(下線を引いた部分はBsi WI部位である)
TCAE 8中の対応するBgl II部位とBsi WI部位については図1および図3を、そしてTCAE 8中の抗CD20中の対応する部位については図12〜21を参照のこと。
1.VH センス(配列番号6)
5' GCG GCT CCC ACGCGT GTC CTG TCC CAG 3'
(下線を引いた部分はMlu I部位である)
2.VH アンチセンス(配列番号7)
5' GG(G/C) TGT TGT GCTAGC TG(A/C) (A/G)GA GAC (G/A)GT GA 3'
(下線を引いた部分はNhe I部位である)
このマウス重鎖配列は図23(配列番号8)に示される。図14〜15のヌクレオチド2401〜2820も参照のこと。図23はこのマウス可変領域、CDRおよびフレームワーク領域のアミノ酸配列も提供する。2B8 からのマウス重鎖可変領域はマウスVH 2B ファミリーに属する。
Kabat (前掲)を参照のこと。
チャイニーズハムスター卵巣("CHO") 細胞DG44はヒポキサンチンとチミジンを欠くSSFM II 培地(Gibco, Grand Island, NY, Form No.91-0456PK)中で増殖させ;SP2/0 マウスミエローマ細胞は5%ウシ胎児血清と20ml/lのグルタミンが補足されたダルベッコ改良イーグル培地("DMEM")(Irvine Scientific, Santa Ana, Ca.,カタログ No.9024)中で増殖させた。 0.4mlの使い捨てキュベット中でBTX 600 エレクトロポレーション装置(BTX, San Diego, CA)を使って、 NotIで制限された25μg のCHO または50μg のSP2/0 プラスミドDNAを用いて400 万個の細胞をエレクトロポレーションした。
実施例II. B. の結果は、特に、キメラ抗CD20抗体がTCAE 8ベクターを使ってCHO およびSP2/0 トランスフェクトーマから生産され、そしてそれらのキメラ抗体がマウス抗CD20モノクローナル抗体2B8 と実質的に同じ特異性と結合力を有したことを指摘している。
i.ヒトC1q 分析
CHO とSP2/0 の両細胞系により生産されたキメラ抗CD20抗体を、フルオレセイン標識C1q (C1q はQuidel, Mira Mesa, CA, Prod. No. A400 から得られ、そしてFITC標識はSigma, St. Louis MO, Prod. No. F-7250 から得られた)を使ったフローサイトメトリーアッセイにおいてヒトC1q 結合について評価した。C1q のFITC標識は、Selected Methods In Cellular Immunology, Michell & Shiigi 編(W.H. Freeman & Co., San Francisco, CA, 1980, p.292)に記載されたプロトコールに従って行った。Becton Dickinson FACScanTMフローサイトメーターを使って分析結果を誘導した(515 〜545 nmの領域に渡ってフルオレセインを測定した)。
図24の結果として、キメラ抗CD20抗体条件についてのみ蛍光の有意な増加が観察された。即ち、付着性キメラ抗CD20抗体を有するSB細胞のみがC1q 陽性であり、一方他の条件は対照と同じパターンを生じた。
キメラ抗CD20抗体をヒト血清(補体源)の存在下でリンパ腫細胞系を溶解する能力について分析した。100 μCiの51Crと1×106 個のSB細胞を37℃で1時間混合することにより、CD20陽性SB細胞を51Crで標識した。次いで標識SB細胞を、当量のヒト補体と当量(0〜50μg/ml)のキメラ抗CD20抗体または2B8 のいずれかの存在下で37℃にて4時間インキュベートした(Brunner, K.T. ら、"Quantitative assay of the lytic action of immune lymphoid cells on 51Cr-labeled allogeneic target cells in vitro." Immunology 14:181-189 (1968)を参照のこと)。結果を図25に与える。
図25の結果は、特に、キメラ抗CD20抗体がそれらの条件下で有意な溶解(49%)をもたらすことを示す。
このアッセイには、CD20陽性細胞(SB)とCD20陰性細胞〔T細胞白血病系HSB; Adams, Richard, "Formal Discussion," Can. Res. 27:2479-2482 (1967) を参照のこと;ATCC寄託番号ATCC CCL 120.1〕を使用した。両者を51Crで標識した。Brunner, K.T. ら、"Quantitative assay of the lytic action of immune lymphoid cells on 51Cr-labeled allogeneic target cells in vitro ; inhibition by isoantibody and drugs." Immunology 14:181-189 (1968)中に記載されたプロトコールに従って分析を行った。
実施例IIの結果は、特に、実施例Iのキメラ抗CD20抗体が免疫学的に活性であったことを示す。
A.非ヒト霊長類実験
3種類の別々の非ヒト霊長類実験を実施した。便宜上、それらを「キメラ抗CD20 : CHO & SP2/0」、「キメラ抗CD20 : CHO」および「高用量キメラ抗CD20」と名付ける。条件は次の通りであった。
キメラ抗CD20 : CHO & SP2/0
キメラ抗CD20 : CHO
2匹のマカクザル(White Sands )に、CHO トランスフェクトーマから生産された16.8mg/kgの免疫学的に活性なキメラ抗CD20抗体(無菌の食塩水中)を連続4週間の期間に渡り毎週点滴注入した。処置の終わりに、骨髄切除のために両動物を麻酔した。リンパ節生検試料も取った。両方の組織セットを、Ling, N.R.ら、"B-cell and plasma cell antigens." Leucocyte Typing III White Cell Differentiation Antigens, A.J. McMichael 編 (Oxford University Press, Oxford UK, 1987), p.302に記載されたプロトコールに従って、Bリンパ球の存在下でフローサイトメトリーによりLeu 16で染色した。
血漿の除去後、白血球をハンクス平衡塩類溶液("HBSS")で2回洗浄し、血漿と同容量のウシ胎児血清(56℃で30分間熱不活性化したもの)中に再懸濁する。この細胞調製物の0.1 ml容量を6本の15ml遠心管の各々に分配した。TおよびBリンパ球集団を同定するために、ヒトリンパ球表面マーカーCD2 (AMAC, Westbrook, ME) 、CD20 (Becton Dickinson) およびヒトIgM (Binding Site, San Diego, CA) に対して特異性を有する蛍光標識モノクローナル抗体を3本の試験管に加えた。全ての試薬は対応するサルリンパ球抗原に陽性であることを前に試験しておいた。
生体内のB細胞を涸渇させることにおいてCHO とSP2/0 により生産された抗体の効力の間には何ら観察できる差は確認できなかったが、CHO トランスフェクトーマから誘導されたキメラ抗CD20抗体を1.6 mg/kgと6.4 mg/kgの用量レベルで注射したサルと、SP2/0 により生産された抗体を0.4 mg/kgの用量レベルで注射したサルについては、第7日後に始まるB細胞再生のわずかな増加が観察された。図27、図28および図29はキメラ抗CD20 : CHO & SP2/0実験から得られた結果を与え;図27は0.4 mg/kg用量レベルに向けられ;図28は1.6 mg/kg用量レベルに向けられ;そして図29は6.4 mg/kg用量レベルに向けられる。
表4は、表3の治療方法を使ったリンパ節の細胞集団に対する免疫学的に活性なキメラ抗CD20抗体の効果を要約する(0.4 mg/kgの4日分量;6.4 mg/kgの1回量);正常リンパ節(対照サル、腋窩およびそ径部)および正常骨髄(2匹のサル)についての比較値も提供する。
i.C2B8の第I/II相臨床実験:単一用量療法研究
組織学的に実証されたB細胞リンパ腫を有する15人の患者を第I/II相臨床実験においてC2B8で処置した。用量増加実験において各患者に単一用量のC2B8を投与した;次の用量:10mg/m2 ;50mg/m2 ;100 mg/m2 ;250 mg/m2 および500 mg/m2 につき3人の患者を使用した。処置は、生理的食塩水中250 ccの最終容量または1mg/mlの最大濃度に希釈されたC2B8を、0.22ミクロンの並列フィルターを通して点滴静注することにより行った。初期速度は最初の1時間の間50cc/時であった。全く毒性が観察されなければ、投与速度を最大200 cc/時まで上げることが可能であった。
測定可能な進行性疾患を伴う組織学的に確証されたB細胞リンパ腫を有する患者は、2部に分けられるこの実験に適格である。第I相は、用量制限する毒性を特徴づけるための用量増加と生物学的に活性な耐容量レベルの決定から成り、この段階では3人の患者から成るグループに合計4回の点滴静注による毎週の点滴静注を行う。3レベルの各々における蓄積量は次の通りである:500 mg/m2 (125 mg/m2 /点滴注入);1000mg/m2 (250 mg/m2 /点滴注入);1500mg/m2 (375 mg/m2 /点滴注入)。生物学的に活性な耐容用量は、耐容できる毒性と適度の活性の両方を有する最低用量として定義され、決定されるだろう。第II相では、C2B8の4回量の活性を決定することに重点をおいて、追加の患者に生物学的に活性な耐容用量を投与する。
B細胞リンパ芽球腫(ラモス腫瘍細胞)を使用するマウス異種移植モデル(nu/nu マウス、雌、約10週齢)において、C2B8とY2B8を使った組合せ療法アプローチを研究した。比較目的で、別のマウスもC2B8とY2B8で処置した。
B.Y2B8 (100 μCi)
C.C2B8 (200 μg) および
D.Y2B8 (100 μCi) + C2B8 (200μg)
C2B8により試験したグループには、1回目の注射の7日後に2回目のC2B8注射(200 μg/マウス)を与えた。腫瘍測定はキャリパーを使って2または3日毎に行った。
処置材料の調製は次のプロトコールに従った:
塩化イットリウム[90](60 mCi)をポリプロピレン試験管に移し、無金属2M酢酸ナトリウムを使ってpH 4.1-4.4に調整した。2B8-MX-DTPA (生理的食塩水中0.3 mg;2B8-MX-DTPA の調製については上記を参照のこと)を加え、渦動攪拌により穏やかに混合した。15分間のインキュベーション後、0.05×容の20mM EDTA と0.05×容の2M酢酸ナトリウムを加えることにより反応を失活させた。この反応混合物 5.0μlを、75mg/ml HSAと1mM DTPAを含む2.5 mlの1×PBS (「配合緩衝液」)中に希釈することにより放射能濃度を測定した。
上記と同様にしてC2B8を調製した。C2B8は生理的食塩水中の無菌試薬として5.0 mg/mlで供給した。注射前に生理的食塩水中に2.0 mg/mlに希釈し、次いで滅菌濾過した。
C.結果
処置後、腫瘍サイズを長さと幅の積として表し、そして図31(Y2B8対食塩水);図32(C2B8対食塩水)および図34(Y2B8+C2B8対食塩水)に指摘した日に測定値をとった。標準誤差も決定した。
図34に示されるように、Y2B8とC2B8の組合せは、Y2B8またはC2B8のいずれかにより得られる効果と同等の殺腫瘍性効果を示した。
前の実施例を考慮して認められる別の治療方法は明らかである。1つのそのような方策は、C2B8の治療用量の後で約一週間以内に2B8 と放射能標識2B8 (例えばY2B8);または2B8, C2B8 およびY2B8;またはC2B8と例えばY2B8のいずれかの組合せを使用する。他の方策は放射能標識C2B8の使用である--- そのような方策はC2B8の免疫学的活性部分の利益に加えて放射能標識に関係する利益の利用を考慮したものである。好ましい放射能標識としては、マウス抗体2B8 に比較して大きなC2B8の循環半減期を仮定すればイットリウム90が挙げられる。
上記の別の治療方法は限定のつもりでなくむしろ例示として与えられる。
特許手続き上の微生物の寄託の国際的承認に関するブタペスト条約( 「ブタペスト条約」)の規定のもとに、TCAE 8中の抗CD20(寄託の目的でE.コリ中に形質転換せしめたもの)をアメリカン・タイプ・カルチャー・コレクション(ATCC), 12301 Parklawn Drive, Rockville, Maryland, 20852に寄託した。該微生物は1992年11月9日にATCCにより試験され、そしてその日に生存可能であると決定された。ATCCはこの微生物に次のATCC寄託番号を付与した:ATCC 69119(TCAE 8中の抗CD20)。ブタペスト条約の規定のもとに1993年6月22日にハイブリドーマ2B8 をATCCに寄託した。該培養物の生存可能性は1993年6月25日に決定され、ATCCはこのハイブリドーマに次のATCC寄託番号を付与した:HB 11388。
Claims (7)
- 免疫学的に活性なキメラ抗−CD20抗体の軽鎖及び重鎖をコードする核酸を含んでなる宿主細胞において、前記軽鎖をコードする配列が、図4に示されるアミノ酸配列のアミノ酸残基+1〜+107をコードするヌクレオチド配列を含んでなり、そして前記重鎖をコードする配列が、図5に示されるアミノ酸配列のアミノ酸残基+1〜+113をコードするヌクレオチド配列を含んでなる、宿主細胞。
- 前記軽鎖をコードする配列が、ヒトκ軽鎖定常領域をコードするヌクレオチド配列を更に含んであり、そして前記重鎖をコードする配列が、ヒトγ1重鎖定常領域をコードするヌクレオチドを更に含んでなる、請求項1に記載の宿所細胞。
- 免疫学的に活性なキメラ抗−CD20抗体を生産することが出来る、請求項1又は2に記載の宿主細胞。
- 哺乳類細胞である、請求項1〜3のいずれか1項に記載の宿主細胞。
- チャイニーズハムスター卵巣(CHO)細胞である、請求項4に記載の宿主細胞。
- SP2/0細胞である、請求項4に記載の宿主細胞。
- 請求項3に記載の宿主細胞中の核酸配列によりコードされる軽鎖及び重鎖を発現せしめ、そして当該細胞により生産された抗体を精製することを含んでなる、精製された抗体の製造方法。
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US97889192A | 1992-11-13 | 1992-11-13 | |
US08/149,099 US5736137A (en) | 1992-11-13 | 1993-11-03 | Therapeutic application of chimeric and radiolabeled antibodies to human B lymphocyte restricted differentiation antigen for treatment of B cell lymphoma |
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JP2000126317A Expired - Lifetime JP4091235B2 (ja) | 1992-11-13 | 2000-04-21 | B細胞リンパ腫の治療のためのヒトbリンパ球限定分化抗原に対するキメラ抗体と放射能標識抗体の療法利用 |
JP2006135870A Expired - Lifetime JP4203080B2 (ja) | 1992-11-13 | 2006-05-15 | B細胞リンパ腫の治療のためのヒトbリンパ球限定分化抗原に対するキメラ抗体と放射能標識抗体の療法利用 |
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JP2000126317A Expired - Lifetime JP4091235B2 (ja) | 1992-11-13 | 2000-04-21 | B細胞リンパ腫の治療のためのヒトbリンパ球限定分化抗原に対するキメラ抗体と放射能標識抗体の療法利用 |
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