JP4976848B2 - アルファ(2)マクログロブリン−抗原分子複合体を用いる癌および感染性疾患の治療のための方法および組成物 - Google Patents
アルファ(2)マクログロブリン−抗原分子複合体を用いる癌および感染性疾患の治療のための方法および組成物 Download PDFInfo
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Description
本発明は、哺乳類の血清から単離されたアルファ(2)マクログロブリン複合体の、癌および感染性疾患の治療および予防のための使用に関する。本発明はまた、血清に由来するアルファ(2)マクログロブリン-抗原分子複合体を作るための組成物および方法をも包含する。
α-マクログロブリンは、補体成分C3、C4およびC5をも含む構造的に関連するタンパク質のスーパーファミリーのメンバーである。ヒト血漿タンパク質アルファ(2)マクログロブリン(α2M)は、元来プロテイナーゼ阻害剤ならびに血漿および炎症性液体のプロテイナーゼスカベンジャー分子として知られていた720kDaのホモ四量体タンパク質である(総論として、ChuおよびPizzo, 1994, Lab. Invest. 71:792を参照されたい)。α2Mは1474アミノ酸残基を有する前駆体として合成される。最初の23アミノ酸はシグナル配列として機能し、開裂して1451アミノ酸残基を有する成熟タンパク質を生成する(Kanら、1985, Proc. Natl. Acad. Sci. U.S.A 82:2282-2286)。
熱ショックタンパク質(HSP)は、ストレスタンパク質とも呼ばれるが、初めは熱ショックに反応して細胞により合成されるタンパク質として同定された。Hspは、分子量に基づいて、Hsp100、Hsp90、Hsp70、Hsp60およびsmHspの5つのファミリーに分類される。後に、これらのファミリーの多くのメンバーが、栄養欠乏、代謝の崩壊、酸素ラジカル、および細胞内または細胞外病原体による感染を含む他のストレスを伴う刺激に反応して誘導されることが見出された(Welch, 1993, Scientific American 56-64; Young, 1990, Annu. Rev. Immunol. 8:401-420; Craig, 1993, Science 260:1902-1903; Gethingら、1992, Nature 355:33-45; およびLindquistら、1988, Annu. Rev. Genetics 22:631-677を参照されたい)。
Srivastavaらは、同系繁殖マウスのメチルコラントレン誘導肉腫に対する免疫反応を証明した(1988, Immunol. Today 9:78-83)。これらの研究において、これらの腫瘍の個々に異なる免疫原性の原因である分子は96kDaの糖タンパク質(gp96)および84から86kDaの細胞内タンパク質であることが見出された(Srivastavaら、1986, Proc. Natl. Acad. Sci. USA 83:3407-3411; Ullrichら、1986, Proc. Natl. Acad. Sci. USA 83:3121-3125)。特定の腫瘍から単離されたgp96またはp84/86によるマウスの免疫化は、マウスにその特定の腫瘍に対する免疫を与えるが、免疫原的に異なる腫瘍に対する免疫を与えない。gp96およびp84/86をコードする遺伝子の単離および解析により、これらの間の著しい相同性が明らかになり、gp96およびp84/86が、それぞれ小胞体および細胞質ゾルの同じ熱ショックタンパク質の対であることが示された(Srivastavaら、1988, Immunogenetics 28:205-207; Srivastavaら、1991, Curr. Top. Microbiol. Immunol. 167:109-123)。さらに、Hsp70は、それが単離された腫瘍に対する免疫を引き出すが、免疫原的に異なる腫瘍に対する免疫を引き出さないことが示された。けれども、ペプチドを取り去ったHsp70はその免疫原活性を失うことが見出された(UdonoおよびSrivastava, 1993, J. Exp. Med. 178:1391-1396)。これらの観察は、熱ショックタンパク質はそれ自体は免疫原性ではなく、抗原ペプチドと非共有結合複合体を形成し、この複合体が抗原ペプチドに特異的な免疫を引き出すことを示唆している(Srivastava, 1993, Adv. Cancer Res. 62:153-177; Udonoら、1994, J. Immunol., 152:5398-5403; Sutoら、1995, Science, 269:1585-1588)。
アルファ(2)マクログロブリン受容体(本明細書においては、“α2MR”または“α2M受容体”とも記載される)は、LDL(低密度リポタンパク質)受容体関連タンパク質(“LRP”)またはCD91としても知られているが、主として肝臓、脳および胎盤に発現される。α2M受容体は、低密度リポタンパク質受容体ファミリーのメンバーである。ヒト受容体の細胞外ドメインは6個の50アミノ酸EGF繰返し体および31個のおよそ40〜42アミノ酸の補体繰返し体を含む。補体繰返し体はアミノ末端からカルボキシ末端へ、クラスターI、II、IIIおよびIVと呼ばれる2、8、10および11繰返し体のクラスターに組織される(Herzら、1988, EMBO J. 7:4119-4127)。1つの研究は、補体繰返し体3〜10 (CR3-10)を含むクラスターII (Cl-II)が受容体の主要なリガンド結合部分であることを指摘している(Hornら、1997, J. Biol. Chem. 272:13608-13613)。α2M受容体は、多様なリガンドのエンドサイトーシスに役割を果たしている。α2Mに加えて、α2MRの他のリガンドには、リポタンパク質複合体、ラクトフェリン、組織型プラスミノーゲン活性化物質(tPA)、ウロキナーゼ型プラスミノーゲン活性化物質(uPA)、および外毒素が含まれる。α2MRのリガンドの他の例は、PCT公開WO97/04794および米国特許第6,156,311号に記載されている。このように、α2M受容体は、エンドサイトーシス、抗原提示、コレステロール調節、ApoE-含有リポタンパク質清澄化、およびキロミクロン断片の除去を含むさまざまな細胞プロセスにおいて役割を果たしている。
主要組織適合遺伝子複合体(MHC)分子は、抗原提示細胞の細胞表面に抗原を提示する。抗原は、それらの由来が細胞内か細胞外かに応じて2つの異なる抗原プロセシング経路によりプロセシングされる。細胞内または内因性タンパク質抗原、すなわち、抗原提示細胞内で合成された抗原は、MHCクラスI (MHC I)分子によりCD8+細胞障害Tリンパ球に提示される。一方、細胞外または外因性に合成された抗原決定因子は、「特異的」または「専門的」APC(たとえば、マクロファージ)の細胞表面上に、MHCクラスII分子によりCD4+T細胞に提示される(一般的には、「基礎免疫学」(Fundamental Immunology), W.E.Paul編、New York: Raven Press, 1984を参照されたい)。この抗原プロセシング経路の分画的分離は、そうでない場合には隣接する細胞MHC I抗原の放出の結果として免疫反応の間に生じ得る組織の崩壊を防ぐために重要である。
Basuらにより報告された研究によれば、熱ショックタンパク質、gp96、hsp90、hsp70およびカルレティキュリンもまたCD91のリガンドである(Basuら、2001, 上記)。gp96は、p80断片と呼ばれるアミノ末端断片に位置するCD91の領域に結合する(Binderら、2000, Nature immunology, 1:151-155; WO 01/92474)。ヒトgp96をコードする遺伝子は、先に我々により染色体12 (q24.2 q24.3)に座位が決定された(Makiら、1993, Somatic Cell Mol. Gen. 19:73-81)。これに関して、CD91遺伝子が同じ染色体のあまり離れていない位置(q13 q14)に座位を決定されていることは興味深い(Hillikerら、Genomics 13:472-474)。gp96は、α2Mのような他のリガンドを介さずに、CD91に直接結合する。溶液中の、または固体マトリックスに架橋した、gp96の均一な標品はCD91に結合する。事実、CD91の主要なリガンドであるα2Mは、実際にgp96のCD91との相互作用を促進せずに阻害し、これがgp96がCD91の直接のリガンドであることの証拠となっている。gp96に結合することが示されている80kDaのタンパク質であるp80は、明らかにCD91のαサブユニットのアミノ末端分解生成物である(Binderら、2000, Nature immunology, 1:151-155)。この範囲の大きさのCD91の分解生成物は、先の研究においても観察され(Jensenら、1989, Biochem. Arch. 5:171-176)、タンパク質加水分解性開裂に対して特に感受性の高いCD91中の別個の細胞外ドメインの存在を示唆している。
本発明は、アルファ(2)マクログロブリンと抗原分子との複合体を用いる癌および感染性疾患を治療および予防するための方法および組成物であって、上記の複合体が癌または感染性疾患を有する患者の体液に由来するものに関する。本発明の好ましい実施形態において、アルファ(2)マクログロブリン-抗原分子複合体は治療される患者に対して自己由来(autologous)である。本発明は、部分的に、腫瘍または病原体に特異的なアルファ(2)マクログロブリン-抗原分子複合体が癌または感染性疾患を有する被験体の血流中に見出され、そこから単離することができるという出願人の発見に基づいている。さらに、出願人は上記のアルファ(2)マクログロブリン-抗原分子複合体を患者の血流から自己由来免疫療法に使用するのに十分な量で単離することができることを発見した。癌治療の分野において、この発見は、それぞれの患者個人の腫瘍に発現される特異的抗原を標的とした、最初に上記のような抗原を解析または同定する必要のない、高度に特異的な、個人に合わせた免疫療法薬の調製を可能にする。本明細書において、上記のようなアルファ(2)マクログロブリン複合体を用いる自己由来免疫療法が癌の治療および予防の両方に非常に有効であることが示される。さらに、上記の結果は感染性疾患を治療および予防するための適用にも拡張することができる。
図1は、アルファ(2)マクログロブリン複合体により免疫化されたマウスの群における18日間の腫瘍のサイズ(mm3)の成長を表すグラフである。実験未使用のマウスを免疫化して複合体が予防効果を与えるかどうかを決定した。A, 負の対照としてPBSにより免疫化されたマウス、PBS1と呼ぶ;B, 放射線照射したMeth A腫瘍細胞により免疫化されたマウス;C-F, 皮内Meth A腫瘍を有するマウスの血清から得たアルファ(2)マクログロブリン-抗原分子複合体により免疫化された3群のマウス(“ASCITES 1-3”と呼ぶ)(群あたり5匹のマウス);G-I, 腫瘍を有するマウスであって、該腫瘍を漂白剤により処理したマウスの血清から得たアルファ(2)マクログロブリン-抗原分子複合体により免疫化された3群のマウス(“BLEACH 1-3”と呼ぶ)(群あたり5匹のマウス);J, 腫瘍を持たないマウスの血清から得たアルファ(2)マクログロブリン-抗原分子複合体により免疫化されたマウス;K, MethA由来gp96により免疫化されたマウス;L, MethA 10(MethA腫瘍溶解液から誘導された10kDa未満のペプチド)と複合体を形成したα2Mにより免疫化されたマウス;M, 肝臓由来のgp96により免疫化されたマウス;N, MethA 10と複合体を形成したgp96により免疫化されたマウス、gp96-MethA 10と呼ぶ;およびO, PBSにより免疫化されたマウス、PBS2と呼ぶ。
本発明は、哺乳類の血清から単離されたアルファ(2)マクログロブリン-抗原分子複合体を癌または感染性疾患の治療および予防に使用するための組成物および方法に関する。本発明は、癌または感染性疾患を有する患者の体液に由来するアルファ(2)マクログロブリン-抗原分子複合体を上記の癌または感染性疾患の治療または予防に使用する方法を包含する。上記の方法には、癌および感染性疾患の自己由来治療法、ならびに癌および感染性疾患の予防のためのワクチンが含まれる。本発明はまた、複数のアルファ(2)マクログロブリン-抗原分子複合体を含む医薬組成物、およびアルファ(2)マクログロブリン-抗原分子複合体と共に癌または感染性疾患の治療のための治療薬を含む医薬組成物を包含する。哺乳類の血清におけるアルファ(2)マクログロブリン-抗原分子複合体の存在を増加させる方法もまた本発明に包含される。
本発明は、癌または感染性疾患を治療および/または予防するために使用することができる、哺乳類の血清から単離されたアルファ(2)マクログロブリン複合体を含む医薬組成物を提供する。上記の組成物は、必要に応じて、HSP-ペプチド複合体、抗腫瘍薬、抗体、サイトカイン、抗ウイルス薬、抗真菌薬、抗生物質、または化学療法薬のような(しかし、これらに限定されない)、癌および感染性疾患の治療に通常用いられる薬物を含んでもよい。本発明の医薬組成物はまた、第5.4節に癌を標的とする薬物として、第5.5節に感染性疾患を標的とする薬物として、および第5.3.3節に併用療法において癌および感染性疾患を標的とする薬物として記載される薬物を含んでもよい。本発明の医薬組成物はまた、第5.9節に記載されるもののような医薬担体をも含む。本発明の医薬組成物は自己由来治療に特に有効である。上記の医薬組成物は、アジュバント、および/または抗原分子の生産を誘導または増加する薬物を含んでもよい。ある実施形態において、上記薬物は腫瘍壊死を起こす。上記医薬組成物を製造する方法は本明細書に記載される。血清中の抗原分子および/またはアルファ(2)マクログロブリン-抗原分子複合体の存在を、上記の複合体の単離の前または単離と同時に増加させる方法もまた本明細書に記載される。
一般的に、本発明のアルファ(2)マクログロブリン-抗原分子複合体は、硫酸アンモニウム沈殿、酸抽出、陰イオンまたは陽イオン交換クロマトグラフィー、ホスホセルロースクロマトグラフィー、イムノアフィニティークロマトグラフィー、ヒドロキシアパタイトクロマトグラフィー、およびレシチンクロマトグラフィーを含む公知の方法により、哺乳類の血清から回収および精製することができる。
5.3.1. 癌の治療および予防の方法
本発明によれば、癌を治療または予防する好ましい方法は、治療を必要をする個体からα2M複合体を単離し、上記複合体を自己由来療法の形で患者に投与することを含む。投与経路に応じて、α2M複合体は単離および精製されて、自己由来法により(たとえば、原発性癌またはその転移を治療するために)上記個体に、または同じ組織型の癌の治療を必要とする他の個体に、または家族歴または環境的危険因子のために癌のリスクが高い個体に投与される。本発明の医薬組成物および方法を用いて第5.4節に記載される癌を治療または予防することができる。
感染性疾患の治療および予防のために、感染性疾患を有する哺乳類の体液からα2M-抗原分子複合体を単離し、感染性疾患に対するワクチンとして使用する。当業者に理解されるように、本明細書に記載されるプロトコールは、アルファ(2)マクログロブリン-抗原分子複合体が存在するいかなる体液からでも、α2Mポリペプチド-抗原分子複合体を単離するために使用することができる。たとえば、細胞そのものが感染媒体により感染し得る。1つの実施形態において、α2M-抗原分子複合体は感染媒体に感染した細胞からの抗原を含む血清から単離される。別の実施形態において、本発明のα2M-抗原分子複合体は、細胞内または細胞外病原体に由来する抗原を含む血清から単離することができる。本発明は、細胞内または細胞外病原体により引き起こされる感染性疾患の治療または予防に限定されない。多くの医学的に重要な微生物については広く文献に記載されている。たとえば、G.L. Mandell, J.E. BennetおよびR. Dolin, 「Mandell, Douglas, and Bennettの感染性疾患の原理および実践」(Mandell, Douglas, and Bennett’s Principles and Practice of Infectious Diseases), Churchill Livingstone, Philladelphia, Pennsylvania 2000を参照されたい。この文献の内容全体を参照により本明細書に組み入れる。
アルファ(2)マクログロブリン複合体を用いる本発明の組成物および方法は、併用療法により他の治療薬と組み合わせて投与することができる。他の治療薬には、熱ショックタンパク質-ペプチド複合体、抗腫瘍薬、抗体、サイトカイン、抗ウイルス薬、抗真菌薬、抗生物質、およびアジュバントが含まれるが、これらに限定されない。
抗体であるOrthoClone OKT4A (Ortho Biotech);ヒト化抗-CD40L IgG抗体であるANTOVATM (Biogen);ヒト化抗-VLA-4 IgG抗体であるANTEGRENTM (Elam);ヒト抗-CD64 (FcγR)抗体であるMDX-33 (Medarex/Centeon);ヒト化抗-IL-5 IgG4抗体であるSCH55700 (Celltech/Schering);それぞれヒト化抗-IL-5およびIL-4抗体であるSB-240563およびSB-240683 (SmithKline Beecham);ヒト化抗-IgE IgG1抗体であるrhuMab-E25 (Genentech/Norvartis/Tanox Biosystems);マウス抗-CD-147 IgM抗体であるABX-CBL (Abgenix);ラット抗-CD2 IgG抗体であるBTI-322 (Medimmune/Bio Transplant);マウス抗-CD3 IgG2a抗体であるOrthoclone/OKT3 (orthoBiotech);キメラ抗-CD25 IgG1抗体であるSIMULECTTM (Novartis Pharm);ヒト化抗-β2-インテグリンIgG抗体であるLDP-01 (LeukoSite);マウス抗-CD18 F(ab’)2であるAnti-LFA-1 (Pasteur-Merieux/Immunotech);ヒト抗-TGF-β2抗体であるCAT-152 (Cambridge Ab Tech);およびキメラ抗-VII因子抗体であるCorsevin M (Centocor)である。好ましい実施形態において、本発明の複合体は抗-CTLA4抗体と併用して投与される。別の好ましい実施形態において、本発明の複合体は抗41BB抗体と併用して投与される。上に挙げた免疫反応性試薬、ならびに他の免疫反応性試薬は、その免疫反応性試薬の供給者により推奨される投与法を含めて、当業者に公知のいかなる投与法に従って投与されてもよい。
1つの実施形態において、本発明の方法およびその併用療法は、癌の予防または治療を補助する補助薬として使用される1つ以上の療法を含む本発明の組成物の投与を包含する。上記療法には、化学療法薬、免疫療法薬、抗脈管形成薬、サイトカイン、ホルモン、抗体、ポリヌクレオチド、放射線照射および光線力学治療薬が含まれるが、これらに限定されない。特定の実施形態において、本発明の医薬組成物の投与を含む併用療法は、癌の再発の防止、転移の阻害、または癌または転移の増殖および/または拡散の阻害のために使用することができる。
sic acid);スピカマイシンD (spicamycin D);スピロムスチン(spiromustine);スプレノペンチン(splenopentin);スポンギスタチン1(spongistatin 1);スクアラミン(squalamine);幹細胞阻害剤;幹細胞分裂阻害剤;スチピアミド(stipiamide);ストロメリシン(stromelysin)阻害剤;スルフィノシン(sulfinosine);過度活動性血管作動性腸ペプチドアンタゴニスト;スラジスタ(suradista);スラミン(suramin);スワインソニン(swainsonine);合成グリコサミノグリカン;タリムスチン(tallimustine);タモキシフェンメチオジド(tamoxifen methiodide);タウロムスチン(tauromustine);タザロテン(tazarotene);テコガラン(tecogalan)ナトリウム;テガフル(tegafur);テルラピリリウム(tellurapyrylium);テロメラーゼ(telomerase)阻害剤;テモポルフィン(temoporfin);テモゾロミド(temozolomide);テニポシド(teniposide);テトラクロロデカオキシド(tetrachlorodecaoxide);テトラゾミン(tetrazomine);タリブラスチン(thaliblastine);チオコラリン(thiocoraline);トロンボポイエチン(thrombopoietin);トロンボポイエチン模擬物;チマルファシン(thymalfasin);チモポイエチン(thymopoietin)受容体アゴニスト;チモトリナン(thymotrinan);甲状腺刺激ホルモン;スズエチルエチオプルプリン;チラパザミン(tirapazamine);チタノセンビクロリド(titanocene bichloride);トプセンチン(topsentin);トレミフェン(toremifene);全能幹細胞因子;翻訳阻害剤;トレチノイン(tretinoin);トリアセチルウリジン;トリシリビン(triciribine);トリメトレキセート(trimetrexate);トリプトレリン(triptorelin);トロピセトロン(tropisetron);ツロステリド(turosteride);チロシンキナーゼ阻害剤;チルホスチン(tyrphostins);UBC阻害剤;ウベニメックス(ubenimex);尿生殖器洞由来成長阻害因子;ウロキナーゼ受容体アンタゴニスト;バプレオチド(vapreotide);バリオリンB (variolin B);ベクター系、赤血球遺伝子療法;ベラレソール(velaresol);ベラミン(veramine);ベルジン;ベルテポルフィン(verteporfin);ビノレルビン(vinorelbine);ビンキサルチン(vinxaltine);ビタキシン(vitaxin);ボロゾール(vorozole);ザノテロン(zanoterone);ゼニプラチン(zeniplatin);ジラスコルブ(zilascorb);およびジノスタチンスチマラマー(zinostatin stimalamer)が含まれるが、これらに限定されない。
本発明の方法により治療または予防される感染性疾患は、ウイルス、細菌、真菌、原生動物、蠕虫、および寄生体を含むがこれらに限定されない感染媒体により引き起こされる。本発明は、細胞内または細胞外病原体により引き起こされる感染性疾患の治療または予防に限定されない。併用療法は、本発明の医薬組成物の投与に加えて、感染性疾患の予防または治療を助ける1つ以上の療法の使用を含む。上記療法には、抗生物質、抗ウイルス薬、抗原生動物化合物、抗真菌化合物、および抗蠕虫薬が含まれるが、これらに限定されない。感染性疾患を治療または予防するために使用することができる他の治療法には、上記のような免疫療法、ポリヌクレオチド、抗体、サイトカイン、およびホルモンが含まれる。
リン(Temocillin);テトラサイクリン;塩酸テトラサイクリン;リン酸テトラサイクリン複合体;テトロキソプリム(Tetroxoprim);チアムフェニコール(Thiamphenicol);チフェンシリン(Thiphencillin)カリウム;チカルシリンクレシルナトリウム(Ticarcillin Cresyl Sodium);チカルシリン二ナトリウム;チカルシリン一ナトリウム;チクラトン(Ticlatone);塩化チオドニウム(Tiodonium);トブラマイシン(Tobramycin);硫酸トブラマイシン;トスフロキサシン(Tosufloxacin);トリメトプリム(Trimethoprim);硫酸トリメトプリム;トリスルファピリミジン(Trisulfapyrimidine);トロレアンドマイシン(Troleandomycin);硫酸トロスペクトマイシン(Trospectomycin);チロトリシン(Tyrothricin);バンコマイシン(Vancomycin);塩酸バンコマイシン;ビルギニアマイシン(Virginiamycin);ゾルバマイシン(Zorbamycin)が含まれるが、これらに限定されない。
anosoma rhodesiense)、トリパノソーマ・ガンビエンス(Trypanosoma gambiense)、イソスポラ(Isospora spp.)、クリプトスポリジウム(Cryptosporidium spp.)、アイメリア(Eimeria spp.)、ネオスポラ(Neospora spp.)、サルコシスティス(Sarcocystis spp.)、住血吸虫(Schistosoma spp.)が含まれる。
上記の癌および感染性疾患の治療または予防のためのいかなる併用療法においても、本発明の医薬組成物は、併用される療法の投与の前、同時、または後に投与することができる。併用される療法は上で癌または感染性疾患の治療または予防用として記載した療法のいずれのものであってもよい。
特定の実施形態において、本発明の医薬組成物は、併用される療法の投与の後、1時間から24時間の時間枠内に被験体に投与される。遅延または連続放出型の薬物送達系を使用する場合には、時間枠をさらに2、3日またはそれ以上に延長することができる。ある実施形態において、本発明の医薬組成物は、患者の余命の間中ずっと、上記の周期で被験体に投与される。
その精製の後、α2M-抗原分子複合体は、そのCD91活性およびCD91シグナル伝達経路に対する効果を測定するためにさらに解析することができる。たとえば、α2M-抗原分子複合体は、そのCD91細胞活性に対する効果を試験することにより解析される。上記のアッセイには、下流シグナル伝達アッセイ、抗原提示アッセイ、細胞障害T細胞の抗原特異的活性化のアッセイ等が含まれる。上記アッセイは免疫反応を試験および/または測定するために使用することができる。
本発明のある実施形態において、動物からアルファ(2)マクログロブリン-抗原分子複合体を単離する前に動物に腫瘍壊死を誘導すると有利である。出願人は複合体の単離の前に腫瘍壊死を誘導すると、癌の治療および予防における複合体の有効性が増大し得ることを証明した。第6節の実施例の結果を参照されたい。出願人は、1つの理論に限定するつもりはないが、壊死した腫瘍細胞が腫瘍に特異的な抗原を放出すると考えている。次いで、放出された抗原分子は血液のような体液に入り、アルファ(2)マクログロブリンと複合体を形成する。
本発明のα2Mポリペプチドと抗原分子の共有結合または非共有結合複合体は、癌または感染性疾患の治療または予防のために、免疫療法に治療上有効な用量で哺乳類に投与するための医薬製品に製剤される。薬物の溶解度および吸収の部位は、治療薬の投与経路を選択する際に考慮すべきファクターである。
試験動物を本発明の組成物により免疫化した後、その免疫反応をモニターすることにより、または当業者に公知のイムノアッセイを用いて、本発明の組成物の免疫能力を決定することができる。体液性(抗体)反応および/または細胞性免疫の発生を免疫反応の指標として用いることができる。試験動物には、マウス、ハムスター、イヌ、ネコ、サル、ウサギ、チンパンジー等、および最終的にヒト被験体が含まれる。ワクチンを導入する方法には、経口、大脳内、皮内、経皮、筋内、腹腔内、静脈内、皮下、鼻内または他の標準的な免疫化の経路が含まれる。試験する被験体の免疫反応は、たとえば、イムノソルベントアッセイ(ELISA)、イムノブロット、放射免疫沈降等のような公知の技術により、または免疫化された宿主の癌または感染性疾患に対する保護によりアッセイされた、得られた免疫血清の問題の抗原に対する反応性のようなさまざまなアプローチにより分析することができる。
本発明は、本発明の治療法を実施するためのキットをも提供する。上記のキットは、1個以上の容器に入った、製薬上許容される剤形の、治療上または予防上有効な量の共有結合または非共有結合によるα2M複合体を含む。本発明のキットのバイアル瓶に入ったα2M複合体は、たとえば無菌生理食塩水、デキストロース溶液、または緩衝溶液と組み合わされた製薬上許容される溶液、または他の製薬上許容される無菌の液体の剤形であってよい。あるいは、上記複合体は凍結乾燥または乾燥されていてもよい。この例においては、必要に応じて、キットはさらに容器に入った、複合体を注射用の溶液に再構成するための、好ましくは無菌の製薬上許容される溶液(たとえば、生理食塩水、デキストロース溶液等)を含む。
下記の結果は、アルファ(2)マクログロブリン複合体を腫瘍を有する動物の血清から完全な形で精製し、癌に対して保護するために使用することができることを示している。腫瘍に由来する抗原分子と複合体化したアルファ(2)マクログロブリンの、生存腫瘍細胞による後の攻撃に対する効果を試験するためのモデルとして同系繁殖マウスを使用した。下に示した結果は、特許請求の範囲に記載された発明、特に腫瘍を有する哺乳類から単離されたアルファ(2)マクログロブリン複合体の投与を含む自己由来療法の有効性を支持している。使用された同系繁殖マウスの免疫系は同一または近似しているので、上記の結果から癌治療のための自己由来療法の有効性を推定することができる。
アルファ(2)マクログロブリン-抗原分子複合体を精製するために、マウスから採取した血清を0.04M Tris pH7.6, 0.15M NaClにより1:1に希釈した。次いで混合物を同じ緩衝液で平衡化した65ml Sephacryl S 300R (Sigma)カラムに適用し、同じ緩衝液により溶離した。約10mlの血清に対して65mlのカラムを使用した。ドットブロットによりアルファ(2)マクログロブリン陽性画分を決定し、PD-10カラムを用いることにより緩衝液をpH 7.5の0.01Mリン酸ナトリウム緩衝液に変えた。あるいは、緩衝液を変えるステップを省略するために65mlカラムにpH 7.5の0.01Mリン酸ナトリウム緩衝液を用いてもよい。複合体を含む画分をConcanavalin Aセファロースカラムに適用した。結合した複合体を0.2Mメチルマンノースピラノシドまたは5%メチルマンノースピラノシドにより溶離して、PD-10カラムに適用して緩衝液をpH 6.0の0.05M酢酸ナトリウム緩衝液に変え、pH6.0の0.05M酢酸ナトリウム緩衝液により平衡化されたDEAEカラムに適用する。アルファ(2)マクログロブリンを0.13M酢酸ナトリウム緩衝液により溶離し、SDS-PAGEおよびイムノブロッティングにより分析した結果、純粋な形であった。
免疫化の結果を図1および表2に示す。マウスの負の対照群PBS1およびPBS2は腫瘍の発達に対して停止または減少を示さないのに対して、腫瘍を有する動物から得られたアルファ(2)マクログロブリン複合体により免疫化された動物は、12日目までに腫瘍の発達の減退を示した。15日目までに、対照群と腫瘍を有する動物に由来するアルファ(2)マクログロブリン複合体により免疫化された動物の間で、腫瘍の体積の劇的な差が明らかになった。腫瘍を有する動物の血清または腹水を有するマウスの血清から単離された複合体はどちらも攻撃されたマウスにおける腫瘍の増殖を予防するのに有効であった。腫瘍壊死を誘導するために腫瘍の中に漂白剤を注射された腫瘍を有するマウスから単離された複合体は特に有効な保護を示し、280mm3を超える体積の腫瘍は観察されなかった。皮内腫瘍を有するマウスの血清に由来するアルファ(2)マクログロブリン複合体もまた、腹水を有するマウスの血清に由来する複合体よりも有効に腫瘍の増殖を阻害することが見出された。
実験結果は、アルファ(2)マクログロブリン複合体を投与して癌を効果的に治療または予防することができることを示している。腫瘍の体積の減少は有効な治療方法であることを証明している。動物に複合体を投与した後に腫瘍細胞により攻撃した場合の予防効果は明白である。腫瘍細胞の壊死をおこす漂白剤によりまず処理された動物に由来する複合体を投与された動物において観察された有効性の程度は特に予期しなかったものであり、有望である。腫瘍細胞の壊死は、上記腫瘍に特異的な抗原分子の放出を促進し、次いでこれが体液中でアルファ(2)マクログロブリンと複合体を形成する。
Claims (11)
- 精製されたアルファ(2)マクログロブリン-抗原分子複合体を含む組成物をインビトロで製造する方法であって、
(a) アルファ(2)マクログロブリン-抗原分子複合体を、前癌状態の病変または癌性腫瘍を有する哺乳類の血清から精製するステップであって、前記複合体が、(i) 前記血清中に見出され前記血清に由来し、(ii)治療上有効量の前記複合体の製剤化を可能にする少なくとも1μgの量で前記血清から精製され、(iii) それぞれ前記前癌状態の病変または前記癌性腫瘍の抗原性を有する抗原分子を含む、前記ステップ;ならびに
(b) 前記治療上有効量の精製されたアルファ(2)マクログロブリン-抗原分子複合体を許容される医薬担体中に製剤化するステップ
を含み、前記治療上有効量が単位用量当り1μg〜5mgである、前記方法。 - アルファ(2)マクログロブリン-抗原分子複合体を前記血清から精製するステップが、
(a) アルファ(2)マクログロブリン-結合分子を含む固相を、前記アルファ(2)マクログロブリン-抗原分子複合体が前記固相に結合するのに十分な時間にわたって前記血清と接触させること;
(b) 前記固相と結合しなかった物質を除去すること;および
(c) 前記固相から前記結合したアルファ(2)マクログロブリン-抗原分子複合体を溶離すること
を含み、前記アルファ(2)マクログロブリン-結合分子がアルファ(2)マクログロブリンに特異的な抗体またはCD91のリガンド結合断片である、請求項1に記載の方法。 - 前記精製ステップがアルファ(2)マクログロブリン-抗原分子複合体を濃縮するために前記血清を分画するステップを含む、請求項1または2に記載の方法。
- 前記精製ステップが陰イオンまたは陽イオン交換クロマトグラフィーを使用することを含む、請求項1に記載の方法。
- 前記精製ステップがレクチンクロマトグラフィーを使用することを含む、請求項1に記載の方法。
- 前記精製ステップがアフィニティークロマトグラフィーを使用することを含む、請求項1に記載の方法。
- 前記精製ステップがフィルター結合分離技術を使用することを含む、請求項1に記載の方法。
- 前記血清を、アルファ(2)マクログロブリンと抗原分子の間の共有結合形成を促進する薬物と混合するステップをさらに含み、前記薬物がプロテアーゼ、アンモニア、メチルアミンまたはエチルアミンである、請求項1〜7のいずれか1項に記載の方法。
- 前記許容される医薬担体が生理的に許容される溶液である、請求項1〜8のいずれか1項に記載の方法。
- 前記哺乳類が前記癌性腫瘍を有し、前記複合体が前記癌性腫瘍の抗原性を有する抗原分子を含む、請求項1〜9のいずれか1項に記載の方法。
- 前記哺乳類がヒトである、請求項1〜10のいずれか1項に記載の方法。
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US20060165710A1 (en) | 2006-07-27 |
EP1601756A2 (en) | 2005-12-07 |
US20150118253A1 (en) | 2015-04-30 |
WO2004074454A2 (en) | 2004-09-02 |
WO2004074454A3 (en) | 2006-12-07 |
EP1601756B1 (en) | 2010-12-15 |
DE602004030541D1 (de) | 2011-01-27 |
AU2004213855A1 (en) | 2004-09-02 |
ATE491463T1 (de) | 2011-01-15 |
US8877204B2 (en) | 2014-11-04 |
AU2004213855B2 (en) | 2010-03-04 |
US9566348B2 (en) | 2017-02-14 |
ES2385933T3 (es) | 2012-08-03 |
JP2007524580A (ja) | 2007-08-30 |
EP1601756A4 (en) | 2007-10-24 |
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