Cacalano N A, Chen B X, Cleveland W L, Erlanger B F
Department of Microbiology, Columbia University, New York, NY 10032.
Proc Natl Acad Sci U S A. 1992 May 15;89(10):4353-7. doi: 10.1073/pnas.89.10.4353.
Cyclosporin A (CsA) is an immunosuppressive agent that inhibits the synthesis of lymphokines by T lymphocytes at the level of transcription. A cytoplasmic protein, cyclophilin, is the most thoroughly studied CsA-binding protein, but its ubiquitous presence in cells of all types raises questions about its role in immunosuppression. In an attempt to ascertain the presence of a cell surface receptor, we synthesized two polyvalent macromolecular CsA derivatives, CsA-BBa-ovalbumin and CsA-BBa-aminodextran (CBD), from the product of the photochemical reaction of CsA and 4-benzoylbenzoic acid (CsA-BBa). (i) They inhibited the peptidylprolyl cis-trans isomerase activity of cyclophilin and the synthesis of interleukin 2 by phorbol ester-activated EL-4 cells. (ii) CBD also inhibited interleukin 2 secretion by Con A-activated T-cell-enriched mouse splenocytes. 4-Benzoylbenzoic acid (BBa)-aminodextran and aminodextran were inactive. (iii) Direct binding and competition studies with [3H]CsA indicated that CBD does not enter EL-4 cells (i.e., it acted at the surface). (iv) CBD caused agglutination of EL-4 cells, murine B and T lymphocytes, human thymocytes, and two T-cell hybridomas. Agglutination was inhibited by a monoclonal antibody to CsA and by CsA and CsA-BBa, but not by BBa. No agglutination was seen with BBa-aminodextran or aminodextran. HeLa cells, Vero (monkey kidney) cells, a mouse plasmacytoma, COS cells, and a poorly differentiated B-cell lymphoma were not agglutinated. (v) EL-4 cells failed to be agglutinated after treatment with trypsin or chymotrypsin. Specific agglutination was again possible after incubation for 5 h at 37 degrees C in the absence of enzyme. (vi) CBD covalently linked to crosslinked agarose beads inhibited interleukin 2 production by phorbol ester-stimulated EL-4 cells. No activity was seen if cell-to-bead contact was prevented by a 0.02-microns microporous filter that did not interfere with the passage of CBD. Our findings support the presence of a functional receptor on the surface of selected cells of the immune system.
环孢素A(CsA)是一种免疫抑制剂,可在转录水平抑制T淋巴细胞合成淋巴因子。一种细胞质蛋白亲环蛋白是研究最深入的CsA结合蛋白,但其在所有类型细胞中的普遍存在引发了对其在免疫抑制中作用的质疑。为了确定细胞表面受体的存在,我们从CsA与4-苯甲酰苯甲酸(CsA-BBa)的光化学反应产物合成了两种多价大分子CsA衍生物,即CsA-BBa-卵清蛋白和CsA-BBa-氨基葡聚糖(CBD)。(i)它们抑制了亲环蛋白的肽基脯氨酰顺反异构酶活性以及佛波酯激活的EL-4细胞中白细胞介素2的合成。(ii)CBD还抑制了刀豆蛋白A激活的富含T细胞的小鼠脾细胞分泌白细胞介素2。4-苯甲酰苯甲酸(BBa)-氨基葡聚糖和氨基葡聚糖无活性。(iii)用[3H]CsA进行的直接结合和竞争研究表明,CBD不会进入EL-4细胞(即,它作用于细胞表面)。(iv)CBD导致EL-4细胞、小鼠B和T淋巴细胞、人胸腺细胞以及两种T细胞杂交瘤发生凝集。凝集被抗CsA单克隆抗体、CsA和CsA-BBa抑制,但不被BBa抑制。BBa-氨基葡聚糖或氨基葡聚糖未观察到凝集现象。HeLa细胞、Vero(猴肾)细胞、小鼠浆细胞瘤、COS细胞和低分化B细胞淋巴瘤未发生凝集。(v)用胰蛋白酶或糜蛋白酶处理后,EL-4细胞未能发生凝集。在无酶条件下于37℃孵育5小时后,再次可能发生特异性凝集。(vi)与交联琼脂糖珠共价连接的CBD抑制了佛波酯刺激的EL-4细胞产生白细胞介素2。如果用不干扰CBD通过的0.02微米微孔滤膜阻止细胞与珠子接触,则未观察到活性。我们的研究结果支持免疫系统特定细胞表面存在功能性受体。