Ryan U S, Ryan J W, Habliston D L, Pena G A
Adv Exp Med Biol. 1979;120B:275-86.
Endothelial cells are a major source of kininase enzymes including kininase II. Kininase II is situated along the plasma membrane, not as an ecto-enzyme but as an enzyme synthesized by the endothelial cells themselves. However, it is likely that endothelial cells do more than degrade kinins. These cells are contractile and may possess kinin receptors; a possibility supported by the fact that kinins stimulate endothelial cells to form and release prostaglandin-related substances. In addition, we have found that endothelial cells in culture are reactive with antibodies to alpha 2-macroglobulin. Endothelial cells can hydrolyze [3H]Pro-Phe-Arg-anilide, a kallikrein substrate, but the reaction is not inhibited by soya bean trypsin inhibitor (SBTI) or Trasylol. Possibly kallikrein or a related trypsin-like enzyme is bound to alpha 2-macroglobulin and is not free to react with the inhibitors. Thus, endothelial cells can bind and inhibit kallikrein-like enzymes, degrade kinins and respond to kinin stimulation.
内皮细胞是包括激肽酶II在内的激肽酶的主要来源。激肽酶II位于质膜上,不是作为一种外切酶,而是作为内皮细胞自身合成的一种酶。然而,内皮细胞可能不仅仅是降解激肽。这些细胞具有收缩性,可能拥有激肽受体;激肽刺激内皮细胞形成并释放前列腺素相关物质这一事实支持了这种可能性。此外,我们发现培养中的内皮细胞与抗α2-巨球蛋白抗体发生反应。内皮细胞可以水解[3H]Pro-Phe-Arg-苯胺,一种激肽释放酶底物,但该反应不受大豆胰蛋白酶抑制剂(SBTI)或抑肽酶的抑制。可能激肽释放酶或一种相关的类胰蛋白酶与α2-巨球蛋白结合,不能自由地与抑制剂反应。因此,内皮细胞可以结合并抑制类激肽释放酶,降解激肽并对激肽刺激作出反应。