Simson J A, Condon J L, Chao L, Chao J
Department of Anatomy and Cell Biology, Medical University of South Carolina, Charleston 29425.
J Histochem Cytochem. 1988 Oct;36(10):1251-4. doi: 10.1177/36.10.3418106.
Tissue kallikrein (E.C. 3.4.21.35) and arginine esterase A, another closely related, kinin-generating serine protease, have been localized by immunocytochemistry in rat kidney, using monoclonal antibodies that do not crossreact with other kallikrein-related enzymes or with tonin. Kallikrein was present primarily in the apical cytoplasm of the connecting tubule and the cortical collecting duct. Esterase A, on the other hand, was present primarily in the basolateral region of both proximal and distal straight tubules in the outer medulla and medullary rays. In addition, esterase A was demonstrable in distal convoluted tubules and, to a lesser extent, in proximal convoluted tubules. The presence of different kinin-generating enzymes at these sites would permit the formation of kinins from appropriate substrates on both the vascular and luminal poles of separate segments of the kidney tubule.
组织激肽释放酶(E.C. 3.4.21.35)和精氨酸酯酶A是另一种密切相关的激肽生成丝氨酸蛋白酶,利用不与其他激肽释放酶相关酶或肾素发生交叉反应的单克隆抗体,通过免疫细胞化学法已将它们定位在大鼠肾脏中。激肽释放酶主要存在于连接小管和皮质集合管的顶端细胞质中。另一方面,酯酶A主要存在于外髓质和髓放线中近端和远端直小管的基底外侧区域。此外,在远曲小管中可检测到酯酶A,在近曲小管中也有较少程度的表达。这些部位存在不同的激肽生成酶,这将使得在肾小管不同节段的血管极和管腔极由合适的底物形成激肽。