Ferro E S, Tambourgi D V, Gobersztejn F, Gomes M D, Sucupira M, Armelin M C, Kipnis T L, Camargo A C
Department of Pharmacology and Immunology, University of São Paulo, Brazil.
Biochem Biophys Res Commun. 1993 Feb 26;191(1):275-81. doi: 10.1006/bbrc.1993.1213.
An endopeptidase capable of metabolizing a number of neuropeptides and generating [Met5] and [Leu5] enkephalin from enkephalin-containing peptides is secreted by glioma C6 cells. This neutral endopeptidase that is likely to be a thiol protease, has a Mr of 71KDa and is effective only towards oligopeptides. Its specificity towards neuropeptides is identical to that of soluble endopeptidase 22.19. Moreover, when a partially purified preparation of enkephalin-generating enzyme secreted by glioma C6 cells was submitted to immunoblotting, an antiserum against purified brain endopeptidase 22.19 recognized a single band at Mr of 71 KDa. These data suggest that the soluble endopeptidase 22.19 may be secreted by glioma C6 cells thus allowing its participation in the biotransformation of opioid peptides in the CNS.
胶质瘤C6细胞分泌一种内肽酶，它能够代谢多种神经肽，并从含脑啡肽的肽中生成[Met5]脑啡肽和[Leu5]脑啡肽。这种中性内肽酶可能是一种巯基蛋白酶，分子量为71KDa，仅对寡肽有效。它对神经肽的特异性与可溶性内肽酶22.19相同。此外，当对胶质瘤C6细胞分泌的生成脑啡肽酶的部分纯化制剂进行免疫印迹时，针对纯化的脑内肽酶22.19的抗血清在分子量71KDa处识别出一条单一的条带。这些数据表明，可溶性内肽酶22.19可能由胶质瘤C6细胞分泌，从而使其参与中枢神经系统中阿片肽的生物转化。
