Funkhouser J D, Tangada S D, Jones M, O S J, Peterson R D
Department of Biochemistry, University of South Alabama College of Medicine, Mobile 36688.
Am J Physiol. 1991 Apr;260(4 Pt 1):L274-9. doi: 10.1152/ajplung.1991.260.4.L274.
A prominent membrane protein of rat type II alveolar cells, p146, was originally identified by one of many mouse monoclonal antibodies that were produced to rat lung cells in the course of a search for differentiation antigens that might prove useful in studying lung differentiation. We report here results from analysis of the primary structure of this molecule and, based on this knowledge, the elucidation of the function of the protein. Amino acid sequencing of the NH2-terminal portion of the p146 protein, plus partial sequencing of several peptides obtained by limited proteolysis, indicates it is identical to aminopeptidase N. Further, the immunoaffinity purified p146 protein has aminopeptidase N activity. The discussion includes references to other molecules such as CD 13 and CD 10 (CALLA) that were recognized as differentiation antigens and subsequently found to be peptidases. The possible biological implications of such a peptidase on the luminal surface of type II alveolar cells are also considered.
大鼠II型肺泡细胞的一种重要膜蛋白p146，最初是在寻找可能有助于研究肺分化的分化抗原过程中，由众多针对大鼠肺细胞产生的小鼠单克隆抗体之一鉴定出来的。我们在此报告对该分子一级结构的分析结果，并基于此知识阐明该蛋白质的功能。对p146蛋白NH2末端部分的氨基酸测序，加上对有限蛋白酶解获得的几种肽的部分测序，表明它与氨肽酶N相同。此外，免疫亲和纯化的p146蛋白具有氨肽酶N活性。讨论中还提及了其他分子，如CD 13和CD 10（CALLA），它们最初被识别为分化抗原，随后被发现是肽酶。还考虑了这种肽酶在II型肺泡细胞腔表面可能的生物学意义。
