Nakagawa O, Nakao K, Saito Y, Shirakami G, Jougasaki M, Mukoyama M, Hosoda K, Suga S, Ogawa Y, Kishimoto I
Department of Medicine, Kyoto University School of Medicine, Japan.
J Cardiovasc Pharmacol. 1991;17 Suppl 7:S13-6. doi: 10.1097/00005344-199100177-00005.
Two endogenous molecules possessing an endothelin-like sequence with an apparent molecular weight of 7 kDa were isolated from serum-free culture medium of porcine aortic endothelial cells, using a specific radioimmunoassay. N-terminal sequences of two molecules were identical to each other and were Ser-Leu-Lys-Asp-Leu-Phe-Pro-Ala-Lys-Ala-Ala-Asp-Arg-Arg-Asp-Arg-X-Gln-X- Ala-X- Gln-Lys-Asp, which corresponds to the sequence [94-117] of preproendothelin-1. This finding indicates that these two molecules may be closely related peptides such as the oxidized form or disulfide analogues and also suggests that the endogenous peptide possessing an endothelin-like sequence is generated by proteolytic cleavage at paired basic amino acids Arg92-Arg93. Further studies on the structure and function of new endogenous peptides possessing an endothelin-like sequence are ongoing in our laboratory.
利用特异性放射免疫分析法，从猪主动脉内皮细胞的无血清培养基中分离出了两种内源性分子，其具有类内皮素序列，表观分子量为7 kDa。这两种分子的N端序列彼此相同，为Ser-Leu-Lys-Asp-Leu-Phe-Pro-Ala-Lys-Ala-Ala-Dsp-Arg-Arg-Asp-Arg-X-Gln-X-Ala-X-Gln-Lys-Asp，该序列对应于前内皮素-1的[94-117]序列。这一发现表明，这两种分子可能是如氧化形式或二硫键类似物等密切相关的肽，也提示具有类内皮素序列的内源性肽是通过在成对碱性氨基酸Arg92-Arg93处进行蛋白水解切割产生的。我们实验室正在对具有类内皮素序列的新内源性肽的结构和功能进行进一步研究。
