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1988年已证实内皮素(endothelin,ET)为一种血管收缩肽,它由血管内皮产生,对平滑肌具有强力而持久的收缩作用,其后又阐明该肽不仅对血管平滑肌而且对各种器官均具有广泛的生理活性,并证实不仅内皮细胞而且某些神经细胞及肾小管上皮细胞亦可产生该肽。已知内皮素为三种结构及活性不同的ET-1、ET-2及ET-3所组成,ET-1、ET-2及ET-3前体分别由211、145、及238个氨基酸组成,并且分别含有由38、37及41个氨基酸组成的中间体,即大ET-1、大ET-2及大ET-3。这些大ET的C末端延长部分无生理活性,经ET转换酶(ECE)作用后,才转变为具有活性的ET。菅野等发现,在中性条件下内皮细胞匀浆中存
It has been demonstrated in 1988 that endothelin (ET) is a vasoconstrictor peptide produced by the vascular endothelium and having a potent and long-lasting contractile effect on the smooth muscle, and later elucidating that the peptide is not only specific to vascular smooth muscle but also to various organs Has a wide range of physiological activity and confirmed that not only endothelial cells but also some nerve cells and tubular epithelial cells can also produce the peptide. Endothelin is known to be composed of three structures and activities of ET-1, ET-2 and ET-3, and ET-1, ET-2 and ET-3 precursors consist of 211, 145, and 238 amino acids, respectively , And contain intermediates consisting of 38, 37 and 41 amino acids, namely Grand ET-1, Grand ET-2 and Grand ET-3, respectively. These large ET C-terminal extension of part of the non-physiological activity, the role of ET converting enzyme (ECE), was transformed into an active ET. Kanno found that under neutral conditions, endothelial cell homogenates exist