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Conversion of big endothelin‐1 to endothelin‐1 by two types of metalloproteinases derived from porcine aortic endothelial cells
Author(s) -
Matsumura Yasuo,
Ikegawa Ruriko,
Tsukahara Yaeko,
Takaoka Masanori,
Morimoto Shiro
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80475-x
Subject(s) - phosphoramidon , cytosol , chemistry , endothelin 1 , incubation , endothelin receptor , metalloproteinase , membrane , radioimmunoassay , cleavage (geology) , matrix metalloproteinase , biochemistry , biology , enzyme , receptor , paleontology , fracture (geology)
Incubation of big endothelin‐1 (big ET‐1 1–39 ) with either the cytosolic or membrane fraction obtained from cultured endothelial cells, resulted in an increase in immunoreactive‐endothelin (IR‐ET), which was markedly inhibited by metal chelators. Phosphoramidon, a metalloproteinase inhibitor, specifically suppressed the membrane fraction‐induced increase in IR‐ET, whereas the increase in IR‐ET observed with the cytosolic fraction was not influenced by phosphoramidon. Reverse‐phase (RP)‐HPLC of the incubation mixture of big ET‐1 with the cytosolic or membrane fraction revealed one major IR‐ET component corresponding to the elution position of synthetic ET‐1 1–21 . Simultaneously, immunoreactivities like the C‐terminal fragment (CTF 22–39 ) of big ET‐1 were present, as deduced from the RP‐HPLC coupled with the radioimmunoassay for CTF. Our results indicate the presence of two types of metalloproteinases, which convert big ET‐1 to ET‐1 via a single cleavage between Trp 21 and Val 22 , in vascular endothelial cells.