Role of mast cell chymase in the extracellular processing of big-endothelin-1 to endothelin-1 in the perfused rat lung
作者： Donna M. Wypij , James S. Nichols , Paul J. Novak , D. Lowell Stacy , Judd Berman
DOI: 10.1016/0006-2952(92)90252-E
关键词: Compound 48/80 、 Extracellular 、 Degranulation 、 Phosphoramidon 、 Pharmacology 、 Mast cell 、 Biology 、 Histamine 、 Endocrinology 、 Chymase 、 Internal medicine 、 Endothelin 1
摘要: Abstract Previous studies of endothelin-1 (ET) synthesis have shown that some cultured endothelial cells secrete an intermediate product, big-endothelin-1 (bigET), suggesting the processing secreted bigET to ET may be physiologically significant. In this study, two pertinent converting enzyme activities, mast cell chymase I (EC 3.4.21.39) and a phosphoramidon-sensitive, neutral metalloprotease, were identified in rat lung particulate fraction. We perfused lungs with chymostatin or phosphoramidon study relevance these proteases extracellular vivo . Addition compound 48 80 (a which activates cells, causing degranulation release chymase) perfusion buffer greatly increased hydrolysis exogenously added ET.ET formation was inhibited completely by 32 μM chymostatin, whereas inhibition 50 incomplete variable. Perfusate histamine levels used monitor extent degranulation, production attributed per se There direct correlation between perfusate both control phosphoramidon-treated (but not chymostatin-treated) lungs. Our results suggest from is capable relevant lung.
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