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In an attempt to “bioassay” endothelium-derived relaxing factor (EDRF) produced by cultured bovine aortic endothelial cells, it was discovered by Hickey et al.7 that the conditioned medium contained a potent vasoconstrictor substance (see Chapter 2). Preliminary characterization revealed that the vasoconstrictor was a peptide, and analogous to EDRF, it was named “endothelium-derived contracting factor” (EDCF).7 This peptidergic EDCF was later isolated by Yanagisawa et al.20 and identified as a novel 21 amino acid peptide, endothelin. The peptide contains two intrachain disulfide bonds and is homologous to sarafotoxin S6b, a venom peptide isolated from an Israeli asp, Atractapsis engaddensis.11 In our brief summary of present knowledge of the cellular synthesis of this new peptide family, we emphasize the gene structure, regulation of gene expression, and biosynthesis of mature endothelin. |
