Novel properties of peptides derived from the sequence coded by exon 26A of human elastin
Copyright policy )Novel properties of peptides derived from the sequence coded by exon 26A of human elastin
The exon 26A is a rarely expressed human elastin exon that codes for a hydrophilic and charged amino acid sequence. The functional role of elastin containing this additional sequence is unknown. The present investigation was aimed to determine the effect of synthetic peptides derived from this exon on the vascular tone of rat thoracic aorta. On phenilephrine-preconstricted rat thoracic aortic rings the peptides LSPELREGD and REGD cause dose-dependent relaxation in the concentration range from 10(-9) to 10(-5) M. omega-nitro-L-arginine methyl ester, a known inhibitor of the NO synthase, highly inhibits, although to a different extent, the relaxation induced by these peptides. Removal of endothelium and blocking of ATP-sensitive potassium channels by glibenclamide significantly inhibited the vasorelaxant activity of LSPELREGD but not that of REGD, suggesting a different mechanism of action and possibly a different receptor.
- University of Basilicata Italy
- University of Bari Aldo Moro Italy
Male, Lactose, In Vitro Techniques, Exon 26A, Models, Biological, Nitroarginine, Muscle, Smooth, Vascular, Phenylephrine, Human elastin, Glyburide, Potassium Channel Blockers, Animals, Humans, Hypoglycemic Agents, Vasorelaxant activity, 4-Aminopyridine, Enzyme Inhibitors, Aorta, Dose-Response Relationship, Drug, Exons, Elastin, Rats, Peptides
Male, Lactose, In Vitro Techniques, Exon 26A, Models, Biological, Nitroarginine, Muscle, Smooth, Vascular, Phenylephrine, Human elastin, Glyburide, Potassium Channel Blockers, Animals, Humans, Hypoglycemic Agents, Vasorelaxant activity, 4-Aminopyridine, Enzyme Inhibitors, Aorta, Dose-Response Relationship, Drug, Exons, Elastin, Rats, Peptides
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