Novel properties of peptides derived from the sequence coded by exon 26A of human elastin.
Int J Biochem Cell Biol
; 34(2): 130-5, 2002 Feb.
Article
in En
| MEDLINE
| ID: mdl-11809415
ABSTRACT
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Aorta
/
Peptides
/
Exons
/
Elastin
/
Muscle, Smooth, Vascular
Type of study:
Prognostic_studies
Limits:
Animals
/
Humans
/
Male
Language:
En
Journal:
Int J Biochem Cell Biol
Journal subject:
BIOQUIMICA
Year:
2002
Document type:
Article
Affiliation country:
Italy
Country of publication:
HOLANDA
/
HOLLAND
/
NETHERLANDS
/
NL
/
PAISES BAJOS
/
THE NETHERLANDS