Lack of biological activity of preproendothelin [110-130] in several endothelin assays.

Abstract:

:A 21 amino acid peptide containing the prepropendothelin sequence from amino acids 110 to 130 and two intrachain disulfide bonds was synthesized and tested for biological activity in the following endothelin assays: 1.) a competition binding assay using [125I]ET-1 and dog heart membranes, 2.) three RIA's using 125I-ET-1, -2 and -3 and the respective anti-ET rabbit antisera; and 3.) a contractile activity bioassay using hamster aortic rings. The synthetic peptide which has been referred to as the "endothelin-like" peptide occurs 36 amino acids C-terminal to endothelin in the prepro-protein sequence. It contains only 40% sequence homology to the three endothelin isoforms, but has the same sequence and cyclization pattern of cysteines at positions 1, 3, 11 and 15. Despite the overall similarity in secondary structure to the three isoforms of endothelin and sarafotoxin S6b, preproendothelin [110-130] had no activity in any of the assays when tested at concentrations of 10(-10)M to 10(-5)M.

journal_name

Life Sci

journal_title

Life sciences

authors

Cade C,Lumma WC Jr,Mohan R,Rubanyi GM,Parker-Botelho LH

doi

10.1016/0024-3205(90)90308-e

subject

Has Abstract

pub_date

1990-01-01 00:00:00

pages

2097-103

issue

23

eissn

0024-3205

issn

1879-0631

pii

0024-3205(90)90308-E

journal_volume

47

pub_type

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