Purification of the skeletal muscle protein Endopin 1B and characterization of the genes encoding Endopin 1A and 1B isoforms.

Abstract:

:In the present work, a new endopin-like serpin designed mEndopin 1B was purified from bovine muscle. Biochemical characterizations (amino acid sequencing and Maldi-Tof mass spectrometry peptide mapping) demonstrated that the purified protein is different from the previously described Endopin 1, renamed mEndopin 1A. The genes and cDNA of both endopins were characterized. The cDNA sequence of mEndopin 1B encodes a predicted protein of 411 amino-acids with a molecular mass of 43808Da. The mEndopin 1B gene comprised four coding exons and an additional 5' untranslated exon. The reactive site sequence of mEndopin 1B is somewhat different from that of mEndopin 1A. Nevertheless, both serpins have a similar peptidase inhibitory pattern against examined proteases (elastase, trypsin, plasmin and chymotrypsin). The high expression of both mEndopin 1A and 1B in bovine serum and tissues and their high efficiency to inhibit elastase (k(ass) approximately 10(6)-10(7) M(-1) s(-1)) suggested that these serpins might play a major role in inflammatory processes.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Herrera-Mendez CH,Brémaud L,Coulis G,Pélissier P,Sentandreu MA,Aubry L,Delourme D,Chambon C,Maftah A,Leveziel H,Ouali A

doi

10.1016/j.febslet.2006.04.099

subject

Has Abstract

pub_date

2006-06-12 00:00:00

pages

3477-84

issue

14

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)00615-6

journal_volume

580

pub_type

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