Premium
Purification of the skeletal muscle protein Endopin 1B and characterization of the genes encoding Endopin 1A and 1B isoforms
Author(s) -
Herrera-Mendez Carlos H.,
Brémaud Laure,
Coulis Gerald,
Pélissier Patrick,
Sentandreu Miguel A.,
Aubry Laurent,
Delourme Didier,
Chambon Christophe,
Maftah Abderrahman,
Leveziel Hubert,
Ouali Ahmed
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.04.099
Subject(s) - serpin , complementary dna , microbiology and biotechnology , gene isoform , biochemistry , peptide sequence , gene , biology , trypsin , chymotrypsin , exon , proteases , amino acid , coding region , protease , chemistry , enzyme
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 43 808 Da. 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 ∼ 10 6 − 10 7 M −1 s −1 ) suggested that these serpins might play a major role in inflammatory processes.