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

FEBS Letters

Volumn 580, Issue 14, 2006, Pages 3477-3484

  Herrera Mendez, Carlos H ^a   Brémaud, Laure ^b   Coulis, Gerald ^a   Pélissier, Patrick ^b   Sentandreu, Miguel A ^a   Aubry, Laurent ^a   Delourme, Didier ^b   Chambon, Christophe ^c   Maftah, Abderrahman ^b   Leveziel, Hubert ^b   Ouali, Ahmed ^a  

^a UR370 QuaPA   (France)

^b UNIVERSITY OF LIMOGES   (France)

^c CEMAGREF   (France)

Author keywords

Bovine; Endopin 1A; Endopin 1B; Genes structure; Muscle; Serpin

Indexed keywords

CHYMOTRYPSIN; COMPLEMENTARY DNA; ELASTASE; ENDOPIN 1A; ENDOPIN 1B; MUSCLE PROTEIN; PLASMIN; PROTEINASE; SERINE PROTEINASE INHIBITOR; TRYPSIN; UNCLASSIFIED DRUG;

5' UNTRANSLATED REGION; AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; COW; DNA SEQUENCE; EXON; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SKELETAL MUSCLE;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CATTLE; CLONING, MOLECULAR; DNA PRIMERS; DNA, COMPLEMENTARY; ENZYME INHIBITORS; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; PANCREATIC ELASTASE; PROTEIN ISOFORMS; SEQUENCE HOMOLOGY, AMINO ACID; SERPINS; TRYPSIN;

BOS TAURUS;

EID: 33646935470     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.04.099     Document Type: Article

References (13)

1. Gettins P.G.W. Serpin structure, mechanism, and function. Chem. Rev. 102 (2002) 4751-4803
2. Hwang S.R., Steineckert B., Yasothornsrikul S., Sei C.A., Tonef T., Rattan J., and Hook V.Y.H. Molecular cloning of endopin 1, a novel serpin localized to neurosecretory vesicles of chromaffin cells. Inhibition of basic residue-cleaving proteases by endopin 1. J. Biol. Chem. 274 (1999) 34164-34173
3. Tassy C., Herrera-Mendez C.H., Sentandreu M.A., Aubry L., Bremaud L., Pelissier P., Delourme D., Brillard M., Gauthier F., Leveziel H., and Ouali A. Muscle endopin 1, a muscle intracellular serpin which strongly inhibits elastase: purification, characterization, cellular localization and tissue distribution. Biochem. J. 388 (2005) 273-280
4. Bige L., Ouali A., and Valin C. Purification and characterization of a low molecular weight cysteine proteinase inhibitor from bovine muscle. Biochim. Biophys. Acta 843 (1985) 269-275
5. Dutaud D., Aubry L., Henry L., Levieux D., Hendil K.B., Kueh L.N., Bureau J.P., and Ouali A. Development and evaluation of a sandwich ELISA for quantification of the 20S proteasome in human plasma. J. Immunol. Methods 260 (2002) 183-193
6. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
7. Marshall C.J. Evolutionary relationships among the serpins. Philos. Trans. R. Soc. Lond. B 342 (1993) 101-119
8. Hwang S.R., Kohn A.B., and Hook V.Y.H. Unique reactive site domains of neuroendocrine isoforms of alpha-l-antichymotrypsin from bovine adrenal medulla and pituitary revealed by molecular cloning. FEBS Lett. 368 (1995) 471-476
9. Hook V.H., Yasothornsrikul S., and Hwang S.R. Novel chromaffin granule serpins, endopin 1 and endopin 2: endogenous protease inhibitors with distinct target protease specificities. Ann. N. Y. Acad. Sci. 971 (2002) 426-444
10. Ragg H., Lokot T., Kamp P.B., Atchley W.R., and Dress A. Vertebrate serpins: construction of a conflict-free phylogeny by combining exon-intron and diagnostic site analyses. Mol. Biol. Evol. 18 (2001) 577-584
11. Bieth J.G. Some kinetic consequences of protein-proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants. In: Fritz H. (Ed). Bayer Symposium V: "Proteinase Inhibitors" (1974), Springer, Berlin 463-469
12. Hwang S.R., Stoka V., Turk V., and Hook V.Y.H. The novel bovine serpin endopin 2C demonstrates selective inhibition of the cysteine protease cathepsin L compared to the serine protease elastase, in cross-class inhibition. Biochemistry 44 (2005) 7757-7767
13. Stephens R.M., and Schneider T.D. Features of spliceosome evolution and function inferred from an analysis of the information at human splice sites. J. Mol. Biol. 228 (1992) 1124-1136