Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
INTERACTION OF CALMODULIN-BINDING DOMAIN PEPTIDES OF NITRIC-OXIDE SYNTHASE WITH MEMBRANE PHOSPHOLIPIDS - REGULATION BY PROTEIN-PHOSPHORYLATION AND CA2-CALMODULIN()
Autore:
MATSUBARA M; TITANI K; TANIGUCHI H;
Indirizzi:
FUJITA HLTH UNIV,DIV BIOMED POLYMER SCI,INST COMPREHENS MED SCI TOYOAKE AICHI 47011 JAPAN FUJITA HLTH UNIV,DIV BIOMED POLYMER SCI,INST COMPREHENS MED SCI TOYOAKE AICHI 47011 JAPAN
Titolo Testata:
Biochemistry
fascicolo: 46, volume: 35, anno: 1996,
pagine: 14651 - 14658
SICI:
0006-2960(1996)35:46<14651:IOCDPO>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
KINASE-C SUBSTRATE; AORTIC ENDOTHELIAL-CELLS; PALMITOYLATION SITES; N-MYRISTOYLATION; MARCKS; ASSOCIATION; ENZYME; BRAIN; TRANSLOCATION; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
M. Matsubara et al., "INTERACTION OF CALMODULIN-BINDING DOMAIN PEPTIDES OF NITRIC-OXIDE SYNTHASE WITH MEMBRANE PHOSPHOLIPIDS - REGULATION BY PROTEIN-PHOSPHORYLATION AND CA2-CALMODULIN()", Biochemistry, 35(46), 1996, pp. 14651-14658

Abstract

Endothelial nitric oxide synthase (eNOS) is unique among the NO synthase isozymes in being modified with myristoyl group, which appears to be necessary for its membrane association. However, the presence of myristoylated eNOS in cytosolic fraction after the stimulation-dependenttranslocation of the enzyme from membrane to cytosol suggests that other regions may be involved in the eNOS-membrane interaction and its regulation. In this study, we have synthesized a 20-amino acid peptide corresponding to the putative calmodulin-binding domain of human eNOS and studied the interaction of the peptide with calmodulin and with various membrane phospholipids. The peptide formed a stoichiometric complex with calmodulin. Upon addition of various acidic phospholipids, the peptide showed a drastic conformational change from random coil to alpha-helix, as was evidenced by circular dichroism spectroscopy. Theseresults suggest that the same domain of eNOS binds both calmodulin and membrane phospholipids. Furthermore, we found that the synthetic peptide was phosphorylated in vitro by protein kinase C. Phosphorylation of the peptide decreased its interaction with membrane phospholipids. Thus, our results raise the possibility that the calmodulin-binding domain is directly involved in the membrane association of eNOS and thatphosphorylation of the domain and Ca2+-calmodulin may regulate the interaction. Synthetic peptides corresponding to the calmodulin-binding domains of macrophage and neuronal isozymes showed similar abilities to bind phospholipids, suggesting that the calmodulin-binding domains of NO synthase serve as the phospholipid-binding domains as well.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 20:54:33