Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Role of MARCKS in regulating endothelial cell proliferation
Autore:
Zhao, Y; Neltner, BS; Davis, HW;
Indirizzi:
Univ Cincinnati, Med Ctr, Dept Internal Med Pulm & Crit Care Med, Cincinnati, OH 45267 USA Univ Cincinnati Cincinnati OH USA 45267 are Med, Cincinnati, OH 45267 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
fascicolo: 5, volume: 279, anno: 2000,
pagine: C1611 - C1620
SICI:
0363-6143(200011)279:5<C1611:ROMIRE>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; GROWTH-FACTOR; SUBSTRATE MARCKS; SIGNALING PATHWAY; SMOOTH-MUSCLE; PROTEOLYTIC CLEAVAGE; CALMODULIN-BINDING; 3T3 CELLS; PHOSPHORYLATION; FIBROBLASTS;
Keywords:
myristoylated alanine-rich C kinase substrate; vascular endothelial growth factor; actin; myosin light chain phosphorylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Zhao, Y Univ Cincinnati, Med Ctr, Dept Internal Med, Div Immunol, POB 670563, Cincinnati, OH 45267 USA Univ Cincinnati POB 670563 Cincinnati OH USA 45267 i, OH 45267 USA
Citazione:
Y. Zhao et al., "Role of MARCKS in regulating endothelial cell proliferation", AM J P-CELL, 279(5), 2000, pp. C1611-C1620

Abstract

Myristoylated alanine-rich C kinase substrate (MARCKS), as a specific protein kinase C (PKC) substrate, mediates PKC signaling through its phosphorylation and subsequent modification of its association with filamentous actin(F-actin) and calmodulin (CaM). PKC has long been implicated in cell proliferation, and recent studies have suggested that MARCKS may function as a cell growth suppressor. Therefore, in the present study, we investigated MARCKS protein expression, distribution, and phosphorylation in preconfluent and confluent bovine pulmonary microvascular endothelial cells (BPMEC) in the presence or absence of the vascular endothelial growth factor (VEGF). In addition, we examined functional alterations of MARCKS in these cells by studying the association of MARCKS with F-actin and CaM-dependent myosin light chain (MLC) phosphorylation. Our results indicate that MARCKS protein is downregulated during BPMEC proliferation. Decreased MARCKS association withF-actin, increased actin polymerization, and CaM-dependent MLC phosphorylation appear to mediate cell shape changes and motility during BPMEC growth. In contrast, VEGF stimulated MARCKS phosphorylation without alteration of protein expression during BPMEC proliferation, which may result in reduced interaction between MARCKS and actin or CaM, leading to actin reorganization and MLC phosphorylation. Our data suggest a regulatory role of MARCKS during endothelial cell proliferation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 21:40:19