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Titolo:
INVOLVEMENT OF PROTEIN PHOSPHATASE-1 IN CYTOSKELETAL ORGANIZATION OF CULTURED ENDOTHELIAL-CELLS
Autore:
SHINOKI N; SAKON M; KAMBAYASHI J; IKEDA M; OIKI E; OKUYAMA M; FUJITANI K; YANO Y; KAWASAKI T; MONDEN M;
Indirizzi:
OSAKA UNIV,SCH MED,DEPT SURG 2,2-2 YAMADAOKA,SUITA 1 SUITA OSAKA 565 JAPAN OSAKA UNIV,SCH MED,CENT LAB RES & EDUC SUITA OSAKA 565 JAPAN
Titolo Testata:
Journal of cellular biochemistry
fascicolo: 3, volume: 59, anno: 1995,
pagine: 368 - 375
SICI:
0730-2312(1995)59:3<368:IOPPIC>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMOOTH-MUSCLE CALPONIN; KINASE-C SUBSTRATE; CALYCULIN-A; OKADAIC ACID; MYOSIN PHOSPHORYLATION; 3T3 FIBROBLASTS; INHIBITORS; ACTIN; NEUTROPHILS; INCREASES;
Keywords:
CALYCULIN A; PROTEIN PHOSPHATASE; CYTOSKELETON; ENDOTHELIAL CELL; IMMUNOCYTOCHEMISTRY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
29
Recensione:
Indirizzi per estratti:
Citazione:
N. Shinoki et al., "INVOLVEMENT OF PROTEIN PHOSPHATASE-1 IN CYTOSKELETAL ORGANIZATION OF CULTURED ENDOTHELIAL-CELLS", Journal of cellular biochemistry, 59(3), 1995, pp. 368-375

Abstract

The phosphorylation and dephosphorylation of cytoskeletal proteins regulate the shape of eukaryotic cells. To elucidate the role of serine/threonine protein phosphatases (PP) in this process, we studied the effects of calyculin A (CLA), a potent and specific inhibitor of proteinphosphatases 1 (PP-1) and 2A (PP-2A) on the cytoskeletal structure ofcultured human umbilical vein endothelial cells (HUVECs). The addition of CLA (5 min) caused marked alterations in cell morphology, such ascell constriction and bleb formation. Microtubules and F-actin were reorganized, becoming markedly condensed around the nucleus. Although the fluorescence intensity of phosphoamino acids was not significantly different according to immunocytochemistry between cells with and without CLA, polypeptides of 135, 140, 158, and 175 kDa were specifically phosphorylated on serine and/or threonine residues. There was no significant effect on tyrosine residues. The effects of CLA on cytoskeletalchanges and protein phosphorylation were almost completely inhibited by the non-selective kinase inhibitor, K-252a. The effect of CLA on cell morphology was at least 100 times more potent than that of okadaic acid, consistent with the inhibitory potency against PP-1. The catalytic subunit of PP-1 was also identified in HUVECs by Western blotting with its monoclonal antibody. These results suggest that PP-1 is closely involved in sustaining the normal structure of the cytoskeleton. (C)1995 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 18:28:41