Catalogo Articoli (Spogli Riviste)

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Titolo:
Activation of protein kinase C modulates cell-cell and cell-substratum adhesion of a human colorectal carcinoma cell line and restores 'normal' epithelial morphology
Autore:
Cowell, HE; Garrod, DR;
Indirizzi:
Univ Manchester, Sch Biol Sci, Epithelial Morphogenesis Res Grp, Manchester Univ Manchester Manchester Lancs England M13 9PT esis Res Grp, Manchester
Titolo Testata:
INTERNATIONAL JOURNAL OF CANCER
fascicolo: 3, volume: 80, anno: 1999,
pagine: 455 - 464
SICI:
0020-7136(19990129)80:3<455:AOPKCM>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
MONOCLONAL-ANTIBODIES; RAT-BRAIN; EXPRESSION; ZETA; PHOSPHORYLATION; LOCALIZATION; CYTOSKELETON; FIBRONECTIN; CULTURE; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Garrod, DR Univfordchester, Sch Biol Sci, Epithelial Morphogenesis Res Grp, 3-239 Stop Univ Manchester 3-239 Stopford Bldg Manchester Lancs England M13 9PT
Citazione:
H.E. Cowell e D.R. Garrod, "Activation of protein kinase C modulates cell-cell and cell-substratum adhesion of a human colorectal carcinoma cell line and restores 'normal' epithelial morphology", INT J CANC, 80(3), 1999, pp. 455-464

Abstract

Abnormal cell adhesion is an important contributing factor in invasion andmetastasis. Here, we show that morphologically 'normal' cell-cell and cell-substratum adhesion can be restored to a poorly differentiated carcinoma cell line by activation of protein kinase C (PKC). This cell line, VACO IONS, grows as multicellular aggregates loosely attached to the substratum. Thephorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA, 7.5 nM) induces rapid adhesive changes with 2 components. First, within 15 min of TPA the cells become closely apposed, an event resembling the 'compaction' seen in the mouse early embryo. Next, over 2 hr, the cells spread, forming a monolayer. We show that compaction depends on extracellular calcium, E-cadherin-mediated adhesion and F-actin but not on protein synthesis, microtubules or substratum adhesion. By contrast, cell spreading is independent of cadherin and extracellular Ca2+ but involves the formation of focal contacts containing av integrin. TPA treatment causes rapid translocation of PKC-or to the insoluble fraction. During compaction, actin- and PKC-alpha-containing lamellae form over the entire aggregate surface, those adjacent to the substratum appearing to initiate spreading. Compaction does not involve increased phosphorylation of the cadherin/catenin complex. We conclude that activation of PKC-alpha restores 'normal' morphology to these poorly differentiated cells. Our results are of general interest in relation to the regulation of cell adhesion and, through further investigation, may lead to identificationof novel targets for therapeutic suppression of invasion and metastasis. (C) 1999 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 10:58:33