Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis
Autore:
Kainulainen, V; Sundvall, M; Maatta, JA; Santiestevan, E; Klagsbrun, M; Elenius, K;
Indirizzi:
Univ Turku, Medicity Res Labs, FIN-20520 Turku, Finland Univ Turku TurkuFinland FIN-20520 ty Res Labs, FIN-20520 Turku, Finland Univ Turku, Dept Pediat, FIN-20520 Turku, Finland Univ Turku Turku Finland FIN-20520 Dept Pediat, FIN-20520 Turku, Finland Univ Turku, Dept Med Biochem & Mol Biol, FIN-20520 Turku, Finland Univ Turku Turku Finland FIN-20520 & Mol Biol, FIN-20520 Turku, Finland Childrens Hosp, Dept Surg, Boston, MA 02115 USA Childrens Hosp Boston MA USA 02115 Hosp, Dept Surg, Boston, MA 02115 USA Childrens Hosp, Dept Pathol, Boston, MA 02115 USA Childrens Hosp Boston MA USA 02115 osp, Dept Pathol, Boston, MA 02115 USA Harvard Univ, Sch Med, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 vard Univ, Sch Med, Boston, MA 02115 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 12, volume: 275, anno: 2000,
pagine: 8641 - 8649
SICI:
0021-9258(20000324)275:12<8641:ANEITD>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR-RECEPTOR; PROTEIN-KINASE-B; PHOSPHATIDYLINOSITOL 3-KINASE; TYROSINE PHOSPHORYLATION; SIGNAL-TRANSDUCTION; PUTATIVE RECEPTORS; FAMILY MEMBERS; DNA-SYNTHESIS; 3-OH KINASE; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
84
Recensione:
Indirizzi per estratti:
Indirizzo: Elenius, K Univ Turku, Medicity Res Labs, Tykistokatu 6 A, FIN-20520 Turku, Finland Univ Turku Tykistokatu 6 A Turku Finland FIN-20520 ku, Finland
Citazione:
V. Kainulainen et al., "A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis", J BIOL CHEM, 275(12), 2000, pp. 8641-8649

Abstract

ErbB4 is a member of the epidermal growth factor receptor (ErbB) family that mediates cellular responses activated by neuregulins (NRG) and other epidermal growth factor-like growth factors. TWO naturally occurring ErbB4 isoforms, ErbB4 CYT-1 and ErbB4 CYT-2, have previously been identified. UnlikeErbB4 CYT-1, ErbB4 CYT-2 lacks a phosphoinositide 3-kinase (PIS-K)binding site and is incapable of activating PI3-K. We have now examined the consequences of the inability of this isoform to activate PI3-K on cell proliferation, survival, and chemotaxis in response to NRG-1 beta: (i) NRG-1 beta stimulated proliferation of cells expressing either ErbB4 CYT-1 or ErbB4 CYT-S, Consistent with the mitogenic responsiveness, analysis of downstream signaling showed that Shc and MAPK were phosphorylated after stimulating eitherisoform with NRG-1 beta. (ii) NRG-1 beta protected cells expressing ErbB4 CYT-1 but not cells expressing ErbB4 CYT-Q from starvation-induced apoptosis as measured by effects on cell number and 4',6-diamidino-2-phenylindole staining. Furthermore, in cells expressing ErbB4 CYT-2, Akt, a protein kinase that mediates cell survival, was not phosphorylated. (iii) NRG-1 beta stimulated chemotaxis and membrane ruffling in cells expressing ErbB4 CYT-1 but not in cells expressing ErbB4 CYT-8, In summary, ErbB4 CYT-8 can mediate proliferation but not chemotaxis or survival. These results suggest a novelmechanism by which cellular responses such as chemotaxis and survival may be regulated by the expression of alternative receptor-tyrosine kinase isoforms that differ in their coupling to PI3-K signaling.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/08/20 alle ore 20:39:13