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Titolo:
PTP1B regulates neurite extension mediated by cell-cell and cell-matrix adhesion molecules
Autore:
Pathre, P; Arregui, C; Wampler, T; Kue, I; Leung, TC; Lilien, J; Balsamo, J;
Indirizzi:
Wayne State Univ, Dept Sci Biol, Detroit, MI USA Wayne State Univ DetroitMI USA ate Univ, Dept Sci Biol, Detroit, MI USA Univ Iowa, Dept Biol Sci, Iowa City, IA 52242 USA Univ Iowa Iowa City IA USA 52242 , Dept Biol Sci, Iowa City, IA 52242 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE RESEARCH
fascicolo: 2, volume: 63, anno: 2001,
pagine: 143 - 150
SICI:
0360-4012(20010115)63:2<143:PRNEMB>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE-PHOSPHATASE; GROWTH CONE GUIDANCE; INSULIN-RECEPTOR; N-CADHERIN; FOCAL ADHESIONS; HUMAN PLATELETS; AXON GUIDANCE; 1B INTERACTS; LAR; ASSOCIATION;
Keywords:
N-cadherin; beta 1-integrin; tyrosine phosphatase; PTP1B; neurite outgrowth;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Lilien, J Univ Iowa, Dept Sci Biol, Iowa City, IA 52246 USA Univ Iowa Iowa City IA USA 52246 Biol, Iowa City, IA 52246 USA
Citazione:
P. Pathre et al., "PTP1B regulates neurite extension mediated by cell-cell and cell-matrix adhesion molecules", J NEUROSC R, 63(2), 2001, pp. 143-150

Abstract

N-cadherin and beta1-integrin adhesion and signaling play important roles in growth cone adhesion and guidance. Each of these adhesion receptor systems is composed of multiprotein complexes, and both adhesion and downstream signaling events are regulated through the interaction of protein tyrosine kinases and phosphatases with many of the proteins that make up these complex systems. Work from our laboratory reported that the nonreceptor protein tyrosine phosphatase PTP1B is localized to adherens junctions and focal adhesion complexes and regulates both N-cadherin- and beta1-integrin-mediated adhesion. PTP1B appears to modulate integrin-mediated adhesion through regulation of src activation and cadherin-mediated adhesion through dephosphorylation of beta -catenin. We have continued these studies and report that PTP1B is localized to the tips of growing neurites and that introduction of anoncatalytic mutant of PTP1B into PC12 cells results in inhibition of N-cadherin- and beta1-integrin-mediated neurite outgrowth but is without effecton neurite outgrowth on poly-L-lysine. Moreover, suppressing the level of PTP1B in primary embryonic chick neural retina cells using antisense oligonucleotides also inhibits N-cadherin- and beta1-integrin-mediated neurite outgrowth. Neither of these techniques reduces the levels of expression of either adhesion receptor. We conclude that PTP1B is a regulatory component ofthe molecular complex required for both N-cadherin and beta1-integrin-mediated axon growth. (C) 2001 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 20:09:50