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Titolo:
Heregulin-dependent trafficking and cleavage of ErbB-4
Autore:
Zhou, WL; Carpenter, G;
Indirizzi:
Vanderbilt Univ, Med Ctr, Sch Med, Dept Biochem, Nashville, TN 37232 USA Vanderbilt Univ Nashville TN USA 37232 t Biochem, Nashville, TN 37232 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 44, volume: 275, anno: 2000,
pagine: 34737 - 34743
SICI:
0021-9258(20001103)275:44<34737:HTACOE>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPIDERMAL GROWTH-FACTOR; AMYLOID PRECURSOR PROTEIN; FACTOR RECEPTOR ACTIVATION; ALPHA-SECRETASE CLEAVAGE; MEMBRANE DOMAINS; SIGNALING NETWORK; CARDIAC MYOCYTES; BREAST-CANCER; MESSENGER-RNA; MAMMARY-GLAND;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Carpenter, G Vanderbilt Univ, Med Ctr, Sch Med, Dept Biochem, 647 Light Hall,23rd Ave SPierce, Nashville, TN 37232 USA Vanderbilt Univ 647 Light Hall,23rd Ave S Pierce Nashville TN USA 37232
Citazione:
W.L. Zhou e G. Carpenter, "Heregulin-dependent trafficking and cleavage of ErbB-4", J BIOL CHEM, 275(44), 2000, pp. 34737-34743

Abstract

Heregulin was shown to promote the proteolytic cleavage of its receptor, ErbB-4, in several cell lines. The growth factor also rapidly promoted the transient translocation of ErbB-4 to a detergent-insoluble fraction, in which the receptor was hyper-tyrosine-phosphorylated compared with the receptorpresent in the detergent-soluble pool. However, an 80-kDa proteolytic fragment of ErbB-4 was found in the detergent soluble fraction, but not in the detergent-insoluble fraction. Although the heregulin-induced cleavage of ErbB-4 produced a fragment of ErbB-4 very similar to that induced by 12-O-tetradecanoylphorbol-13-acetate or pervanadate teach of which is blocked by metalloprotease inhibitors), the growth factor-induced cleavage was not sensitive to these inhibitors under the same conditions. The heregulin-induced cleavage of ErbB-4 could be blocked by conditions that prevent clathrin-coated pit formation, suggesting that heregulin-mediated ErbB-4 cleavage occurssubsequent to internalization. When reagents that prevent acidification ofendosomes were employed, heregulin-induced ErbB-4 cleavage was sensitive to metalloprotease inhibitors. The results imply that during ligand-dependent receptor trafficking, activated ErbB-4 receptors are subject to proteolytic cleavage involving an intracellular metalloprotease.

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Documento generato il 08/04/20 alle ore 11:16:30