1998
DOI: 10.1074/jbc.273.32.20589
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Tyrosine Phosphorylation and Proteolysis

Abstract: Enhancement of tyrosine phosphorylation in cells by the application of pervanadate, an extremely potent phosphotyrosine phosphatase inhibitor, provokes the rapid metalloprotease-dependent cleavage of ErbB-4, a transmembrane receptor tyrosine kinase. The pervanadate-induced proteolysis occurs in NIH 3T3 cells expressing transfected human ErbB-4 and in several cell lines that express endogenous ErbB-4. One product of this proteolytic event is a membrane-anchored molecule of approximately 80 kDa, which is heavily… Show more

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Cited by 80 publications
(43 citation statements)
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“…ErbB-4 receptor cleavage is greatly enhanced by the protein kinase C activator TPA or by pervanadate, a potent phosphotyrosine phosphatase inhibitor (19,20). These results suggest the presence of intracellular signaling pathways that can regulate this cleavage event.…”
mentioning
confidence: 68%
See 1 more Smart Citation
“…ErbB-4 receptor cleavage is greatly enhanced by the protein kinase C activator TPA or by pervanadate, a potent phosphotyrosine phosphatase inhibitor (19,20). These results suggest the presence of intracellular signaling pathways that can regulate this cleavage event.…”
mentioning
confidence: 68%
“…Fragment-To determine whether growth factor binding to the ErbB-4 receptor tyrosine kinase initiates proteolytic cleavage of this receptor, as previously reported for TPA (19) and pervanadate (20), several cell lines were surveyed. These included two breast carcinoma cell lines (T47D and SK-Br-3), three ovarian carcinoma cell lines (OVCAR3, OVCA432, and OVCA429), two lung carcinoma cell lines (H661 and H1155), one glioma cell line (C6), a mouse cardiomyocyte cell line (AT-1), and the NIH 3T3-derived cell line T47-14.…”
Section: Ligand-induced Accumulation Of the 80-kda Erbb-4mentioning
confidence: 99%
“…Treatment of NIH NC2 cells with 12-O-tetradecanoylphorbol-13-acetate (TPA) resulted in the accumulation of p20 TrkCNC2 in the cells, although to a lesser extent, as compared to NT-3 stimulation (Figure 3c). Since cleavage of several receptor tyrosine kinases have been described (Zupan et al, 1989;Cabrera et al, 1996;Vecchi et al, 1998), we performed parallel experiments on cells expressing the TrkC catalytic isoform. Untreated NIH K cells, maintained in 10% serum, do not express a truncated version of the catalytic receptor (Figure 1a).…”
Section: Cleavage Of the Noncatalytic Trkc Receptor S Mateos Et Almentioning
confidence: 99%
“…These growth factors are expressed at the cell surface as transmembrane proteins, yet can also be released as soluble growth factors as a result of their ectodomain shedding (12)(13)(14)(15)(16)(17). Both the soluble and the transmembrane forms of these growth factors can activate the receptors, i.e.…”
mentioning
confidence: 99%