Induction of renal adenocarcinoma by a nonmutated erbB oncogene

Taglienti-Sian, C; Banner, Barbara F.; Davis, Roger J.; Robinson, Harriet L.

doi:10.1128/jvi.67.2.1132-1136.1993

Cited by 4 publications

(2 citation statements)

References 29 publications

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“…Independent isolates of the acutely transforming avian erythroblastosis virus (AEV) can induce tumor formation in more than one tissue type. The primary site of oncogenesis associated with AEV infection is the bone marrow, resulting in the development of erythroleukemia; however, fibrosarcomas, hemangiosarcomas, angiosarcomas, and renal adenocarcinomas can also occur in AEVinfected birds (17,31,38).…”

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Tissue- and transformation-specific phosphotyrosyl proteins in v-erbB-transformed cells

McManus

Connolly

Maihle

1995

J Virol

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To understand the mechanism of tissue-specific and transformation-specific signaling by the v-ErbB oncoprotein, we have investigated signaling pathways downstream of this transmembrane tyrosine kinase. In this report, we describe tissue-specific patterns of phosphotyrosyl proteins in three distinct cell types transformed by the v-erbB oncogene: fibroblasts, erythroblasts, and endothelial cells. In addition, we describe transformation-specific tyrosine phosphorylation events and signal complex formation in v-erbB-transformed fibroblasts. Two patterns of phosphotyrosyl proteins have been detected in v-erbB-transformed cells. The first is a fibroblast-specific pattern which includes unique phosphotyrosyl proteins of 170 kDa (c-ErbB1), 158 kDa, and 120 kDa (the catenin-like protein p120 cas). The second is an erythroblast/endothelial cell-specific pattern which includes a prominent unidentified phosphotyrosyl protein of 120 kDa. Evaluation of the phosphotyrosyl proteins p120 cas and SHC in chicken embryo fibroblasts infected with transforming and nontransforming v-erbB mutants reveals transformation-specific patterns of tyrosine phosphorylation. One corollary of these phosphorylation events in v-erbB-transformed fibroblasts is the formation of a complex involving SHC, growth factor receptor-bound protein 2, and a novel 75-kDa phosphotyrosyl protein. The results of these studies suggest that the v-ErbB oncoprotein can couple to multiple signal tranduction pathways, that these pathways are tissue specific, and that v-erbB-mediated transformation involves specific tyrosine phosphorylation events.

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confidence: 99%

Tissue- and transformation-specific phosphotyrosyl proteins in v-erbB-transformed cells

McManus

Connolly

Maihle

1995

J Virol

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“…Expression of this amino-terminally truncated receptor results in ligand-independent neoplastic transformation of avian erythrocyte precursors. Truncation of the ligand-binding domain in combination with short COOH-terminal deletions and/or internal deletions within the carboxyl-terminal domain further results in the induction of fibrosarcomas, angiosarcomas, renal adenocarcinomas, or hemangiomas (35,36,41,42).…”

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confidence: 99%

Tyrosine kinase activity may be necessary but is not sufficient for c-erbB1-mediated tissue-specific tumorigenicity

Connolly

Toutenhoofd

Maihle

1994

J Virol

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Expression of mutant avian c-erbBl genes results in tissue-specific transformation in chickens. Site-directed mutagenesis was used to generate kinase-defective mutants of several tissue-specific v-erbB transforming mutants by replacement of the ATP-binding lysine residue in the kinase domain with an arginine residue. These kinase-defective v-erbB mutants were analyzed for their in vitro and in vivo transforming potentials. Specifically, kinase-defective mutants of erythroleukemogenic, hemangioma-inducing, and sarcomagenic v-erbB genes were assessed for their oncogenic potential. In vitro transformation potential was assessed by soft-agar colony formation in primary cultures of chick embryo fibroblasts (CEF). In vivo transformation potential was determined by infection of 1-day-old line 0 chicks with concentrated recombinant retrovirus and then monitoring of birds for tumor formation. These transformation assays demonstrate that kinase activity is absolutely essential for transformation by tissue-specific transforming mutants of the avian c-erbBl gene. Since all of the tissue-specific v-erbB mutants characterized to date exhibit tyrosine kinase activity in vitro but do not transform all tissues in which they are expressed, we conclude that v-erbB-associated tyrosine kinase activity may be necessary but is not sufficient to induce tumor formation.

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