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Jeanjacques Madjar - One of the best experts on this subject based on the ideXlab platform.
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v erbb oncogene expression accounts for most variations in protein synthesis after Avian Erythroblastosis Virus infection of chicken embryo fibroblasts a two dimensional electrophoresis study
Electrophoresis, 1992Co-Authors: Christelle Desbois, Jacques Samarut, Olivier Gandrillon, Jeanjacques MadjarAbstract:The effect of the v-erbA and/or v-erbB oncogenes on cellular gene expression was investigated after separation by two-dimensional polyacrylamide gel electrophoresis of [35S]methionine-labelled proteins from chicken embryo fibroblasts (CEF), infected by either the Avian Erythroblastosis Virus (AEV) carrying both oncogenes, or by Viruses carrying only one of them. We observed significant changes in the synthesis of 34 proteins in AEV-transformed CEF as compared with control cells. The synthesis of 24 of them was increased while the synthesis of the other 10 proteins was decreased. The expression of v-erbB alone is necessary and sufficient to induce changes in the synthesis of 27 proteins while the 7 remaining modifications are observed only in cells expressing v-erbB together with v-erbA. Moreover, the deregulation of protein synthesis by v-erbB-expressing Viruses was correlated with the morphological transformation state of cells.
J T Parsons - One of the best experts on this subject based on the ideXlab platform.
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the protooncogene c sea encodes a transmembrane protein tyrosine kinase related to the met hepatocyte growth factor scatter factor receptor
Proceedings of the National Academy of Sciences of the United States of America, 1993Co-Authors: J L Huff, Mary Anne Jelinek, C A Borgman, T J Lansing, J T ParsonsAbstract:c-sea is the cellular homologue of the Avian Erythroblastosis Virus S13-encoded oncogene v-sea. We have isolated and determined the nucleotide sequence of overlapping chicken cDNAs that encode the putative c-sea protooncogene product. The predicted reading frame encoded a 1404-aa polypeptide that had the structure of a receptor-like protein-tyrosine kinase and exhibited the highest degree of sequence similarity with the Met/hepatocyte growth factor/scatter factor receptor. Analysis of steady-state RNA expression revealed that c-sea mRNA levels were elevated approximately 5-fold in chicken embryo cells transformed by activated variants of the src nonreceptor protein-tyrosine kinase gene but not in cells transformed by the nuclear oncogenes v-myc or v-rel. A survey of c-sea expression in a variety of chicken tissues indicated that the highest levels of mRNA were located in peripheral white blood cell populations and in the intestine.
Martin L Privalsky - One of the best experts on this subject based on the ideXlab platform.
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a subpopulation of the v erb a oncogene protein a derivative of a thyroid hormone receptor associates with heat shock protein 90
Journal of Biological Chemistry, 1991Co-Authors: Martin L PrivalskyAbstract:Abstract The v-erb A oncogene of Avian Erythroblastosis Virus is derived from a host gene for a thyroid hormone receptor and is able to block differentiation of erythroid cells and modify the growth properties of fibroblasts. Unlike its host cell progenitor, the v-erb A protein is found in both cytoplasmic and nuclear fractions of the cell. I report here that the cytoplasmic form of the v-erb A protein is associated in a higher molecular weight complex with heat shock protein 90, the same polypeptide found in association with the unliganded steroid receptors and with the soluble forms of the src oncogene.
Hsing Jien Kung - One of the best experts on this subject based on the ideXlab platform.
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dissecting the activating mutations in v erbb of Avian Erythroblastosis Virus strain r
Journal of Virology, 1991Co-Authors: Hui Kuo G Shu, Robert Pelley, Hsing Jien KungAbstract:The v-erbB oncogene isolated from the R (or ES4) strain of Avian Erythroblastosis Virus is capable of inducing erythroleukemia and fibrosarcomas. This oncogene differs from the proto-oncogene c-erbB, the Avian homolog of the epidermal growth factor receptor, by its lack of an intact ligand-binding domain as well as additional alterations in its cytoplasmic coding sequences. By contrast, the insertionally activated c-erbB, a variant oncogene, which encodes a product that also lacks the ligand-binding domain but is otherwise unaltered in its cytoplasmic coding sequences, is capable of inducing leukemia but cannot induce sarcomas. In this report, we show that the critical changes for activating the sarcomagenic potential displayed by v-erbB R are two point mutations within the tyrosine kinase domain and an internal deletion of 21 amino acids in the carboxyl-terminal regulatory domain. The removal of the carboxyl-terminal autophosphorylation sites is not obligatory. These activating mutations (Arg-263 to His, Ile-384 to Ser, and the deletion of residues 494 to 514), when introduced singly into the insertionally activated c-erbB, all dramatically increase fibroblast-transforming potential. Arg-263 resides near the highly conserved HRD motif of the kinase domain, and its mutation to His increases the autophosphorylation activity. The other two mutations do not alter the intrinsic kinase activity and presumably affect other aspects of the receptor involved in growth signaling. Therefore, the high transforming potential of v-erbB R is a consequence of synergism among multiple activating mutations. Images
J L Huff - One of the best experts on this subject based on the ideXlab platform.
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the protooncogene c sea encodes a transmembrane protein tyrosine kinase related to the met hepatocyte growth factor scatter factor receptor
Proceedings of the National Academy of Sciences of the United States of America, 1993Co-Authors: J L Huff, Mary Anne Jelinek, C A Borgman, T J Lansing, J T ParsonsAbstract:c-sea is the cellular homologue of the Avian Erythroblastosis Virus S13-encoded oncogene v-sea. We have isolated and determined the nucleotide sequence of overlapping chicken cDNAs that encode the putative c-sea protooncogene product. The predicted reading frame encoded a 1404-aa polypeptide that had the structure of a receptor-like protein-tyrosine kinase and exhibited the highest degree of sequence similarity with the Met/hepatocyte growth factor/scatter factor receptor. Analysis of steady-state RNA expression revealed that c-sea mRNA levels were elevated approximately 5-fold in chicken embryo cells transformed by activated variants of the src nonreceptor protein-tyrosine kinase gene but not in cells transformed by the nuclear oncogenes v-myc or v-rel. A survey of c-sea expression in a variety of chicken tissues indicated that the highest levels of mRNA were located in peripheral white blood cell populations and in the intestine.
