Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.11.1 (protein kinase)
81,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The nucleotide sequence of the region of Gardner-Rasheed feline sarcoma virus (GR-FeSV) encoding its primary translation product, p70gag-fgr, has been determined. From the nucleotide sequence, the amino acid sequence of this transforming protein was deduced. Computer analysis indicates that a portion of P70gag-fgr has extensive amino acid sequence homology with actin, a eukaryotic cytoskeletal protein. A second region of P70gag-fgr is closely related to the tyrosine-specific kinase gene family. Thus, the v-fgr oncogene appears to have arisen as a result of recombinational events involving two distinct cellular genes, one coding for a structural protein and the other for a protein kinase.
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PMID:Gene product of v-fgr onc: hybrid protein containing a portion of actin and a tyrosine-specific protein kinase. 631 14

A new strain of feline sarcoma virus, designated HZ1-FeSV, was isolated from a 4-year-old domestic cat with multicentric fibrosarcoma. A primary tumor cell line was established and virus produced from that line was found to induce foci in feline embryonic lung fibroblasts (FLF3) and mink lung fibroblasts (CCL64) in tissue culture and fibrosarcomas in inoculated 10-week-old kittens. The derivation of transformed nonproducer clones of FLF3 and CCL64 cells containing helper virus-rescuable, focus-forming activity indicated that HZ1-FeSV was defective for replication. The only discernible translation product of the HZ1-FeSV genome in cultured cells was a 100,000-Da polyprotein (P100) which contained amino-terminal sequences of the FeLV gag gene precursor protein covalently linked to a sarcoma virus-specific domain. Immunoprecipitates containing P100 exhibited a protein kinase activity capable of phosphorylating tyrosine residues of P100. Immunologically, P100 was highly cross-reactive with gag-fes polyproteins encoded by two previously characterized strains of FeSV, the GA- and the ST-FeSV. By comparison of methionine-containing tryptic peptides, the HZ1-FeSV protein was shown to be more closely related to the GA-FeSV protein than to the ST-FeSV protein, but to be distinguishable from both other proteins.
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PMID:Isolation of a new feline sarcoma virus (HZ1-FeSV): biochemical and immunological characterization of its translation product. 632 May 33

The translation products of the Snyder-Theilen (ST) and Gardner-Arnstein (GA) strains of feline sarcoma virus (FeSV), termed gag-fes proteins, are high molecular weight polyproteins containing different amounts of the amino terminus of the feline leukemia virus (FeLV) gag gene-coded precursor protein linked to a similar sarcoma virus-specific polypeptide. Both polyproteins are phosphoproteins with indistinguishable in vitro associated tyrosine-specific protein kinase activities. The polyproteins are extremely hydrophobic proteins which are intimately associated with the plasma membrane fraction of transformed cells. Approximately 10% of the proteins are modified by glycosylation and expressed on the cell surface where they are accessible to lactoperoxidase-mediated radio-iodination and trypsinization. Cell surface localization of the polyproteins does not appear to be necessary for transformation. However, preliminary evidence suggests that the amount of FeLV p30 sequences at the amino end of the proteins may have some effect on the intracellular distribution of the gag-fes polyproteins and on the phenotype of the transformed cell.
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PMID:Association of the transforming proteins of the ST and GA strains of feline sarcoma virus and their in vitro associated protein kinase activities with cellular membranes. 632 Sep 92

The protooncogene c-fps/fes is a single vertebrate locus homologous to both the fps transforming gene of Fujinami avian sarcoma virus and the fes transforming gene of two feline sarcoma virus isolates. The human c-fps/fes locus has been previously cloned and characterized. We report that a recombinant gene in which 3' human c-fps/fes sequences replace over 80% of the feline sarcoma virus fes sequences transforms NIH 3T3 mouse fibroblasts and encodes a protein kinase. Cells transformed by this recombinant possess increased phosphotyrosine levels. These observations demonstrate that a large carboxyl portion of a human c-fps/fes protein product can functionally complement a retroviral transforming protein.
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PMID:Transforming potential of a human protooncogene (c-fps/fes) locus. 632 90

Oligopeptides predicted from the nucleotide sequence of the oncogene v-fes of feline sarcoma virus (FeSV) were synthesized chemically and used to generate specific antibodies. Antisera against a 12-amino-acid-long oligopeptide (12-mer) located 42 residues from the carboxyl terminus of the v-fes coding sequence efficiently recognized the transforming proteins encoded by Snyder-Theilen (ST) and Gardner-Arnstein (GA) strains of FeSV. This 12-mer also contains 10 amino acid residues homologous in order and position to those predicted from the nucleotide sequence of the oncogene v-fps of avian Fujinami sarcoma virus (FSV). The anti-12-mer immunoprecipitated the FSV-specific transforming protein molecules from FSV-transformed cells. Binding of these antipeptide antibody molecules to the v-fes and the v-fps gene products inhibited their associated tyrosine-specific protein kinase (EC 2.7.1.37) activities. The ability to generate such site-specific antisera to the products of related oncogenes will be valuable in the molecular characterization of retroviral transforming proteins and their normal cellular homologs.
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PMID:Antibodies of predetermined specificity detect two retroviral oncogene products and inhibit their kinase activities. 657 83

The Gardner-Rasheed strain of feline sarcoma virus (GR-FeSV), is a recent isolate of a naturally occurring cat sarcoma. The primary translational product of GR-FeSV (GR P70) was shown to be a phosphoprotein with associated tyrosine-specific protein kinase activity. The relationship between the GR-FeSV provirus and once genes of other transforming retroviruses known to code for tyrosine kinases was examined by molecular hybridization. Probes repesenting onc genes of Snyder-Theilen and McDonough strains of feline sarcoma virus, Rous sarcoma virus, and Abelson murine leukemia virus did not detectably hybridize integrated GR-FeSV. These findings suggest that GR-FeSV contains a distinct tyrosine kinase-coding onc gene.
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PMID:Analysis of the primary translational product and integrated DNA of a new feline sarcoma virus, GR-FeSV. 660 28

The transforming genes of acutely transforming retroviruses are derived from conserved cellular genes (c-onc genes) which are believed to be important in normal cell growth and differentiation. Recent studies indicate that altered expression of c-onc genes, for example, by insertion of viral genomes, gene amplification or chromosomal translocation, can lead to development of malignant diseases in man and animals. c-myb and c-fes are homologues of the transforming genes of avian myeloblastosis virus and feline sarcoma virus (Gardner and Snyder-Theilen strains), respectively. c-myb is transcribed preferentially in immature haematopoietic cells and probably codes for a protein important in differentiation of these cells. The viral fes gene, like several other viral onc genes, encodes a tyrosine-specific protein kinase. However, c-fes transcripts have not been detected in the types of human cells examined so far. c-myb and c-fes have been assigned to human chromosomes 6 and 15, respectively. Specific aberrations involving these chromosomes have been observed at high frequency in several human neoplasms. We have now sublocalized c-myb to 6q22-24 and c-fes to 15q25-26 by in situ hybridization of the human c-onc probes to human mitotic chromosome preparations. These chromosomal segments are indeed involved in nonrandom translocations in several human tumours. The results encourage further investigation into the role of onc genes in the pathogenesis of specific neoplasms.
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PMID:Chromosomal sublocalization of human c-myb and c-fes cellular onc genes. 686 12

The Gardner strain of feline sarcoma virus (FeSV) has previously been shown to encode as its major translational product, a phosphoprotein of molecular weight (Mr) = 115,000 (P115) with an associated protein kinase activity and probable transforming function. In the present study, we demonstrate that this enzyme specifically phosphorylates tyrosine and that Gardner FeSV-transformed mink and rat cells exhibit constitutively higher levels of phosphotyrosine than nontransformed control cells. In addition, we identify a Mr = 150,000 cellular substrate for the FeSV P115-associated protein kinase activity. This latter protein, designated P150, is expressed in cells of a number of mammalian species including cat, mink, dog, rat, mouse and human, possesses broadly reactive interspecies antigenic determinants, and exhibits binding affinity for FeSV P115. Although P150 exhibits an associated protein kinase activity, this activity differs from the FeSV P115-associated enzyme in that it phosphorylates serine and threonine rather than tyrosine. On the basis of immunologic criteria and tryptic peptide analysis, the possibility that P150 is structurally related to Gardner FeSV P115 is excluded. As a consequence of its affinity for FeSV P115, P150 is efficiently incorporated into FeSV pseudotype virions, providing a source for its purification and preparation of antisera for study of its expression in mammalian cells.
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PMID:Feline sarcoma virus P115-associated protein kinase phosphorylates tyrosine. Identification of a cellular substrate conserved during evolution. 743 Jan 66

Expression of the v-fms oncogene of feline sarcoma virus in fibroblasts causes surface exposure of an activated receptor tyrosine kinase, v-Fms, that is autophosphorylated at multiple sites within its cytoplasmic domain. Cellular proteins interacting with this part of v-Fms modulate the mitogenic activity and morphology of the cells. We show here that the tyrosine residue in position 807 (Y-807) of the v-Fms molecule constitutes a major autophosphorylation site. The replacement of this residue by phenylalanine (Y807F mutation) allowed us to functionally dissect v-Fms-specific mitogenic and morphogenic cascades. Cells expressing the mutant v-Fms molecule resembled wild-type (wt) v-Fms-transformed (wt-v-Fms) cells in terms of [3H]thymidine uptake rates and activation of the Ras/Raf-1 mitogenic cascade. Such cells showed, however, a flat morphology and contained intact actin cables and fibronectin network. Our studies indicate that the v-Fms molecule controls cell morphology by a cascade that involves a direct interaction with p120RasGAP and p190RhoGAP: (i) in contrast to wt v-Fms molecules, the Y807F v-Fms protein failed to associate with and phosphorylate p120RasGAP; (ii) tight complexes between p120RasGAP and p190RhoGAP as well as detectable RhoGAP activity were present exclusively in wt-v-Fms cells; and (iii) p190RhoGAP was dispersed throughout the cytoplasm of wt-v-Fms cells, whereas its distribution was restricted to perinuclear regions of cells expressing the mutant v-Fms gene.
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PMID:Tyrosine 807 of the v-Fms oncogene product controls cell morphology and association with p120RasGAP. 766 6

The c-fes protein (NCP92) is a tyrosine-specific protein kinase, capable of both autophosphorylation and phosphorylation of other substrates. We have analysed c-fes RNA expression in human/murine ontogenetic development and in homogeneous populations of embryonic and adult human hematopoietic cells. c-fes expression has been observed in rapidly proliferating embryonic-fetal tissues originating from different germinal layers, but not in adult non-hematopoietic tissues. In particular, a spatially and temporally regulated transcription was observed in the central nervous system and in developing cartilage. Expression in hematopoietic cells was evaluated in progenitors purified from embryonic-fetal liver and adult peripheral blood differentiating gradually and specifically along the erythroid or granulomonocytic lineage. In both embryonic and adult hematopoietic cells c-fes was abundantly expressed in undifferentiated progenitors of both lineages, as well as in differentiated granulomonocytic precursors, but not in erythroblasts. This expression pattern correlates with that of GM-CSF and in part IL-3 receptors (Testa et al., 1993 and our unpublished results). Altogether, these results suggest a possible role for c-fes in signal transduction, in both embryonic non-hematopoietic tissues and embryonic/adult hematopoietic cells, following interaction of growth factors with their tyrosine-kinase negative receptors (i.e., GM-CSF and IL-3 receptors in adult hematopoietic cells and other hypothetical growth factor(s) receptors during embryonic development.
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PMID:c-fes expression in ontogenetic development and hematopoietic differentiation. 810 16


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