calmodulin/sarcoma

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Phosphorylation of tyrosine residues of calmodulin in Rous sarcoma virus-transformed cells.

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Calmodulin, a wide-spread eukaryotic Ca2+-binding protein, was phosphorylated at its tyrosine residues in Rous sarcoma virus (RSV)-transformed chicken and rat cells but not in normal chicken embryo fibroblasts. In contrast, serine and threonine phosphorylation of calmodulin was found to occur in

Antitumor effect of a calmodulin antagonist on the growth of solid sarcoma-180.

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A calmodulin antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), proved to have antitumor activity against solid Sarcoma-180. In particular, intraperitoneal injection of W-7 strongly inhibited the growth of solid Sarcoma-180 in mice given a daily dose, 10 mg/kg for 10 consecutive

Reversal of drug resistance in sarcoma-45 by the new calmodulin antagonist--trihydrochloride of [1,2,5-trimethyl-4-phenyl-4-beta-[N-(beta-ethylamino)-N-4'-methoxybe nzy l]-ethylamino] piperidine (AR-2).

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The anti-drug resistance effect of three derivatives (AR-1, AR-2 and AR-3) of [1,2,5-trimethyl-4-phenyl-4-beta-(N,N-disubstituted-ethylamino)] piperidines, that were evaluated as calcium and calmodulin antagonists, was studied on doxorubicin (ADM) and vincristine (VCR) resistant Sarcoma-45

A calmodulin-dependent protein kinase in Rous sarcoma virus-transformed rat cells and normal liver.

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A calmodulin-dependent protein kinase has been purified extensively from a Rous sarcoma virus-transformed rat cell line (RR1022) and from normal rat liver. The calmodulin-dependent protein kinase activity was manifested by in vitro phosphorylation of a single Mr 57 000 endogenous phosphoprotein

[Calmodulin in osteogenic sarcoma].

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The activating role of phospho-(Tyr)-calmodulin on the epidermal growth factor receptor.

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The activity of calmodulin (CaM) is modulated not only by oscillations in the cytosolic concentration of free Ca(2+), but also by its phosphorylation status. In the present study, the role of tyrosine-phosphorylated CaM [P-(Tyr)-CaM] on the regulation of the epidermal growth factor receptor (EGFR)

[Hormones and auto-paracrine tumor growth regulators in osteogenic sarcoma].

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The paper analyzes the data of long-term studies made in the N. N. Blokhin Cancer Research Center, Russian Academy of Medical Sciences. The study dealt with androgen exchange, the baseline levels of serum sexual steroid hormones and their receptors in the tumor, the blood concentrations of the

Purification of the Rous sarcoma virus src kinase by casein-agarose and tyrosine-agarose affinity chromatography.

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A simple and effective purification method for the src kinase, the transforming gene product of Rous sarcoma virus, has been developed by using affinity chromatography on casein-agarose and tyrosine-agarose columns. NaDodSO4/polyacrylamide gel electrophoresis and silver staining analysis showed that

Disordered binding regions of Ewing's sarcoma fusion proteins.

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A relationship was found between the Amino acid (AA) composition, Intrinsic Protein Disorder (IPD) and Protein Binding Regions (PBRs) of the functional regions of Ewing's sarcoma protein (EWS) and oncogenic EWS fusion proteins (EFPs). EWS has high IPD and 64% predicted Disordered Binding Regions

Biosynthesis of calmodulin in normal and virus-transformed chicken embryo fibroblasts.

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We report here that the higher levels of calmodulin in transformed chicken embryo fibroblasts are due to an increase in the rate of synthesis of calmodulin that results from an increased amount of calmodulin-specific mRNA in transformed cells. Transformation of several types of eucaryotic cells by

The role of calmodulin in the proliferation of transformed and phenotypically normal tsASV-infected rat cells.

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NRK cells infected with a temperature-sensitive, transformation-defective mutant of avian sarcoma virus (ASV), tsLA23, behaved as if nontransformed at a nonpermissive 40 degrees C and were rendered quiescent by serum deprivation. These serum-deprived cells were stimulated to start entering S phase

Regulation of intracellular levels of calmodulin and tubulin in normal and transformed cells.

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Transformation of mammalian tissue culture cells by oncogenic viruses results in a 2-fold increase in the intracellular concentration of calmodulin quantitated by radioimmunoassay. The two pairs of companion cell lines used in this study were the Swiss mouse 3T3/simian virus 40-transformed 3T3 cells

Down-regulation of a calmodulin-related gene during transformation of human mammary epithelial cells.

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A human cDNA library obtained from cultured normal mammary epithelial cells (HMECs) was searched by subtractive hybridization for genes whose decrease in expression might be relevant to epithelial transformation. One clone identified by this procedure corresponded to a 1.4-kilobase mRNA, designated

Calmodulin and Ca2+ in normal and transformed cells.

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Numerous lines of evidence implicate calcium and calmodulin (CaM) as regulators of cell growth and functional differentiation. In light of this evidence, several studies of the possible involvement of the CaM system in cellular transformation by RNA and DNA tumor viruses have been carried out. This

Calcium/calmodulin regulation of the rat prolactin gene is conferred by the proximal enhancer region.

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The effects of the calcium/calmodulin signaling system on expression of the rat PRL gene were studied in rat pituitary GH3 cells using two specific naphthalene sulfonamide calmodulin (CaM) antagonist drugs, W7 and a more potent and more highly specific iodo-derivative, 5-iodo-1-C8. PRL (but not GH)

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