Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Microtubules prepared from pig brain by two cycles of assembly-disassembly comprise cyclic nucleotide-independent protein kinase activity with phosvitin and troponin T as substrates. 2. Phosphocellulose chromatography resolved two phosvitin kinase activity peaks, one of which coincided with the troponin T kinase peak. 3. The activity peak corresponding to troponin T kinase was inhibited by heparin (I50 = 0.06 micrograms/ml), whereas the other phosvitin kinase peak was unaffected. 4. Both kinase fractions phosphorylated tubulin and microtubule-associated protein (MAP-2). 5. It is concluded that pig brain microtubules contain bound casein kinases I and II. The association may target the action of these kinases toward microtubular proteins in vivo.
Cell Mol Neurobiol 1988 Sep
PMID:Casein kinases I and II bound to pig brain microtubules. 322 59

Casein kinase II has been isolated from ribosome-free extracts of Rana temporaria oocytes by chromatography on heparin-sepharose, phosphocellulose and mono Q. It consists of different subunits with molecular weights 43, 41 and 29 Kda. Protein kinase has been labelled in vitro with 125I and injected back into amphibian oocytes. With the help of radioautography it is shown that this enzyme forms in the oocyte cytoplasm a wide concentric ring around the nucleus. Part of the labelled casein kinase II is associated with free cytoplasmic informosomes.
Mol Biol (Mosk)
PMID:[Intracellular localization of casein kinase of type II in oocytes of Rana temporaria]. 326 65

Several oncogenes have now been implicated in mammary carcinogenesis. We investigated the phenotypic effects of expressing three representative oncogenes in mammary epithelial cells. v-myc (coding for a nuclear protein), v-Ha-ras (a G-protein homologue) and v-fgr (a tyrosine kinase) genes were introduced into the nontumorigenic clone 14 of the mouse mammary epithelial cell line COMMA-1D. Their effects upon growth and differentiation were determined. Anchorage-independent growth was induced by all three oncogenes with low efficiency. v-Ha-ras and v-fgr induced tumorigenicity in nude mice. The effect of oncogenes upon parameters unique to mammary epithelial cells in vitro was assayed. Both v-myc and v-fgr abolished the ability of clone 14 to grow as three-dimensional branching structures in hydrated collagen gel. v-fgr completely and v-myc partially inhibited the expression of the epithelium specific cytokeratins. Clone 14 can be induced to produce the beta-casein milk protein by the combination of the lactogenic hormones, dexamethasone, insulin, and PRL. Introduction of v-myc into clone 14 cells resulted in an estimated 50-fold increased induction of beta-casein protein and at least a 60-fold increase in beta-casein mRNA. The number of cells stained with anti-beta casein antibodies also showed a 10-fold increase after v-myc introduction. This still required the synergistic action of all three lactogenic hormones. Thus v-myc can alter the normal response of mammary epithelial cells to lactogenic hormones.
Mol Endocrinol 1988 Feb
PMID:v-myc alters the response of a cloned mouse mammary epithelial cell line to lactogenic hormones. 339 47

The association of a protein kinase with cytoplasmic non-polysomal messenger ribonucleoproteins is demonstrated by chromatography on oligo(dT)-cellulose and sucrose gradient centrifugation. The cAMP-independent enzyme is inhibited by caffeine and poly(L)-glutamic acid and is classified as a casein kinase II. Among the exogenous proteins initiation factor eIF2 is the best substrate and is 7.8 times more efficiently phosphorylated than casein. Endogenous mRNP protein substrates have a Mr of 125 000, 65 000, 38 000, 26 000 and 23 500. The main phosphate acceptor is the Mr 38 000 poly(A)-binding protein. Dephosphorylation of the poly(A)-binding protein by protein phosphatases decreases its RNA binding property. The effect of phosphorylation-dephosphorylation of mRNP proteins on the initiation of protein synthesis is discussed.
Mol Biol Rep 1986
PMID:Identification of the substrates of the casein kinase II associated with non-polysomal messenger ribonucleoproteins of A. salina cryptobiotic embryos. 346 Dec 61

In order to ascertain whether the effect of corticoids upon casein synthesis in pregnant rabbit mammary gland culture is due to interactions with classical glucocorticoid or type I (mineralocorticoid) receptors we have demonstrated the existence of both types of receptors in the tissue and have studied the effects of aldosterone and the specific glucocorticoid agonist RU 28362 upon casein synthesis in tissue culture. Both compounds significantly stimulated prolactin-induced casein synthesis. On dose-response studies RU 28362 proved to be as active as dexamethasone, cortisol was active at intermediate concentrations and aldosterone was the least active. The three glucocorticoids were able to stimulate DNA synthesis in the tissue, but aldosterone had no effect. Finally, RU 486, a potent glucocorticoid antagonist, blocked the action of aldosterone and the other corticoids upon casein synthesis, whereas spironolactone, a mineralocorticoid antagonist, was unable to do so. These results demonstrate that the stimulatory effect of corticoids upon casein synthesis in pregnant rabbit mammary tissue culture is mediated through classical (type II) glucocorticoid receptors. Transferrin accumulation in the tissue was not modified by any treatment, indicating that the action of the steroids was specific for casein, and not a general stimulation of protein synthesis.
Mol Cell Endocrinol 1987 Aug
PMID:Binding and action of glucocorticoids and mineralocorticoids in rabbit mammary gland. Exclusive participation of glucocorticoid type II receptors for stimulation of casein synthesis. 365 4

Membrane proteins of human erythrocytes can be phosphorylated not only by membrane casein kinase (MS) but also by cytosolic casein kinases CS and CTS, resembling casein kinase I and II, respectively. Casein kinase CS, like membrane casein kinase MS, preferentially phosphorylates membrane proteins such as band 2 (spectrin, beta-subunit) and band 3, which are the major phosphate-acceptor proteins in the endogenous phosphorylation of isolated ghosts in the presence of [gamma-32P]ATP. By contrast, cytosolic casein kinase CTS phosphorylates, in addition to band 2, some membrane proteins, whose endogenous phosphorylation in isolated ghosts under the same conditions is negligible, if any. The CS- and CTS-catalyzed phosphorylations exhibit different response to increasing NaCl (or KCl) concentrations up to physiological levels (140 mM KCl, 20 mM NaCl); i.e. CS- and MS-catalyzed phosphorylations are strongly inhibited by 75-150 mM KCl (or NaCl), while CTS-catalyzed phosphorylation is practically unaffected. In the absence of added NaCl, CS- and MS-catalyzed phosphorylations are markedly inhibited by 1.5-3 mM 2,3-bisphosphoglycerate, whereas CTS-catalyzed phosphorylation appears to be practically unaffected. Finally, CS- and MS-catalyzed phosphorylations are slightly inhibited also by 1 mM spermine, while CTS-catalyzed phosphorylation is enhanced by this polycation concentration.
Mol Cell Biochem 1985 Oct
PMID:Phosphorylation of membrane proteins by cytosolic casein kinases in human erythrocytes. Effect of monovalent ions, 2,3-bisphosphoglycerate and spermine. 386 41

Two monoclonal antibodies, LICR-LON-32.2 (32.2) and LICR-LON-14.1 (14.1), are described which react with human casein. 32.2 reacts with human beta-casein and 14.1 with human kappa-casein. 32.2 also reacts with rat band 2 casein and bovine beta-casein, but 14.1 appears to be specific for human kappa-casein. These monoclonal antibodies do not cross-react with other milk proteins.
Mol Immunol 1985 Aug
PMID:Monoclonal antibodies to human casein. 390 Jun 97

A sensitive immunoassay was used to identify recombinant DNA plasmids carrying cDNA fragments of bovine caseins in the cDNA library from rRNA of bovine mammary glands. Colonies grown on nitrocellulose filters were lysed in situ and proteins from the lysates were blotted onto CNBr-activated filter paper. Antigens covalently bound to the CNBr-activated paper or bound to the nitrocellulose filters were detected by reaction with antiserum to caseins, followed by 125I-labeled protein A from Staphylococcus aureus and autoradiography. Four clones were positive among 5400 bacterial clones of the cDNA library--al, b2, b5, h7. Molecular weights of chimeric proteins pre-beta-lactamase:casein synthesized in Escherichia coli were determined by immunoblotting. Colony hybridization and DNA sequence analysis showed that clone b5 contained cDNA fragment of bovine kappa-caseins and clone h7 cDNA fragment of beta-casein. The last clone was designated pKcas beta-7.
Mol Biol (Mosk)
PMID:[Identification of bacterial clones that encode cow's caseins by direct immunological screening of the cDNA library]. 390 Jun 95

Ovariectomy or ovariohysterectomy on day 18 of pregnancy augmented mammary beta-casein content 28 h later. Progesterone injected immediately and 12 h after ovariectomy showed a clear inhibitory effect on casein synthesis. Estrogen induced a significant increase in mammary beta-casein content when injected 12 h after surgery. Treatment with CB-154 to prevent prolactin release did not affect the increase of casein induced by ovariectomy. When CB-154 was injected to ovariohysterectomized pregnant rats, significant reduction of casein synthesis was obtained. According to these findings, rat placental lactogen in the absence of prolactin and progesterone induces beta-casein synthesis. Therefore prolactin, ovarian and placental hormones interplay at the end of pregnancy for full expression of the mammary gland genome.
Mol Cell Endocrinol 1985 Feb
PMID:Hormonal regulation of casein synthesis at the end of pregnancy. 397 61

A cyclic nucleotide-independent protein kinase which phosphorylates preferentially acidic proteins such as casein or phosvitin was isolated from cytosol of chick duodenal mucosa. The enzyme was purified more than 633 fold to apparent homogeneity by ammonium sulfate fractionation, column chromatography on DEAE-cellulose, phosphocellulose, hydroxylapatite and by sucrose density gradient centrifugation. The native enzyme has a molecular weight of 131 000 as measured by gel filtration. The enzyme is a complex protein containing three polypeptides of molecular weight of 39 000, 36 000 and 27 000. It behaves as a complex throughout its purification and gel filtration but its components are readily separated by electrophoresis in denaturing buffer. The 27 000 molecular weight band was selectively autophosphorylated when the enzyme was incubated in the presence of [gamma-32P]ATP. When casein was used as substrate, physiological concentrations of naturally occurring polyamines such as spermine and spermidine markedly stimulated enzyme activity. However with phosvitin as substrate polyamines were strong inhibitors of the enzyme activity. This contrasting effect on intestinal kinase activity was also apparent using cytoplasmic proteins as endogenous phosphate acceptors. A characterization of this differential effect is presented and some possible physiological implications are discussed.
Mol Cell Biochem 1985 Mar
PMID:Polyamine-sensitive protein kinase from chick intestinal mucosa. 398 5


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