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)

The B1 molecule (CD20) is a phosphoprotein expressed only by B-lymphocytes. In this study, analysis of B1 immunoprecipitated from surface iodinated B-cell lines and B-lymphocytes has shown that there are several expressed forms of B1. A predominant species of Mr 33,000 represents 75-80% of the iodinated cell surface B1 and a Mr 35,000 species represents 20-25%. Limited proteinase digestion of these two species generated similar peptide maps demonstrating that the different forms of B1 shared common peptides. Biosynthetic labeling with [35S]methionine revealed that the Mr 35,000 B1 species may actually represent two bands of Mr 34,500 and 36,000. Endoglycosidase digestion studies and metabolic labeling in the presence of tunicamycin indicated that neither the Mr 33,000 or 34,500-36,000 forms of B1 were glycosylated. The Mr 33,000 and 34,500-36,000 forms of B1 were constitutively phosphorylated in B-cell lines. However, exposure of B-cells to PMA resulted in a significant increase in the phosphorylation of the Mr 34,500-36,000 form. Exposure to PMA also resulted in an increase in the amount of Mr 34,500-36,000 protein immunoprecipitated from 35S labeled cells. These results suggest that there are multiple forms of the B1 molecule expressed by B-lymphocytes and that this heterogeneity may result from phosphorylation of the B1 protein.
Mol Immunol 1988 Dec
PMID:Heterogeneity in the B1 (CD20) cell surface molecule expressed by human B-lymphocytes. 246 90

Analysis of 53 somatic cell hybrids between TNF-sensitive myeloid cells (U937) and TNF-resistant T-cell lines HUT78 (UH-hybrids) and Jurkat (UJ-hybrids), respectively, revealed complete resistance to TNF-mediated cytostasis in all cases. Moreover, all hybrids remained insensitive to a combined treatment with TNF-alpha and IFN-gamma, which exert synergistic growth inhibition and cytotoxicity on parental U937 cells. Analyses of cell surface marker expression, membrane phosphoproteins, and expression of tissue-specific cytokine genes revealed differential conservation of myeloid and T-cell-specific properties in each of these hybrids, but invariant, dominant resistance to TNF-alpha-mediated growth inhibition. All TNF-resistant hybrids expressed a membrane phosphoprotein pattern, which closely resembled that of the respective parental T-cell lines. In particular, two membrane phosphoproteins of apparent molecular weight of 50,000 and 38,000 were common in the two parental T-cell lines and all UH- and UJ-hybrid clones, suggesting a possible role of these proteins in mediating TNF resistance.
Mol Biother 1988
PMID:Mechanisms of TNF resistance: identification of membrane phosphoproteins associated with a dominant resistant phenotype in lymphoid-myeloid somatic cell hybrids. 247 98

Specific changes in the two-dimensional gel electrophoretic pattern of mouse oocyte phosphoproteins precede germinal vesicle breakdown (GVBD). We report that changes in the relative abundance of phosphoamino acids occurred prior to GVBD. We also report data that further strengthen the close association of the changes in phosphoprotein patterns with resumption of meiosis. The calmodulin antagonist W7, which transiently inhibits GVBD, inhibited partially at least two of the maturation-associated phosphoprotein changes, the dephosphorylation of a 60,000 Mr phosphoprotein and the phosphorylation of a 36,000 Mr protein. In oocytes from juvenile mice that were incompetent to resume meiosis, neither these changes nor the phosphorylation of proteins of Mr 24,000 and 28,000 occurred; all these changes occurred, however, in oocytes from juvenile mice that were competent to resume meiosis. The microinjection of the heat-stable inhibitor of cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKI), which induces GVBD in fully grown oocytes, did not induce GVBD in meiotically incompetent oocytes. Microinjected PKI did not induce the increased protein phosphorylations associated with maturation, but it did induce the dephosphorylation of the 60,000 Mr phosphoprotein. These results provide molecular markers for commitment to resume meiosis in GV-intact oocytes and indicate a potential basis for meiotic incompetence.
Mol Reprod Dev 1988
PMID:Protein phosphorylation in meiotically competent and incompetent mouse oocytes. 248 89

We investigated the reaction mechanism for GTP-dependent Ca2+ uptake by canine cardiac microsomes enriched in fragmented sarcoplasmic reticulum (SR), because previous studies reported that GTP utilization in cardiac SR occurs via a pathway very different from that for ATP utilization (for a review, see "Entman, M.L., Bick, R., Chu, A., Van Winkle, W.B., & Tate, C.A. (1986) J. Mol. Cell. Cardiol. 18, 781-792"). In cardiac microsomes, we detected slow but distinct oxalate-dependent Ca2+ accumulation, which reached 550 nmol/mg protein in 10 min, and similarly slow Ca2+-dependent GTP hydrolysis. In 50 microM [gamma-32P]-GTP at 0 degrees C, we detected Ca2+-dependent formation of phosphoprotein whose level in the steady state was about a half of the maximum obtained with [gamma-32P]ATP. Kinetic properties of the phosphoprotein, its molecular weight and its chemical stability after the acid treatment are consistent with the conclusion that the phosphoprotein is an acylphosphate intermediate for Ca2+-dependent GTP hydrolysis catalyzed by the Ca2+-pump ATPase. Analysis of the kinetics of the turnover of phosphoprotein revealed that slow GTP hydrolysis is due to slow phosphoprotein formation; at 25 degrees C, the latter arises mainly from slow binding of Ca2+ to the dephosphorylated enzyme. These results indicate that, contrary to the previous data, the reaction pathway for GTP-dependent Ca2+ transport in cardiac SR is basically the same as that for ATP-dependent transport.
 ...
PMID:Guanosine triphosphate utilization by canine cardiac muscle sarcoplasmic reticulum. 253 46

Cyclic AMP-regulated phosphoproteins with specific cellular localizations in brain represent important targets through which this second messenger system can mediate or modulate distinct neurotransmitter signals. This study reports that two cyclic AMP-regulated phosphoproteins (Mr 90,000 and 93,000) found in brain share several properties, including similar isoelectric points and similar phosphopeptide maps. This protein doublet is particularly enriched in the forebrain basal ganglia, but it can also be found in the substantia nigra, a brainstem region which is a major target for fibers from the forebrain basal ganglia. Quinolinic acid lesions of neurons in the neostriatum decrease the levels of the 90/93 kDa phosphoprotein doublet to about the same extent as they reduce the levels of DARPP-32, a phosphoprotein specifically enriched in striatonigral medium-sized spiny neurons. These reductions are seen in both the neostriatum and the substantia nigra. Therefore, within the basal ganglia, the 90/93 kDa phosphoprotein doublet, termed adenosine 3':5'-monophosphate-regulated phosphoprotein, Mr = 90,000 (ARPP-90), is largely, if not solely, present in striatonigral cells and fibers. The specific localization in these neurons suggests that ARPP-90 could be important in receptor-regulated, cyclic AMP-mediated functions in the striatonigral neurons.
Brain Res Mol Brain Res 1989 Mar
PMID:Localization of ARPP-90, a major 90 kiloDalton basal ganglion-enriched substrate for cyclic AMP-dependent protein kinase, in striatonigral neurons in the rat brain. 254 3

Protein kinase A (cAMP-dependent) and C (calcium, phospholipid-dependent) activities were measured and in vitro phosphorylation of endogenous proteins by these kinases were observed by SDS-PAGE in 100,000 x g supernatant (soluble) fractions of ovine small (12-22 microns) and large (greater than 22 microns) luteal cells. No differences in stimulation (P less than 0.05) of A kinase activity between small and large cells were detected. Protein kinase C activity was stimulated (P less than 0.05) 2.9-fold in small cells but not significantly enhanced above basal (P greater than 0.05) in large cells. By direct comparison, greater stimulation (P less than 0.05) over basal of A versus C kinase (6.1- versus 2.9-fold) was measured in small cells. These stimulations were greater than those observed in large cells (A kinase, 4.8-fold; C kinase, 1.8-fold). Maximal specific activities of both kinases (per mg protein) were greater (P less than 0.05) in small than in large cells. Endogenous proteins that could serve as substrates for phosphorylation by A and C kinases differed between small and large cells. Phosphorylation of six proteins by A kinase was consistently greater in small than in large cells. One endogenous protein (37 kDa) appeared to serve as a preferred substrate for phosphorylation by A kinase in small cells and C kinase in large cells. One protein (81 kDa) was predominantly phosphorylated in large rather than small cells by a calcium-dependent, C kinase-independent mechanism. These results support the accepted role of cAMP via A kinase and a possible role for C kinase in regulating steroidogenesis in ovine small luteal cells. The inability of large cells to respond to cAMP with enhanced secretion of progesterone may be due to an unavailability of phosphoprotein substrates for A kinase. Furthermore, protein kinase C activity and available protein substrates display quantitative and qualitative differences between small and large cells. Differences in regulation of steroidogenesis between the cell types may be due to these observed differences.
Mol Cell Endocrinol 1989 Apr
PMID:Protein kinase A and C activities and endogenous substrates in ovine small and large luteal cells. 254 89

Alloxan diabetes induced in white rats by intraperitoneal injection of alloxan-monohydrate (15 mg/100 g body weight) was used to study changes in the glycogen phosphorylase a and b, phosphoprotein phosphatases and hexokinase activities under insulin deficiency conditions. Among the enzymes studied, an increase in muscle phosphorylase a activity as well as the a/b ratio have been obtained. In diabetic muscle phosphoprotein phosphatases and hexokinase activities were diminished. AMP increased the liver glycogen phosphorylase activity twice in diabetic rats whereas in normal animals the enzyme was less sensitive to this effector. The changes in liver hexokinase activity at diabetes were not connected and correlated with the altered phosphorylase and protein phosphatase activities. The logical chain of probable molecular events taking place in muscle glycogen metabolism under the conditions of insulin deficiency is offered.
Mol Cell Biochem 1989 Oct 31
PMID:Changes in the activity of enzymes, participating in glycogen metabolism of alloxan diabetic rats. 255 79

Previous studies have shown that insulin and IGF-I bind to their respective receptors and stimulate autophosphorylation of the receptor beta subunits in detergent extracts of neuronal and glial cells. In the present study, intact neuronal and glial cells in primary culture have been utilized to characterize insulin- and IGF-I-stimulated phosphorylation of their receptors. Following [32P]orthophosphate labelling and stimulation by insulin or IGF-I, the cells were solubilized and the phosphorylated receptors were partially purified on wheat germ agglutinin--agarose columns, and immunoprecipitated using anti-phosphotyrosine or anti-insulin receptor antibodies. Insulin stimulated the phosphorylation of its receptor beta subunit (95 kD phosphoprotein) in a dose-dependent manner, within at least 20 seconds in both neuronal and glial cells. Additionally, a 102-kD phosphoprotein was observed in insulin-stimulated neuronal cells. Maximal stimulation of receptor phosphorylation occurred at 1 minute for the glial cells, and 10 minutes for the neuronal cells. IGF-I stimulated the phosphorylation of two phosphoproteins in intact neuronal and glial cells; a 95-kD protein and a 102-kD protein, in a dose-dependent manner. These observations demonstrate that both insulin and IGF-I stimulate the phosphorylation of the beta subunits of their respective receptors in brain cells in a similar fashion to their effects on receptors from nonneural tissues.
J Mol Neurosci 1989
PMID:Insulin and IGF-I stimulate phosphorylation of their respective receptors in intact neuronal and glial cells in primary culture. 256 92

To determine how functional changes such as growth and differentiation in the prostatic epithelium would alter protein phosphorylation on tyrosyl residues, differentiated (secretory) and basal (non-secretory) prostatic epithelial cells from normal and from metaplastic canine prostates were labeled with [32P]phosphate and their alkali-resistant phosphoproteins were analyzed by autoradiography after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The tyrosine protein kinase activity of the cells was also assayed by phosphorylation of a synthetic substrate, poly(Glu80-NaTyr20), in the presence of [gamma-32P]ATP. The prostates were characterized by tissue morphology and the cells by their density on Percoll gradients and [3H]thymidine incorporation into DNA. In prostates from intact dogs, tall columnar secretory epithelial cells were predominant and the non-secretory or basal epithelial cells were quiescent and did not incorporate [3H]thymidine. In metaplastic glands obtained from estrogen-treated castrated dogs, most of the isolated cells were non-secretory and synthesized DNA. Alkali-resistant phosphoproteins were present in all cell types. Except for two common phosphoproteins, p44 and p82, the relative phosphoprotein distribution within the gel differed when normal prostatic cells were compared to the metaplastic cells. However, the phosphoprotein patterns were the same in secretory and non-secretory cells from the same prostate tissue. On the other hand, the relative labeling intensity of phosphoproteins was always higher in non-secretory cells compared to corresponding secretory cells. Accordingly, tyrosine protein kinase (TPK) activity, expressed on a cell basis, was also higher in non-secretory cells; the ratios of TPK activities, non-secretory over corresponding secretory cells, was always higher than unity for all preparations but overlapped when cells from metaplastic glands were compared to those isolated from normal prostates. Thus, non-secretory epithelial cells isolated from either normal or metaplastic glands have a higher ability than corresponding secretory cells to phosphorylate endogenous alkali-resistant phosphoproteins and their TPK activity, measured with the synthetic substrate poly(Glu80-NaTyr20), is also higher.
Mol Cell Endocrinol 1989 Sep
PMID:Alkali-resistant protein phosphorylation and tyrosine kinase activity of epithelial cell types from normal and metaplastic canine prostates. 258 63

The cdc2+ gene function plays a central role in the control of the mitotic cell cycle of the fission yeast Schizosaccharomyces pombe. Recessive temperature-sensitive mutations in the cdc2 gene cause cell cycle arrest when shifted to the restrictive temperature, while a second class of mutations within the cdc2 gene causes a premature advancement into mitosis. Previously the cdc2+ gene has been cloned and has been shown to encode a 34 kDa phosphoprotein with in vitro protein kinase activity. Here we describe the cloning of 11 mutant alleles of the cdc2 gene using two simple methods, one of which is presented here for the first time. We have sequenced these alleles and find a variety of single amino acid substitutions mapping throughout the cdc2 protein. Analysis of these mutations has identified a number of regions within the cdc2 protein that are important for cdc2+ activity and regulation. These include regions which may be involved in the interaction of the cdc2+ gene product with the proteins encoded by the wee1+, cdc13+ and suc1+ genes.
Mol Gen Genet 1989 Jul
PMID:Molecular cloning and sequence analysis of mutant alleles of the fission yeast cdc2 protein kinase gene: implications for cdc2+ protein structure and function. 267 50


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