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)

Incubation of a highly purified fraction derived from rat liver Golgi apparatus with [gamma-32P]ATP results in phosphorylation of several endogenous phosphoproteins. One phosphoprotein with an apparent Mr of 48,300 is radiolabeled to an apparent extent at least 5-fold higher than any other phosphoprotein as part of either the Golgi apparatus or highly purified rat liver fractions derived from the rough endoplasmic reticulum, mitochondria, plasma membrane, coated vesicles, cytosol, and total homogenate. Approximately 70% of the 48.3-kDa phosphoprotein appears to be a specific extrinsic Golgi membrane protein with the phosphorylated amino acid being threonine. The protein kinase which phosphorylates the 48.3-kDa protein is an intrinsic Golgi membrane protein and is dependent on Mg2+, independent of Ca2+, calmodulin, and cAMP, and is inhibited by N-ethylmaleimide. Preliminary evidence suggests that there are also intrinsic membrane protein kinases in the Golgi apparatus which are dependent on Ca2+ and cAMP. The physiological role of the above phosphoproteins and protein kinases is not known.
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PMID:Phosphoproteins and protein kinases of the Golgi apparatus membrane. 405 4

Stimulation of exocytosis in exocrine glands is associated with an increased phosphorylation of several particulate proteins. Irrespective of the type of secretagogue (cAMP-dependent agonists, calcium-dependent agonists, calcium ionophores, phorbol esters) exocytosis is always accompanied by an enhanced phosphorylation of the ribosomal protein S6. It is shown by an analysis of the phosphopeptide pattern of the in vivo and the in vitro phosphorylated S6 protein that the protein kinase responsible for phosphorylation of the S6 protein during enhanced exocytosis is protein kinase C. This is so irrespective of whether the agonist uses cAMP or calcium as second messenger. Experiments with isolated guinea pig parotid gland lobules reveal that not only the acetylcholine analog carbamoylcholine, but also the beta-agonist isoproterenol lead within seconds to an increased formation of diacylglycerol. As diacylglycerol increases the affinity of protein kinase C for calcium this finding would explain why the phosphorylation pattern of the S6 protein reflects activation of protein kinase C also under conditions where (as in the case of stimulation with beta-agonists) cAMP is the primary second messenger. It would further explain why the changes of the phosphorylation of individual histones observed during agonist-induced exocytosis in the parotid gland are quite similar for isoproterenol on one hand and carbamoylcholine on the other. A 22 K protein which becomes phosphorylated only when cAMP serves as second messenger is located in the membrane of the endoplasmic reticulum. A possible relationship of this protein with the calcium transport ATPase of the endoplasmic reticulum is under investigation.
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PMID:Regulation of protein kinases in exocrine secretory cells during agonist-induced exocytosis. 407 96

In the adrenal cortex, the adenosine 3':5'-cyclic monophosphate (cAMP)-receptor protein and the cAMP-dependent protein kinase are located in both the cytosol and endoplasmic reticulum. The cAMP-dependent protein kinase from the cytosol catalyzes the phosphorylation of ribosome-associated protein. Ribosomes washed in 0.5 M NH(4)Cl retain the substrate of the protein kinase reaction, but are dependent on the NH(4)Cl extract for in vitro protein synthesis. Dissociation of the 80S ribosomes by 0.88 M KCl, however, releases the ribosome-associated (protein) substrate of the phosphorylation reaction.
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PMID:Phosphorylation of ribosome-associated protein by an adenosine 3':5'-cyclic monophosphate-dependent protein kinase: location of the microsomal receptor and protein kinase. 432 2

Polyoma virus appears to encode a transforming function. A variety of studies lead to the conclusion that this function resides mainly, and in some instances possibly exclusively, within the virally-coded middle T-antigen. Whereas this protein was originally isolated from membranes of cells infected with polyoma virus as a 55 kilodalton species, our recent studies, using monoclonal antibodies, suggest that middle T-antigen is a family of proteins, at least one member of which (but not all others) can be associated with a protein kinase activity. Investigation of the sub-cellular location of the middle T-antigen (s), using either immunofluorescence or immunoelectron-microscopy, and the monoclonal antibodies, show them to be associated with all cytoplasmic membranes. At early times post-infection, most of the middle T-antigen is found in association with the rough endoplasmic reticulum of the cell; only a few percent can be found located at the plasma membrane. At late times post-infection, this percentage increases. These data lead to the hypothesis that structurally similar viral proteins might have different functions, expressed at different locations within the cell. Which function(s) pertain to transformation remain to be defined.
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PMID:The transforming gene of polyoma virus. 631 Nov 33

Stimulation of secretion in exocrine cells by agonists involving cAMP as second messenger is associated with the phosphorylation of a specific membrane-associated 22.4-kDa protein (protein III) (Jahn et al.). Here it is shown by subcellular fractionation of rat parotid gland lobules that protein III is associated with the endoplasmic reticulum. The submicrosomal fractions containing protein III, also contain the ATP-dependent microsomal calcium pump activity. Protein III in microsomal subfractions can be phosphorylated in vitro with catalytic subunit from cAMP-dependent protein kinase. Phosphorylated protein III contains exclusively P-serine. Protein III can be removed from ER-membranes with acid chloroform-methanol or Triton X-114, but not by high salt wash indicating that it is tightly associated with the membranes. Protein III is smaller than phospholamban and, in contrast to phospholamban, resistant to heating in SDS. A relationship between phosphorylation of protein III and microsomal calcium sequestration is discussed.
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PMID:Specific phosphorylation of a protein in calcium accumulating endoplasmic reticulum from rat parotid glands following stimulation by agonists involving cAMP as second messenger. 631 93

A model has been presented for the role of the kidney in the physiologic and pathophysiologic control of erythropoiesis. It is postulated that an oxygen deficit created by anemia or hypobaric hypoxia results in the release of prostacyclin and its metabolite 6-keto PGE1, and the release of PGE2 with ischemic hypoxia. Prostacyclin, 6-keto-PGE1, or PGE2 activation of adenylate cyclase, an increase in cyclic AMP, activation of a protein kinase and the phosphorylation of hydrolases, which have been released from lysosomes by hypoxia, lead to increased biosynthesis of erythropoietin (Ep). The mechanism of labilization of lysosomes and the release of hydrolases from these cell organelles is postulated to be related to increases in cyclic GMP levels in a renal cell. An Ep-producing human renal carcinoma cell line grown in tissue culture has been demonstrated to produce significant amounts of PGE2. Meclofenamate, an inhibitor of prostaglandins synthesis, was found to inhibit in vitro production of PGE2, Ep, and dome formation in these renal carcinoma cells, giving support to our hypothesis that pathophysiologic production of Ep tumor cells depends upon prostaglandins production. An Ep-producing clone from this renal carcinoma cell line has been developed that contains low electron density (LED) cells after the cells reach confluency, which show a cytoplasm, with abundant and widely dilated endoplasmic reticulum, an oval nucleus, dispersed chromatin, and prominent nucleoli. These are the cells responsible for dome formation and Ep production. Non-EP-producing clones have also been produced from this renal carcinoma cell line, which did not produce domes even at high cell density and had a distinctly different cell type than the Ep-producing clone. Thus, it is postulated that prostacyclin (PGI2) and its metabolite 6-keto PGE1 play a significant role in hypoxic hypoxia stimulation of Ep production and PGE2 is involved in ischemic hypoxia and renal carcinoma cell production of Ep. A modulating effect of PGE2 and PGD2, the two primary bone marrow prostaglandins, has been proposed in Ep stimulation of the erythroid progenitor cell compartment (CFU-E and BFU-E).
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PMID:Effects of prostaglandins on erythropoiesis. 654 52

Calmodulin-activated protein kinase activity in the endoplasmic reticulum fraction of rat adipocytes was identified and characterized. The major endogenous protein substrate of the calmodulin-activated kinase activity has an apparent molecular weight of 54,000 as determined by sodium dodecyl sulfate gel electrophoresis. The calmodulin-activated component of the activity was saturated at 10 microM ATP. Calcium or calmodulin alone did not increase the activity, but the simultaneous presence of calcium and calmodulin increased activity three to four-fold. Half-maximal activation of this activity occurred at 8 microM Ca2+. The addition of increasing amounts of calmodulin caused a concentration-dependent activation in the presence of calcium, which was saturable at high calmodulin concentrations. Magnesium was required for activity, with half-maximal activity occurring at 230 microM. The antipsychotic drug trifluoperazine inhibited the activation of the protein kinase activity by calmodulin, but had a negligible effect on the basal activity. Half-maximal inhibition occurred at 63 microM. Phosphorylation of the 54,000 mol. wt band was independent of cAMP, cGMP and the combination of cAMP and cAMP-dependent protein kinase. Calmodulin-activated protein kinase phosphorylated both phosphoserine and phosphothreonine residues in the 54,000 mol. wt substrate. These experiments have partially characterized a calmodulin-activated protein kinase activity from adipocytes, which appears to be a unique activity of unknown function.
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PMID:Characterization of calmodulin-activated protein kinase activity of rat adipocyte endoplasmic reticulum fraction. 670 68

Serine-specific and threonine-specific casein kinase activities have been identified in a Golgi-enriched membrane fraction isolated from the lactating guinea-pig mammary gland. The serine-specific casein kinase has been purified 2000-fold by affinity chromatography on ATP-agarose. The enzyme has an estimated Mr of 100000 as determined by sucrose gradient centrifugation and phosphorylates the serine residues of dephosphorylated guinea-pig caseins A and B in a qualitatively and quantitatively identical manner to caseins A and B secreted by lactating mammary gland explants in organ culture. The enzyme also phosphorylates casein C at serine, but not threonine residues. Studies on the relative location of the enzyme within a Golgi-enriched membrane fraction show that it is an integral component of the membrane, either in the form of a transmembrane protein or exposed on the luminal side of the membrane. Although casein kinase activity is not associated with the endoplasmic reticulum, it remains to be proven whether it is truly a Golgi enzyme, since analysis of subcellular membrane components fractionated by sucrose gradient centrifugation shows that the particulate protein kinase activity of the lactating mammary gland does not cosediment with galactosyl transferase, possibly a reflection of the heterogeneous nature of mammary gland Golgi apparatus. It seems likely that the serine-specific casein kinase activity described is responsible for the phosphorylation of caseins in the lactating guinea-pig mammary gland, and that this occurs after the sequestration of processed but unphosphorylated caseins within the lumen of the endoplasmic reticulum.
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PMID:Characterisation of a membrane-bound serine-specific casein kinase isolated from lactating guinea-pig mammary gland. 680 32

The fifty of so phosphorylated hydroxyamino acid residues hitherto investigated in caseins from different species have been found to occur in tripeptide sequences -Ser/Thr-X-A- where X represents any amino acid residue and A is an acidic residue. This strongly suggests that phosphorylation of caseins involves basically the stepwise enzymatic recognition of primary and secondary anionic amino acid triplets where the determinants are dicarboxylic residues and phosphoseryl residues, respectively. Studies of genetic variants of bovine caseins have provided clear-cut evidence for the actual occurrence of the former recognition sites. The occurrence of the above tripeptide sequences is a necessary but not a sufficient condition for phosphorylation of caseins to occur. Possible factors of constraint such as different intrinsic properties of both phosphate acceptor residues and acidic determinants, the characteristics of the local environment in terms of overall charge and hydrophilicity, secondary structure and steric hindrance, an insufficient available pool of casein kinase(s)... are discussed. All evidence now available supports the concept that phosphorylation of caseins is a posttranslational event and it is suggested that the process may occur during the transfer of completed polypeptide chains from the smooth endoplasmic reticulum to the Golgi apparatus where most of phosphate incorporation is presumably carried out. This organelle is rich in membrane-bound specific cyclic AMP-independent kinase(s) able in vitro to rephosphorylate specifically although not completely phosphatase-treated caseins and caseinophosphopeptides.
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PMID:Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases. 701 21

1. In each of five tissues (brain, heart, spleen, mammary acini and pancreatic acini) the prominent endogenous protein substrate possessed a molecular weight between 51,900 and 56,800 on SDS gel electrophoresis. 2. Evidence was obtained for two species of protein substrate, differing slightly in molecular weight, which appear to be distributed in a tissue-specific manner. 3. One species, with a molecular weight of 52,900, was found in spleen, mammary acini and brain; the other species, with a molecular weight of 56,200, was found in heart and pancreatic acini. 4. The specific activity of calmodulin-activated protein kinase in homogenates varied from a high of 44 pmol/min/mg in brain to 4.2 pmol/min/mg in mammary acini. 5. Subcellular fractionation of these tissues demonstrated that most of the activity was found in the cytosolic fraction and a "light-particle" fraction obtained by ultracentrifugation, but the kinase was not associated with endoplasmic reticulum. 6. High concentrations of calmodulin were required to activate the protein kinase activity from each tissue. 7. Calmodulin concentrations producing half-maximal activation were 94 nM for brain, 377 nM for spleen, 132 nM for pancreatic acini, 350 nM for heart, and 117 nM for mammary acini. 8. The calmodulin-activated protein kinase activity in these tissues were similar, but the few differences in properties from tissue to tissue left open the possibility that multiple, calmodulin-activated kinase activities exist in these tissues.
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PMID:A survey of calmodulin-activated protein kinase activity in several tissues of Rattus rattus. 715 1


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