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)

Cytoplasmic and membrane fractions prepared from human peripheral-blood lymphocytes both contained cyclic AMP-dependent protein kinase activity and endogenous protein kinase substrates. Protein kinase activity in the particulate fractions was not eluted with 0.25 M-NaCl, suggesting that it was not derived from non-specifically absorbed soluble cytoplasmic protein kinase. Nor was the particulate protein kinase activity eluted by treatment with cyclic AMP, suggesting that the catalytic subunit is membrane-bound and arguing against cyclic AMP-induced translocation of particulate activity. Cyclic AMP-dependent protein-phosphorylating activity in the cytoplasmic fraction was highly sensitive to inhibition by Mn2+, and was co-eluted from DEAE-cellulose primarily with type-I rabbit skeletal-muscle kinase. Cyclic AMP-dependent phosphorylating activity in the plasma-membrane fractions was stimulated at low [Mn2+] and inhibited only at high [Mn2+]. When solubilized with Nonidet P-40, plasma-membrane protein kinase was co-eluted from DEAE-cellulose with type-II rabbit muscle kinase. These differences, together with the strong association of the particulate kinases with the particulate fraction, suggest the possibility of compartmentalized protein phosphorylation in intact lymphocytes.
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PMID:Protein phosphorylation in human peripheral blood lymphocytes. Subcellular distribution and partial characterization of adenosine 3':5'-cyclic monophosphate-dependent protein kinase. 22 56

A high level of cholesterol esterase activity, comparable to that of hormone-sensitive triglyceridase, has been demonstrated in rad adipose tissue. Essentially all of the activity was in the isolated adipocytes, primarily in the 100,000 times g supernatant fraction of the adipocytes. Cholesterol esterase activity in the 100,000 times g supernatant fraction was increased 40 plus or minus 16% by incubation with ATP (0.5 mM), Mg-2+ (1.25 mM), and cyclic adenosine 3':5'-monophosphate (cyclic AMP) (10 muM), conditions which also activated hormone-sensitive triglyceridase. Protein kinase inhibitor (rabbit skeletal muscle) blocked activation, and activation was restored by the addition of excess protein kinase (bovine skeletal muscle). In extracts prepared from adipocytes first incubated for 5 min with 10 muM epinephrine and 1 mM theophylline, there was no cyclic AMP-dependent cholesterol esterase activation, implying that the enzyme had been activated by a similar mechanism in the intact cell. The physiological role of this high level of cholesterol esterase activity in adipose tissue is unclear. Its relationship to hormone-sensitive triglyceride lipase, with which it extensively co-fractionates, and its possible involvement in fat mobilization remain to be determined.
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PMID:Cholesterol esterase in rat adipose tissue and its activation by cyclic adenosine 3':5'-monophosphate-dependent protein kinase. 23 2

Protein kinase, which was isolated from cells infected with T7, is indeed a viral gene product. This is shown by DNA-dependent synthesis in vitro. The protein kinase transfers phosphate from ATP to seryl or threonyl residues in protein. The enzyme has only a relative requirement for magnesium ions, but is only active at low ionic strength. The best substrate is lysozyme. T7 protein kinase activity is not stimulated by cyclic 3':5'-AMP and/or cyclic 3':5'-GMP. The T7 protein kinase carries -- SH groups essential for activity. There is indication that the enzyme phosphorylates itself and causes self inactivation, which may explain the fast disappearance of enzyme activity in vivo. Bacteriophage T3 also induces a protein kinase which is similar to the T7-induced enzyme in all respects tested.
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PMID:Protein kinase of bacteriophage T7. 2. Properties, enzyme synthesis in vitro and regulation of enzyme synthesis and activity in vivo. 24 Jun 95

Glycogen synthetase (2.4.1.11) forms I (independent or active) and D (dependent or passive) as well as the enzymes active in the transformation of the pathways, protein kinase and phosphatase transferase, were studied in the sensory cells and glycogen rich epidermal cells of the weakly electric fish Gnathonemus petersii (Mormyridae). For light microscopy an indirect cytochemical method which differentiated between glycogen originally present and that produced during incubation in the presence of UDPG was used. This differentiation was obtained by iodine, PAS and alpha and beta amylases. Glycogen synthetase is present in the sensory cells in the I and D forms. The epidermal cells only contain the D form. Protein kinase (active I yields D) has only been found in the sensory cells but phosphatase transferase (active D yields I) has been found in both the epidermal cells and the sensory cells, but only within certain organs. Electron microscopy studies of glycogen synthetase I and D and protein kinase were restricted to the sensory cells only. As with the light microscope it was possible to differentiate between native glycogen and newly formed glycogen. This was done using ultrathin sections and staining with uranyl acetate, lead citrate or by the PATAg reaction. It was possible from these observations to locate precisely the positions of these enzymes. In fact, glycogen synthetase I and D are found both in the sensory cytoplasm and in the sensory cavity with the polysaccharide filaments. Protein kinase is also abundant in the sensory cytoplasm especially in the periphery of the cell near the microvillary border.
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PMID:Enzyme activity during the metabolism of glycogen. II. Cytochemical study of glycogen synthetase in the sensory cells of the tuberous organ of Gnathonemus petersii (Mormyridae). 41 9

DEAE-cellulose chromatography of the 105,000 X g supernatant fraction (cytosol) obtained from popped estrous rabbit follicles revealed the presence of a single form of cAMP-dependent protein kinase, designated protein kinase 3. The iv injection of an ovulatory dose of hCG to estrous rabbits promoted the appearance of a second, transient peak of cytosol cAMP-dependent protein kinase, protein kinase 1. Protein kinase 1 was detected within 10 min of hCG administration but had regressed to undetectable levels by 24 h in corpora lutea (CL) of pseudopregnancy and by 72 h in CL of pregnancy. Ovulation and subsequent CL formation were accompanied by the appearance of a third form of cAMP-dependent protein kinase, designated protein kinase 2. Protein kinase 2 was present within 2 h after hCG administration and persisted as a major form of cytosol cAMP-dependent protein kinase throughout the life span of CL. All three forms of protein kinase were inhibited by the heat-stable protein kinase inhibitor from rabbit skeletal muscle, possessed cAMP-binding activity, and were markedly stimulated by 10(-7) M cAMP. The activity of protein kinase 3 in CL of pregnancy, in corpora albicantia, and in interstitial tissue was markedly greater than that in follicles or in CL of pseudopregnancy, while the activity of protein kinase 2 remained relatively constant throughout the luteal life span. The iv injection of a luteolytic dose of hCG to 4-day pseudopregnant rabbits promoted no alterations of the protein kinase elution profile upon DEAE-cellulose chromatography of the luteal cytosol obtained 10 min to 3 days post-hCG injection. However, with dedifferentiation of corpora albicantia into interstitial tissue, the cAMP dependency of protein kinase 2 was reduced. The results indicate that the enzymatic activity and multiplicity of cAMP-dependent protein kinases in the cytosol of ovarian structures are subject to regulation by LH (hCG) and depend upon the various reproductive stages of the rabbit.
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PMID:Rabbit ovarian protein kinases. II. Effect of an ovulatory dose of human chorionic gonadotropin or luteinizing hormone on the multiplicity of follicular and luteal protein kinases. 57 Apr 95

A procedure is described of the isolation of protein kinase, which phosphorylates isolated troponin T with a rate, 5--30 fold exceeding the phosphorylation rate of other substrates (phosvitine, caseine, protamine sulphate, H1, H2A, H2b, H3, H4 histones). Troponin T-specific protein kinase transfers 0.85--0.95 moles of P per 1 mol of dephosphorylated troponin T. It phosphorylates only N-terminal acetylated serine residue, i. e. the site of troponin T structure, which is normally phosphorylated, when the whole troponin complex is isolated from skeletal muscles. Protein kinase is incapable to phosphorylate N-terminal serine residue in a mixture of triptic peptides of troponon T.
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PMID:[Skeletal muscle troponin and phosphorylation: a site of troponin T, that is phosphorylated by specific protein kinase]. 64 84

Protein kinase activity has been detected associated with the outer surface of guinea pig peritoneal macrophages. Macrophages incubated with [gamma-32P]ATP incorporated 32P-phosphate into cell-associated proteins. Inorganic phosphate did not compete, nor could inorganic [32P]phosphate substitute as the phosphate donor, demonstrating that transfer of phosphate from ATP to protein is direct and extracellular. The macrophage-associated protein kinase was also shown to phosphorylate added acceptor protein (histone) and to be tightly associated with the cell surface. Thus, a new ectoenzyme, a protein kinase, has been detected in macrophages.
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PMID:Protein kinase activity associated with the surface of guinea pig macrophages. 70 62

Glycerol release was employed as an index of endogenous glyceride hydrolysis in rat hearts perfused by a Langendorff technique with Krebs-Henseleit-bicarbonate buffer containing 5.5 mM glucose. Changes in cardiac contractility induced by glucagon, isoproterenol, epinephrine and ouabain were associated with an increase in glycerol efflux from the heart in a dose-dependent fashion. Propranolol, a beta adrenergic blocking agent, markedly diminished the increase in glycerol release due to isoproterenol without affecting this same parameter subsequent to glucagon or ouabain infusion. Insulin, a potent antilipolytic agent in adipose tissue failed to diminish glycerol efflux elicited by any of the inotropic agents studied. Protein kinase activity ratios were employed as an index of cyclic adenosine 3':5'-monosphate levels. Increases in cardiac contractility and glycerol efflux induced by isoproterenol and glucagon were associated with increases in protein kinase activity ratios while increases in contractility and glycerol efflux induced by ouabain were not accompanied by an increase in protein kinase activity ratios.
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PMID:The effect of inotropic agents on glycerol release and protein kinase activity ratios in the isolated perfused rat heart. 83 56

Protein kinase activities were determined in liver from normal, thyroidectomized and triiodothyronine (T3)-treated rats. Changes related to thyroid hormone were observed in cytosol and nuclear protein kinase activities. When protamine was used as substrate for phosphorylation, thyroidectomy induced a decrease of protein kinase activity associated with nuclei but an increase of activity was found in the cytosol. Fifteen hours after injection of T3 the levels in nuclei and cytosol were restored to normal. When casein was used as substrate, hypothyroidism led to a lowering of protein kinase activity in both fractions and T3 treatment augmented the activity in both. These studies suggest that thyroid hormones modify hepatic protein kinase activity. Results differ depending upon the substrate used. The hormones also appear to alter the subcellular distribution of some protein kinase activities.
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PMID:Liver protein kinase activity and triiodothyronine. 83 87

Two subfractions of bovine thyroid plasma membranes, light membranes (L-membranes) and heavy membranes (H-membranes), were obtained by a discontinuous sucrose gradient centrifugation of plasma membranes. Electron microscopy of the plasma membrane and its subfractions showed that the H-membranes were very similar to the plasma membrane fraction, both contained junctional complexes, long membrane sheets, and vesicles. In contrast, the L-membranes consisted mainly of short membrane sheets and vesicles, and only a few junctional complexes. The H-membranes had greater adenylate cyclase activity which responded to thyroid-stimulating hormone (TSH) while this hormone had very little effect on the enzyme activity in the L-membranes. Despite the marked difference in TSH stimulation of adenylate cyclase activity in the H- and L-membrane fractions, specific binding of 125I-TSH was similar in both fractions. The L-membranes had higher specific activities of 5'-nucleotidase and Mg2+ATPase while (Na+ + K+)-ATPase and alkaline phosphatase activities were similar in the two subfractions. Protein kinase activity of H-membranes was not significantly stimulated by exogenous cyclic adenosine 3':5'-monophosphate (cAMP). Plasma membranes and H-membranes contained a substrate capable of being phosphorylated. Such phosphorylation was slightly increased by addition of soluble protein kinase. The phosphorylation of exogenous histone by protein kinase of plasma membranes and H-membranes was augmented by cAMP. In contrast, L-membranes had very little protein kinase activity even when exogenous histone was added. They were not a very good substrate for cytosolic protein kinase.
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PMID:Preparation and characterization of subfractions of bovine thyroid plasma membranes. 85 12


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