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)

Several aspects of the cyclic 3', 5'-adenosine monophosphate system of rat mammary glands were investigated including effects of stage of pregnancy and lactation upon tissue cyclic 3', 5'-adenosine monophosphate amounts and adenyl cyclase, cyclic 3', 5'-adenosine monophosphate phosphodiesterase, and protein kinase activities. Cyclic 3', 5'-adenosine monophosphate decreased at early lactation, and this decrease coincided with an increase in phosphodiesterase activity. Adenyl cyclase activity remained unchanged from late pregnancy to end of lactation. At late pregnancy, activity of protein kinase was about the same as during lactation indicating that increase in protein kinase activities in the glands precedes increases in activities of other major enzymes and the increase in ribonucleic acids in late pregnancy or early lactation. Epinephrine, prolactin, growth hormone, thyroxine, and prostaglandine caused 60, 80, 140, 200, and 270% increases in adenyl cyclase activity in vitro.
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PMID:Changes in the cyclic 3', 5'-adenosine monophosphate system of rat mammary gland during lactation cycle. 16 62

1. The effects of thyroliberin were studied in cultured rat pituitary-tumour cells that synthesize and secrete prolactin (the GH4C1 cell strain). 2. Prolactin and cyclic AMP were measured by radioimmunological methods, and a cyclic AMP-dependent protein kinase was characterized by using histone as substrate. 3. Prolactin release was studied after 5-60min of treatment, and synthesis after 48h of treatment with thyroliberin. One-half maximum stimulation of release and synthesis were observed at 0.25 and at 4nM respectively. 4. Cyclic AMP was temporarily increased in cell suspensions after treatment with thyroliberin, and one-half maximum stimulation was observed at 25nM. 5. Dibutyryl cyclic AMP increased prolactin release and synthesis, one-half maximum effects being obtained at 20 micronM. 6. A cyclic AMP-dependent protein kinase, which was one-half maximally stimulated at 30 nM-cyclic AMP, was demonstrated. 7. An increase in the activity ratio (-cyclic AMP/+cyclic AMP) of the cyclic AMP-dependent protein kinase was observed after treatment with thyroliberin. Total protein kinase activity in the presence of cyclic AMP was unaltered. The time-course of enzyme activation was similar to that of cyclic AMP formation and corresponded to the time when prolactin release was first observed. 8. It is concluded that thyroliberin induces cyclic AMP formation, resulting in the activation of a cyclic AMP-dependent protein kinase.
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PMID:Effect of thyroliberin on the concentration of adenosine 3':5'-phosphate and on the activity of adenosine 3':5'-phosphate-dependent protein kinase in prolactin-producing cells in culture. 19 21

The pituitary-specific transcription factor Pit-1 is a cell-specific activator of prolactin and growth hormone gene transcription in the anterior pituitary. Pit-1 has also been shown to mediate both thyrotropin-releasing hormone (TRH) and cAMP stimulation of the prolactin and thyrotropin beta-subunit (TSH beta) genes. The molecular mechanism by which Pit-1 mediates these stimulatory effects remains unclear. At least three Pit-1-binding elements within the TSH beta gene mediate responsiveness to TRH and cAMP. The present studies were designed to test the hypothesis that phosphorylation is an important modulator of Pit-1 interaction with the TSH beta gene. TSH beta elements bind less well to nonphosphorylated Pit-1 than to phosphorylated Pit-1 and are weak activators of gene expression, unlike high-affinity Pit-1 binding sites in the prolactin and growth hormone genes. Phosphorylation by protein kinase A or C enhances Pit-1 binding to TSH beta elements 3- to 8-fold. Conversely, phosphorylation generally reduces binding of Pit-1 to elements within the prolactin and growth hormone genes. A variation within the consensus sequence for Pit-1 binding in TSH beta gene elements [A(A/T)(A/T)AATNCAT in the TSH beta gene versus A(A/T)(A/T)TATNCAT in the prolactin and growth hormone genes] could explain these differences. These elements may limit basal activation of the TSH beta gene by binding less well to nonphosphorylated Pit-1 while conferring hormonal stimulation through enhanced binding of phosphorylated Pit-1.
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PMID:Hormonal regulation of the thyrotropin beta-subunit gene by phosphorylation of the pituitary-specific transcription factor Pit-1. 132 28

Two protein kinase-inhibitors, 6-dimethyl amino purine and 2-amino purine inhibited induction of beta-casein synthesis by prolactin when added to the culture medium of rabbit mammary explant and cells. The accumulation of the mRNA for alpha s1- and beta-caseins and for whey acidic protein did not take place in the presence of the inhibitors whereas beta-actin mRNA concentration was not altered. In the same experimental conditions, H7, an inhibitor of protein kinase C and, to a lower extent, of protein kinase A did not prevent prolactin from acting. These data suggest for the first time that specific protein kinases are involved in the transduction of the prolactin signal to milk protein genes.
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PMID:6-Dimethyl amino purine and 2-amino purine inhibit the induction of expression of milk protein genes by prolactin. 139 84

The immunoregulatory function of prolactin (PRL) and the mechanism of its action in mammals seem to be well documented. Reciprocal interdependence between PRL secretion and immune system function is essential for normal ontogeny, development and aging. PRL receptors in lymphocytes participate in the transduction of its regulatory signal into the intracellular enzymatic machinery including that of the nucleus, leading to the expression of some genes and to the synthesis of new proteins. Activation of phosphoinositide turnover and subsequent increase in protein kinase-C activity seems to be a possible mechanism acting in the regulatory influence of PRL on mammalian immune cells. These cells in turn, under mitogen or antigen stimulation, secrete a substance with PRL-like activity. The regulatory function of PRL within the avian immune system is less well known, but it seems to have some features in common with those in mammals. Direct mitogenic action on thymocytes and splenocytes in the chicken might indicate the existence of PRL receptors in these cells and could explain the immunostimulatory effect of PRL observed in vivo, which is dependent on the time of hormone administration. As the avian PRL stimulates mitogenesis of rat Nb2 lymphoma cells, the mechanism of direct PRL action on immune cells in mammals and birds seems to be similar. PRL in chickens also modifies the level and the diurnal rhythm of corticosterone which, in turn, influences the immunoregulatory effect exerted by PRL. Thus, PRL seems to be an important factor, influencing directly or indirectly the avian immune system.
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PMID:Prolactin as an immunoregulatory hormone in mammals and birds. 144 15

In an attempt to characterize the ras signaling pathway, we studied the effects of expression vectors encoding the valine 12 mutant ras oncogene on rat prolactin (rPRL) promoter activity. Using this approach we have been able to dissect the interplay between the ras and the protein kinase A (PKA) pathways as they relate to neuroendocrine gene activation. Here we show that the ras oncogene product induces rPRL promoter activity selectively from 5- to 14-fold in GH4 rat pituitary tumor cells, whereas it has a minimal effect on the SV40 early promoter and no effect on the Rous sarcoma virus (RSV) or rat growth hormone promoters. By contrast, an inactivated form of ras (N-17 ras) did not stimulate the rPRL promoter, but rather inhibited it to 40% of control. Of note, activation of the PKA pathway by two different methods decreased the fold activation mediated by ras by at least 50%, whereas inhibition of the PKA pathway accentuated ras activation of the rPRL promoter. Although rPRL promoter activity is consistently induced by PKA activation in control GH4 cells, acute ras oncogene expression inhibited forskolin induction of rPRL promoter activity. Moreover, this ras-mediated interference of the forskolin activation of rPRL promoter activity was also noted in GH4 cells stably expressing ras. Taken together, these data show that the valine 12 ras oncogene activates the rPRL promoter selectively and, more importantly, that the ras and PKA signaling pathways are mutually antagonistic with respect to specific transcriptional activation of a neuroendocrine gene.
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PMID:The ras and protein kinase A pathways are mutually antagonistic in regulating rat prolactin promoter activity. 162 May 44

To determine whether GH and prolactin could be phosphorylated, turkey GH, chicken GH, chicken prolactin and turkey prolactin were incubated in vitro with the catalytic subunit of protein kinase A and [gamma-32P]ATP. Phosphorylation was assessed after sodium dodecyl sulphate-polyacrylamide gel electrophoresis, Western blotting and autoradiography. Polyacrylamide electrophoresis showed that both purified native chicken GH and turkey GH were phosphorylated under the conditions employed. However, the glycosylated variant of chicken GH did not appear to be labelled. Chicken prolactin, turkey prolactin and the glycosylated variant of turkey prolactin were all intensely phosphorylated by protein kinase A. Ovine and rat prolactins could also be phosphorylated by protein kinase A. The phosphate content of different native prolactin (turkey, ovine and rat) and GH (ovine and chicken) preparations was also determined and found to be significant. Chicken pituitary cells in primary culture incorporated 32P in GH- and prolactin-like bands isolated by non-denaturing polyacrylamide gel electrophoresis, and this was stimulated by phorbol myristate acetate. Phosphorylation of GH and prolactin may thus explain some of the charge heterogeneity of these hormones.
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PMID:Phosphorylation of prolactin and growth hormone. 163 94

The present study examines the effect of chronic dopamine treatment, known to inhibit prolactin release from anterior pituitary, on two Ca2+ and K+ currents in cultured rat lactotrophs. K+ and Ca2+ currents were recorded using the whole-cell mode of the patch-clamp technique. The two types of voltage-dependent Ca2+ currents are called SD and FD (slowly deactivating and fast deactivating current component, respectively) and the two types of voltage-dependent K+ currents, IA and IK. All current types were isolated by tail current analysis. The amplitude of both normalized calcium components depended on the length of the culture (n = 48) while normalized amplitudes of both potassium currents remained constant (n = 9). Incubation of cells during 72 h with 50 microM of Actinomycin D, an inhibitor of mRNA synthesis, suggested that this increase in Ca2+ currents involved the synthesis of proteins. Long-lasting D2 receptor stimulation (8 days; 10 nM RU 24213) prevented this selective effect through activation of a pertussis toxin-sensitive G protein. We also examined whether cyclic adenosine-3',5'-cyclic-monophosphate (cyclic AMP) or Ca2+/phospholipid-dependent protein kinase (protein kinase C) could affect this development of channel activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Chronic stimulation of D2 dopamine receptors specifically inhibits calcium but not potassium currents in rat lactotrophs. 168 31

The neuropeptide galanin (GAL) is widely distributed throughout the diffuse neuroendocrine system, and is coexpressed with acetylcholine, norepinephrine, prolactin, and a variety of other messenger substances in different cell types. Bovine chromaffin cells in primary culture synthesize and store GAL along with catecholamines, chromogranin A, and enkephalin peptides, as well as other neurosecretory products, and secrete all these molecules in response to nicotinic stimulation. The regulation of GAL biosynthesis and secretion were studied by measuring changes in messenger RNA (mRNA(GAL], and peptide immunoreactivity, 24-72 h after stimulation of secretion (40 mM potassium or 10 microM veratridine), or exposure to stimulators of protein kinase C (100 nM phorbol myristate acetate) and protein kinase A (25 microM forskolin). Depolarization-induced stimulation of GAL biosynthesis, like that of enkephalin and other neuropeptides, was calcium dependent, suggesting that calcium generally mediates both exocytotic release and new peptide synthesis thus coordinating maintenance of neuropeptide levels in chromaffin cells. GAL and mRNA(GAL) were also upregulated by stimulation of protein kinase A with forskolin. Treatment with PMA increased GAL and mRNA(GAL) to an even greater extent than depolarization. Thus GAL expression can be regulated by three distinct signal transduction systems in chromaffin cells: depolarization-stimulated calcium influx, activation of protein kinase C and activation of protein kinase A, which in addition differentially up- and down-regulate the expression of several other neurosecretory proteins and peptides resulting in different patterns of GAL/neuropeptide coexistence in bovine chromaffin cells. GAL coexistence with diverse neuroendocrine substances may reflect the relative activity of these three signalling systems in other neuroendocrine cell types as well.
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PMID:Galanin gene expression in chromaffin cells is controlled by calcium and protein kinase signaling pathways. 170 Nov 35

We report that the rat pituitary cell line GH3 contains a Ca2(+)- and calmodulin-dependent protein kinase with properties characteristic of multifunctional Ca2+/calmodulin-dependent protein kinase (CaM kinase) from rat brain. The GH3 kinase exhibits the hallmark of authentic CaM kinase: conversion from Ca2(+)-dependent to Ca2(+)-independent activity following a brief initial phosphorylation in vitro. This phosphorylation occurs at a site which is similar or identical to that of the "autonomy" site of the rat brain enzyme and thus may be an autophosphorylation event. GH3 CaM kinase is phosphorylated and becomes Ca2(+)-independent in situ. Depolarization of intact cells with K+ opens calcium channels and leads to the phosphorylation of CaM kinase at the autonomy site, and the kinase becomes significantly and persistently Ca2(+)-independent. Treatment of cells with thyrotropin-releasing hormone (TRH), which activates the phosphatidylinositol signaling pathway, also generates a Ca2(+)-independent CaM kinase in situ. The primary effect of TRH on CaM kinase activity is transient and correlates with the spike of Ca2+ released from intracellular stores and the rapid phase of prolactin release from GH3 cells. This study demonstrates that CaM kinase is able to detect and respond to both calcium that enters the cell through voltage-sensitive Ca2+ channels and calcium released from internal stores via the phosphatidylinositol pathway. We find that TRH, a hormone that causes release of prolactin and was previously believed to activate primarily protein kinase C, also significantly activates CaM kinase in intact cells.
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PMID:Activation of multifunctional Ca2+/calmodulin-dependent protein kinase in GH3 cells. 184 56


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