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)

The possibility that chicken growth hormone (cGH) can be phosphorylated has been examined. Both native and biosynthetic cGH were phosphorylated by cAMP-dependent protein kinase (and gamma -32P-ATP). The extent of phosphorylation was however less than that observed with ovine prolactin. Under the conditions employed, glycosylated cGH was not phosphorylated. Chicken anterior pituitary cells in primary culture were incubated in the presence of 32P-phosphate. Radioactive phosphate was incorporated in vitro into the fraction immunoprecipitable with antisera against cGH. Incorporation was increased with cell number and time of incubation. The presence of GH releasing factor (GRF) increased the release of 32P-phosphate labelled immunoprecipitable GH into the incubation media but not content of immunoprecipitable GH in the cells. The molecular weight of the phosphorylated immunoreactive cGH in the cells corresponded to cGH dimer.
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PMID:Phosphorylation of chicken growth hormone. 221 76

We have studied the mechanisms that regulate the expression of the mouse gene encoding steroid 11 beta-hydroxylase (11 beta-OHase), a steroidogenic cytochrome P450 enzyme that is expressed only in the adrenal cortex. DNase I footprinting and gel-mobility shift analyses revealed potential regulatory elements at -370 and -310 in the 11 beta-OHase promoter region. To determine the contributions of these elements to expression, we altered their sequences by site-selected mutagenesis and studied promoter activity after transfection into Y1 mouse adrenocortical tumor cells. Mutation of either element markedly decreased basal promoter activity but did not affect the response to treatment with 8-bromo cAMP. These experiments thus document the functional roles of these elements, within the context of the intact promoter, in constitutive expression of 11 beta-OHase. Moreover, addition of either of these elements to p-40GH, a 5'-deletion plasmid containing 11 beta-OHase sequences from -40 to +8 upstream of a growth hormone reporter gene, significantly increased promoter activity but did not confer cAMP responsiveness. Finally, increased expression was seen after transfection of Y1 derivatives deficient in cAMP-dependent protein kinase, indicating that neither element required cAMP-dependent protein kinase activity. These studies thus define two regulatory elements that play important roles in 11 beta-OHase expression.
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PMID:Identification and characterization of two upstream elements that regulate adrenocortical expression of steroid 11 beta-hydroxylase. 223 42

Highly purified growth hormone (GH) has been isolated from Atlantic salmon (Salmo salar) pituitaries by extraction with acid acetone, acidic precipitation, and reversed-phase high-performance liquid chromatography (HPLC). The yield was 2.5 mg/g wet tissue. The Atlantic salmon GH (sGH) emerged as a single symmetrical peak after HPLC on a reverse phase C18 column. SDS-gel electrophoresis revealed only one band with an estimated molecular weight of 23,000. Atlantic sGH showed a uniform molecular weight, but two-dimensional (2D) gel electrophoresis of the purified sGH revealed charge heterogeneity with pI's ranging from 6.5 to 8.2. Treatment of the purified sGH with alkaline phosphatase concentrated these different forms into a single more alkaline position (pI 8.2) indicating removal of acidic groups. These results were documented using both silver- and immunostaining of the 2D SDS gels. The purified sGH was phosphorylated in vitro by a calmodulin-dependent protein kinase. Phosphorylation of sGH may be a post-translational modification resulting in several molecular forms with variable acidity. Analysis of the amino acid composition of Atlantic sGH revealed homology with GHs isolated from other teleost species and the amino-terminal sequence showed only three different amino acids within the first 25 residues compared to GH isolated from chum salmon (Oncorhynchus keta) and coho salmon (Oncorhynchus kisutch) pituitaries. Atlantic sGH had a methionine as the amino-terminal residue. Antibodies against chum sGH cross-reacted with Atlantic sGH. Antibodies against either Atlantic or chinook (Oncorhynchus tschawytscha) salmon prolactin or human GH did not cross-react with Atlantic sGH. Atlantic sGH was shown to have a slight growth-promoting activity in the rat tibia assay.
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PMID:Purification and characterization of Atlantic salmon growth hormone and evidence for charge heterogeneity. 228 75

The steroid 21-hydroxylase (21-OH) gene is selectively expressed in the adrenal cortex and is transcriptionally regulated by ACTH. We examined the role of the 5'-flanking sequences of 21-OH in this regulated expression by analyzing their ability to direct the expression of a human growth hormone (hGH) reporter gene upon transfection into Y1 mouse adrenocortical tumor cells. The 330 bp of 5'-flanking sequences directed basal and hormonally-inducible expression of hGH in Y1 cells, but did not direct expression in I-10 mouse testicular Leydig cells. Both constitutive and hormonally-inducible expression required a functional cAMP-dependent protein kinase. These results indicate that the first 330 bp of 5'-flanking sequences of the 21-OH gene contain sufficient information for cell-specific and hormonally regulated expression, and that this expression requires the integrity of cAMP-dependent protein kinase. Markedly lower expression of hGH was seen when 156 bp of 5'-flanking sequences were placed in front of the reporter gene, suggesting that sequences between -330 and -156 are essential for expression. The addition of sequences from -330 to -150 to the p-156GH plasmid, in either the correct or the reverse orientation, restored promoter activity to approximately the level obtained with the 330 bp of 5'-flanking sequences. Moreover, the addition of sequences from -230 to -150 increased by 5-fold the expression of hGH driven by the heterologous thymidine kinase promoter. Based on these results, we conclude that an enhancer element is contained within the sequences from 230 to 150 bp upstream of the transcription initiation site.
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PMID:Regulation of 21-hydroxylase gene expression. 254 98

The mouse gene encoding adrenal steroid 11 beta-hydroxylase (11 beta-OHase) has been cloned and the nucleotide sequence of its 5' end has been determined. The coding regions sequenced are homologous (75%) to the sequence of bovine 11 beta-OHase cDNA. The 5'-flanking region of the 11 beta-OHase gene contains a potential cAMP response element (TGACGTGA) located 56 base pairs upstream of the transcription initiation site (position -56) and two motifs at positions -249 and -148 which are similar to an element postulated to be required for the expression of 21-hydroxylase. Transfection of mouse Y1 adrenocortical tumor cells and MA-10 testicular Leydig cells with plasmids containing the 11 beta-OHase promoter linked to a growth hormone reporter gene showed that the 11 beta-OHase promoter can direct cell-specific expression. Deletion analyses of the 5'-flanking region suggest that multiple sequence elements, one of which is located between positions -425 and -338 and a second between positions -338 and -123, interact to produce full levels of promoter activity. Mutant Y1 cells defective in cAMP-dependent protein kinase activity do not express growth hormone driven by the 11 beta-OHase promoter, indicating that expression of 11 beta-OHase in Y1 cells requires an intact cAMP second messenger system. Moreover, mutation of the putative cAMP response element at position -56 abolishes expression. These experiments thus present a useful system for the investigation of cis-acting elements involved in the transcriptional regulation of 11 beta-OHase.
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PMID:Structural and functional analysis of the promoter region of the gene encoding mouse steroid 11 beta-hydroxylase. 278 17

We have purified and characterized the 50 kd activator protein 2 (AP-2), another enhancer-binding protein interacting with the human metallothionein IIA (hMT-IIA) gene control region. Purified AP-2 activates transcription in vitro from a hybrid promoter containing hMT-IIA upstream sequences. AP-2 also recognizes control elements of the human growth hormone, c-myc, and H-2Kb genes, and the SV40 and bovine papilloma virus enhancers. Multiple synthetic copies of the hMT-IIA high-affinity AP-2 binding site can act as efficient, cell-type-specific enhancer elements; their activity increases after treatment of cells with phorbol ester or cAMP-elevating agents. In contrast, a synthetic enhancer recognized by factor AP-1 is activated only by phorbol ester. AP-2 appears to mediate transcriptional activation in response to two different signal-transduction pathways, one involving the phorbol-ester- and diacylglycerol-activated protein kinase C, the other involving cAMP-dependent protein kinase A.
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PMID:Transcription factor AP-2 mediates induction by two different signal-transduction pathways: protein kinase C and cAMP. 282 55

The steroid 21-hydroxylase (21-OHase) gene is selectively expressed at high levels in cells of the adrenal cortex and is transcriptionally regulated by corticotropin (ACTH). In this study, we examined the contribution of cis-acting nucleotide sequences to the regulated expression of the mouse 21-OHase gene. The 5'-flanking sequences of the mouse 21-OHase gene, extending 330 bp upstream from the transcription initiation site, were placed in front of the human growth hormone (hGH) reporter gene, and expression of the fusion gene was measured following transient transfection in Y1 mouse adrenocortical tumor cells. The 330 bp of 21-OHase flanking sequence directed both basal and ACTH-stimulated expression of hGH in Y1 adrenocortical cells but did not direct hGH expression in I-10 mouse testicular Leydig cells or in mouse fibroblast L cells. The 21-OHase/hGH fusion gene was poorly expressed in Y1 mutants defective in cAMP-dependent protein kinase activity. These results indicate that sequences necessary for adrenal cell-selective and ACTH-regulated expression of the 21-OHase gene reside within the first 330 bp of 5'-flanking DNA and that constitutive expression of the gene requires the integrity of cAMP-dependent protein kinase. The constitutive expression of hGH in Y1 cells was decreased dramatically (40-fold) when the 21-OHase flanking sequences in front of hGH were shortened to 156 bp from the transcription initiation site and was restored when the upstream sequences of the 21-OHase gene, from -330 to -150, were added back; the sequences from -330 to -150 were equally effective in either the correct or reverse orientation. From these observations, we conclude that an enhancer element is contained within the sequences from -330 to -150 bp upstream of the 21-OHase transcription initiation site.
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PMID:An enhancer element and a functional cyclic AMP-dependent protein kinase are required for expression of adrenocortical 21-hydroxylase. 284 6

Incubation of cultured ovine pituitary cells with the tumor-promoting phorbol ester, 12-O-tetradecanoylphorbol 13-acetate (TPA) (0.1-100 nM), caused a dose-related stimulation of both growth hormone (ED50 approximately 4 nM) and prolactin (ED50 approximately 14 nM) secretion. Stimulation by TPA (100 nM) produced a substantial 10-fold increase in growth hormone with a smaller, 2-fold rise in prolactin secretion over 30 min; significant effects on the release of both hormones occurred within 2 min. Treatment with TPA also produced a small, time- and concentration-dependent rise in cellular cyclic AMP content which reached, at maximum, a level 20-30% over basal values. Non-tumor-promoting phorbol esters did not stimulate the secretion of either growth hormone or prolactin. In the presence of TPA (10 nM), dopamine (1-1000 nM) suppressed prolactin secretion to a level close to that observed for maximal inhibition of unstimulated cells. At high concentrations (0.1-1.0 microM) dopamine also partially attenuated (by 43%) the TPA-induced stimulation of growth hormone secretion. Somatostatin (0.01-1.0 microM) completely inhibited the substantial (approximately 9-fold) TPA-induced stimulation of growth hormone secretion (inhibitory ED50 approximately 47 nM), and also suppressed TPA-stimulated prolactin secretion to the control level. Our results suggest that activation of protein kinase-C may be involved in the stimulatory regulation of both growth hormone and prolactin secretion in sheep pituitary cells. Failure of TPA to attenuate the inhibitory activity of dopamine and somatostatin suggests that inhibitory regulation occurs at, or beyond, the point in the secretory process regulated by protein kinase-C.
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PMID:Effects of dopamine and somatostatin on phorbol ester-stimulated prolactin and growth hormone secretion. 287 53

In experiments designed to study the mechanism by which peptide hormones binding to their plasma membrane receptors stimulate the expression of specific genes, the transcription of two neuroendocrine genes, prolactin and growth hormone, was analyzed in a rat pituitary cell line. The results showed that cyclic adenosine monophosphate (cyclic AMP) stimulates the transcription of discrete subsets of eukaryotic genes by at least two independent molecular mechanisms. Cyclic AMP stimulated growth hormone gene transcription and phosphorylation of a 19,000-dalton nuclear protein; this appears to reflect direct nuclear actions of the cyclic AMP-dependent protein kinase. In contrast, the stimulation by cyclic AMP of prolactin gene transcription appears to reflect activation of a discrete calcium-dependent event.
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PMID:Cyclic AMP regulation of eukaryotic gene transcription by two discrete molecular mechanisms. 299 47

The N-terminal part sequences of pituitary growth hormone, N alpha-acetyl-hGH 7-13 and hGH 6-13, promoted conversion of glycogen synthase b to glycogen synthase a in skeletal muscle and adipose tissue when injected intravenously. The peptides also caused conversion of phosphorylase a to phosphorylase b in liver and adipose tissue, but not in muscle, where the peptides antagonised activation of phosphorylase. Synthase phosphatase activity in muscle and phosphorylase phosphatase activity in liver increased after injection of peptide, with time courses of change similar to those seen for muscle synthase and liver phosphorylase activities. Injection of peptide also decreased both the cyclic AMP dependent and independent synthase kinase activities in muscle. These results show that the insulin-like activities of these peptides on glycogen synthase and phosphorylase involve both increases in protein phosphatase activities and inhibition of protein kinase activities. These results are discussed in relation to the insulin-like activities of growth hormone.
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PMID:Activation of phosphoprotein phosphatases by growth hormone sequences with insulin-like activity. 303 64


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