Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01275 (glucagon)
 26,492 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In rat skin the histidase activity was observed 2--3 days before delivery; it was increased at the first days of postnatal development, achieving a maximal level at the 5th day and then it was decreased (within 2--3 weeks of postnatal development) to the level activity, which was found in adult animals. Concentration of urocaninic acid in skin correlated with the histidase activity. Content of urocaninic acid in skin and the histidase activity were altered under effect of administration of cylic-3',5'-AMP, dibutyryl cyclic-3',5'-AMP, glucagon, sodium fluoride, theophylline, actinomycin D and cycloheximide.
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PMID:[Role of cyclic adenosine-3',5'-monophosphate in the regulation of histidase in the skin in the process of ontogeny]. 19 91

The mechanisms by which estrogen, glucocorticoid, glucagon, and adenosine 3':5'-monophosphate (cAMP), regulators which participate in the postnatal development of rat liver histidase, elevate the catalytic activity of this enzyme have been explored. A monospecific antibody against homogeneously purified preparations of rat liver histidase has been elaborated in the goat. Employing this antibody in immunotitration experiments, it has been demonstrated that the elevations of hepatic histidase activity elicited by administration in vivo of estradiol-17beta, cortisol acetate, glucagon, and N6,O2'-dibutyryl adenosine 3':5'-monophosphate (dibutyryl cAMP) are paralleled, in each instance, by equivalent increments in immunoprecipitable histidase protein. Following administration of each of the three hormones and dibutyryl cAMP, rates of [14C]leucine incorporation in vivo into rat liver histidase, isolated by immunoprecipitation, relative to incorporation rates into total soluble hepatic protein, increase in magnitudes which are comparable to increases in enzyme amount and catalytic activity. It is thus inferred that estrogen, glucocorticoids, and glucagon, via cAMP, each regulate rat liver histidase development at specific postnatal stages by inducing increases in histidase biosynthetic rates.
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PMID:Effects of estrogen, glucocorticoid, glucagon, and adenosine 3':5'-monophosphate on catalytic activity, amount, and rate of de novo synthesis of hepatic histidase. 19 32

Synthesis of rat liver histidase is under multihormonal control; estrogen, glucocorticoid, and glucagon, via cAMP, induce this enzyme. By means of in vivo [3H]leucine incorporation into immunoprecipitated histidase, relative to that incorporated into total soluble protein, we have now demonstrated that de novo hepatic histidase synthesis, as well as catalytic activity, is selectively increased following hypophysectomy. Treatment of hypophysectomized rats with physiological levels of triiodothyronine (T3) diminished histidase synthetic rates and catalytic activities to normal levels, despite concomitant elevation in total soluble protein synthesis. Thyrotoxic doses of T3 further reduced histidase synthesis to barely measurable rates. Since thyroid hormone is under pituitary regulation, this hormone may be primary in the hypophyseal suppression of histidase. Estrogen does not induce hepatic histidase in the hypophysectomized rat. However, administration of the histidase suppressor, T3, or prolactin, which in itself has no effect on this enzyme, was ineffective in reinstating estrogen inducibility of histidase in the hypophysectomized animal. Thus, some as yet unknown hypophyseal agent is required for estrogenic inducibility of this liver enzyme.
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PMID:Effects of hypophysectomy and triiodothyronine on de novo biosynthesis, catalytic activity, and estrogen induction of rat liver histidase. 739 Oct 78

The effect of dietary protein on the expression of histidase (Hal) was investigated to understand the mechanism of induction of histidase by a high protein diet. In this study, we examined the following: 1) the effect of 0, 6, 18, 35 and 50% casein diets on hepatic and epidermal Hal activity, amount of the enzyme and Hal-mRNA; 2) the effect of a high histidine diet (1.25%) on Hal expression; 3) the response of Hal expression in rats fed a 10% casein diet and injected with glucagon (0.6 mg /(100 g body wt.d); and 4) the half-lives of the enzyme and Hal-mRNA in rats fed an 80% casein diet for 7 d followed by a protein-free diet. Hal activity increased as the protein content in the diet increased (r = 0.986, P < 0.001) and was associated with a significant increase in Vmax without a change in Km. The dietary regulation was liver specific because skin Hal was unresponsive. Increments in hepatic Hal activity were accompanied by concomitant significant increases in the amount of histidase and its mRNA. The response was more pronounced in rats fed diets containing >18% casein. Rats fed a 12% casein diet containing 1.25% histidine did not have different Hal activity and mRNA levels compared with rats fed a 12% casein diet, indicating that Hal expression is not modified by its substrate. Injection of glucagon into rats fed the 10% casein diet increased Hal activity threefold and Hal- mRNA expression fivefold compared with uninjected rats fed the same diet. The apparent half-life of hepatic histidase in protein-depleted rats previously fed an 80% casein diet was 2.8 d, whereas the half-life of Hal-mRNA was 17 h. In summary, these data support the hypothesis that Hal expression is regulated by dietary protein at the pretranslational level in rat liver, and that glucagon is one of the hormones involved in the induction of Hal.
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PMID:Histidase expression is regulated by dietary protein at the pretranslational level in rat liver. 956 87

The effect of glucagon and hydrocortisone was investigated to understand the mechanism of induction of hepatic histidase gene. In this study, glucagon (0.6 mg/100 g body wt/d) was injected to rats fed 10% casein diet. After 3 h of the last injection, histidase activity and amount of enzyme were induced by 3 fold and histidase mRNA concentration by 6 fold. Injection of hydrocortisone (2 mg/100 g body wt/d) increased 100% histidase activity and mRNA concentration and by 150% the amount of enzyme after 3 h of the last injection. These results indicate that glucagon is a better inductor of histidase gene expression than hydrocortisone. Another purpose of the study was to evaluate if a protein-free/high carbohydrate diet could reverse the induction of Hal expression produced by a high protein diet. Hal activity, amount of enzyme and mRNA concentration was repressed by 68, 88 and 95% respectively by a protein-free/high carbohydrate diet. Injection of glucagon reversed partially the effect of a high carbohydrate diet, however, injection of hydrocortisone under the concentration used in these experiments did not reverse the effect of a high carbohydrate diet. These results support the evidence that hepatic histidase gene expression is probably regulated transcriptionally by hormones.
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PMID:Regulation of histidase gene expression by glucagon, hydrocortisone and protein-free/high carbohydrate diet in the rat. 980 19

Glucagon has been postulated as an important physiological regulator of histidase (Hal) gene expression; however, it has not been demonstrated whether serum glucagon concentration is associated with the type and amount of protein ingested. The purpose of the present work was to study the association between hepatic Hal activity and mRNA concentration in rats fed 18 or 50% casein, isolated soy protein, or zein diets in a restricted schedule of 6 h for 10 days, and plasma glucagon and insulin concentrations. On day 10, five rats of each group were killed at 0900 (fasting), and then five rats were killed after being given the experimental diet for 1 h (1000). Rats fed 50% casein or soy diets showed higher Hal activity than the other groups studied. Rats fed 50% zein diets had higher Hal activity than rats fed 18% casein, soy, or zein diets, but lower activity than rats fed 50% casein or soy diets. Hal mRNA concentration followed a similar pattern. Hal activity showed a significant association with serum concentrations of glucagon. Serum glucagon concentration was significantly correlated with protein intake. Thus the type and amount of protein consumed affect Hal activity and expression through changes in serum glucagon concentrations.
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PMID:Soy protein, casein, and zein regulate histidase gene expression by modulating serum glucagon. 1237 30

Histidase (Hal), the amino acid-degrading enzyme of histidine, is regulated by the protein content of the diet and by hormones such as glucocorticoids and glucagon. However, glucagon can activate the following two possible transduction pathways: protein kinase A (PKA) and protein kinase C (PKC). The aim of this study was to isolate the 5'-flanking region of rat Hal gene to locate possible cAMP- and glucocorticoid-responsive elements and to identify whether the activation of the Hal promoter by glucagon occurs via PKA or PKC. The results showed that glucagon was able to induce Hal expression 1.5-fold in primary hepatocytes. The addition of phorbol 12-myristate,13-acetate (PMA) and forskolin to hepatocytes increased Hal mRNA concentration by 100 and 40%, respectively. To identify the Hal gene regulatory region, a 1248-bp fragment of the 5'-region was obtained. The transcription initiation site was located at 404 bp from ATG. The sequence did not show consensus TATA-like or CAAT-like boxes in the first 100 bp upstream from the transcription start site. The promoter contained six GC rich boxes, seven putative AP1 binding sites, and four glucocorticoid-responsive elements. The putative Hal promoter region was cloned into the pGL3basic vector and transfected into HepG2 cells. Luciferase expression was significantly stimulated by glucagon (0.9-fold), forskolin (0.9-fold), PMA (2.0-fold), and dexamethasone (2.9-fold). This evidence supports that the Hal gene is turned on by glucocorticoids and by glucagon either via PKC or PKA, but prefers the PKA pathway.
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PMID:Regulation by glucagon of the rat histidase gene promoter in cultured rat hepatocytes and human hepatoblastoma cells. 1574 Dec 41

Increased dietary protein intake rapidly (3 h) decreases hepatic malic enzyme and increases hepatic histidase mRNA expression in broiler chicks. A series of experiments was conducted to determine the role that glucagon or a specific mixture of dietary amino acids might have in regulating the rapid changes in mRNA expression of these enzymes, when dietary protein intake is increased. Three hours after the injection of glucagon (240 microg/kg of BW) into the brachial vein of broiler chicks, hepatic malic enzyme mRNA expression was significantly lower and hepatic histidase mRNA expression was significantly greater than the level detected in saline-injected chicks. In addition, broiler chicks fed a high (40 g/ 100 g of diet) protein diet had significantly higher plasma glucagon levels at 1 and 3 h after initial access to this diet than broiler chicks fed a basal (22 g/100 g of diet) protein diet. The plasma glucagon concentration, however, was not different between the chicks fed the 2 dietary protein levels at 2 h after the initial access to the 2 diets. When a mixture of indispensable or dispensable amino acids was added to the basal diet to equal the concentrations of the individual indispensable or dispensable amino acids in the high protein diet, hepatic mRNA expression of malic enzyme and histidase were intermediate to the expression found in chicks fed the basal and high protein diet. The results indicate that glucagon may mediate the changes in the mRNA expression of malic enzyme and histidase in response to dietary protein intake and that total amino acid intake rather than the ingestion of specific amino acids regulates the mRNA expression of malic enzyme and histidase in chicks.
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PMID:The role of glucagon in regulating chicken hepatic malic enzyme and histidase messenger ribonucleic acid expression in response to an increase in dietary protein intake. 1661 60