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)

Jejunal mucosa of 6 d-old rats were cultured for 24 and 48 h in the presence of thyroxine, insulin, pentagastrin, glucagon, epidermal growth factor (EGF) or dibutyryl-A-3:5-MP cyclic with or without dexamethasone (DX). The enzymes were assayed on the purified brush borders. The various agents added alone to the basic culture medium had no effect with the exception of DX on the levels of enzyme activities. Dexamethasone alone induced sucrase, stimulated maltase, and protected other brush border enzyme activities (aminopeptidase, lactase, and alkaline phosphatase). When added to DX-supplemented medium, only the following factors modified the levels of enzymatic activities observed with DX alone. Insulin (10(-6) M) increased maltase, alkaline phosphatase, and lactase activity to a greater extent than DX at 24 h culture, the effect being maintained at 48 h on alkaline phosphatase only. At 48 h culture, both EGF (10(-8) M) and dbcAMP (10(-3) M) decreased DX-induced sucrase activity. The latter agent also depressed DX-stimulated aminopeptidase activity.
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PMID:Organ culture of suckling rat intestine: comparative study of various hormones on brush border enzymes. 674 50

A human colon carcinoma cell line, HC84S, was established in serum-supplemented medium from a colon tumor line T84 transplanted in nude mice. These cells also grew in a serum-free, synthetic medium supplement with insulin, glucagon, epidermal growth factor, transferrin, hydrocortisone, triiodothyronine, selenium, and ascorbic acid. HC84S cells grew 3 times faster in this medium than in serum-containing medium and formed gland-like structures closely resembling the original tumor morphologically. In serum-containing medium, the cells grew as a monolayer and did not form such structures. Primary cultures from transplantable human colon tumor lines maintained in nude mice and a primary tumor from a patient were established directly in this hormone-supplemented medium in collagen-treated plastic dishes without fibroblast overgrowth. The hormone-supplemented medium may be generally useful for the establishment of human colon carcinoma cell lines.
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PMID:Hormonal control of human colon carcinoma cell growth in serum-free medium. 693 31

When [125I]iodoepidermal growth factor is incubated with freshly isolated rat hepatocytes, cell-associated radioactivity reaches apparent steady state by 60 min at 20 C and by 30 min of incubation at 37 C. When the distribution of cell-associated radioactivity is studied at different times of incubation by quantitative electron microscopic autoradiography, the ligand initially associates with the plasma membrane and is progressively internalized as a function of time. The internalized ligand preferentially associates with lysosome-like structures. Qualitatively, these events are similar to those previously obtained with labeled insulin and glucagon in this cell, but quantitatively, the internalization of epidermal growth factor is much greater. The data suggest that the ligand or its specific receptor rather than the cell type is the major determinant of the rate of internalization.
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PMID:The fate of [125I]iodoepidermal growth factor in isolated hepatocytes: a quantitative electron microscopic autoradiographic study. 697 64

Low doses (10(-14)--10(-11) M) of epidermal growth factor (EGF)/urogastrone and/or equimolar mixtures of glucagon and insulin administered to 4-day-old primary neonatal rat liver cultures stimulated both DNA synthesis and proliferation of hepatocytes within 24 h. The precise roles played in this process by EGF and the two pancreatic hormones were investigated by constructing curves of the fraction of labeled hepatocytes in mitosis and studying the dilution of incorporated [3H]thymidine with time. The results indicate that EGF both activates and then promotes prereplicative development of hepatocytes, while glucagon and insulin only promote prereplicative development.
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PMID:Effects of epidermal growth factor/urogastrone and associated pancreatic hormones on mitotic cycle phases and proliferation kinetics of neonatal rat hepatocytes in primary culture. 701 89

Insulin and glucagon were injected ip at four different circadian states into separate subgroups of female adult BALB/Cann mice that had been standardized to 12 h of light alternating with 12 h of darkness. Comparable control subgroups were injected with saline. Four, 8, 12, and 18 h after each of the four injections, subgroups of seven mice that had been injected 30 min earlier with tritiated thymidine ([4H]TdR) were killed; a total of 336 mice were used. The incorporation of [3H]TdR into DNA of the esophagus, stomach, duodenum, jejunum, caecum, colon, rectum, and spleen was subsequently determined. The results demonstrate for the first time that both hormones affect the incorporation of [3H]TdR into DNA in all of the examined organs but in different ways and at different circadian stages. The effects of these hormones were complex, but several generalizations emerged. 1) Insulin tended to increase the incorporation of [3H]TdR into DNA in the examined organs, whereas glucagon tended to decrease it. 2) Insulin was more effective in stimulating the incorporation of [3H]TdR into DNA when injected either at the end of the dark span or the beginning of the light span, as opposed to the end of the light span or the beginning of the dark span. 3) Insulin had its greatest effect on [3H]TdR incorporation into DNA in the glandular stomach and rectum, whereas glucagon had its greatest effect on the colon and spleen. 4) The effects of both insulin and glucagon were different from those of epidermal growth factor, as revealed in a similar study done by us. Our results suggest that insulin, glucagon, and epidermal growth factor play important roles in the control of growth of various endodermally derived organs.
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PMID:Circadian stage-dependent effects of insulin and glucagon on incorporation of [3H]thymidine into deoxyribonucleic acid in the esophagus, stomach, duodenum, jejunum, ileum, caecum, colon, rectum, and spleen of the adult female mouse. 704 65

This laboratory has reported previously that a cytoplasmic extract of weanling or regenerating adult rat liver (but not normal rat liver) will produce a 2.5-fold increase in the incorporation of tritiated thymidine ([3H]dThd) into liver DNA of a 34%-hepatectomized test animal. (J. Physiol. London 248: 273-284, 1975). The present study showed that hepatic stimulator substance (HSS) will stimulate DNA synthesis in normal adult rats and CF1 mice as well. The increased incorporation of [3H]dThd into DNA produced in the normal, nonhepatectomized adult rat was comparable with that induced by a 34% hepatectomy. Autoradiographic studies revealed that the [3H]dThd was incorporated into nuclear DNA and that the stimulation occurred almost exclusively in parenchymal cells. HSS was shown to be heat stable (100 degrees C for 15 min) and was precipitated but not inactivated by alcohol. Ultrafiltration and dialysis studies suggested a molecular weight slightly greater than 10,000. HSS proved to be organ specific, stimulating the liver but not the kidney, bone marrow, or spleen. HSS was found to contain no insulin, glucagon, epidermal growth factor, or peptides of the nonsuppressible insulinlike/multiplication-stimulating activity (somatomedin) group.
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PMID:Hepatic stimulator substance: physicochemical characteristics and specificity. 706 90

A biologically-active succinylated porcine relaxin was iodinated by a modification of the Bolton-Hunter method. Fibroblasts cultured from the mouse pubic symphysis and human skin were used to investigate relaxin binding sites. 125I-labelled relaxin binding to both cell types was time- and temperature-dependent. An accelerated rate of labelled hormone degradation (90%) was observed when both cell types were incubated at 37 degrees C. Specific relaxin binding sites on the mouse and human cells were observed as other peptides, such as insulin, epidermal growth factor, glucagon, hFSH and human prolactin, failed to inhibit relaxin binding. Further results indicate that porcine relaxin is mitogenic to these specific fibroblasts because increasing concentrations (10(-9) to 10(-6) M) of this hormone stimulated cell growth in vitro. These data suggest that the effect of relaxin at the target tissue level is mitotic in nature.
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PMID:Characterization of the binding of 125I-labelled succinylated porcine relaxin to human and mouse fibroblasts. 735 88

Using rat liver hepatocytes, we studied the effect of the tyrosine kinase inhibitor genistein on the Ca2+/IP3 (inositol 1,4,5-trisphosphate) and the cAMP (adenosine 3:5-cyclic monophosphate) transduction mechanisms. Genistein specifically blocked the activation of glycogen phosphorylase after EGF (epidermal growth factor). Genistein on its own partially activated phosphorylase and inactivated glycogen synthase. Genistein did not influence levels of IP3, but increased those of cAMP. This was especially clear when genistein was given together with glucagon. The data suggest an effect of a tyrosine kinase on the synthesis/degradation of cAMP.
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PMID:Effect of genistein on both basal and glucagon-induced levels of cAMP in rat hepatocytes. 748 48

In the adult rat hepatocyte, the gap junction proteins consist of a major component, connexin32 (Cx32) and a minor component, connexin26 (Cx26). Although we recently reported our success in inducing and maintaining Cx32 in adult rat hepatocytes cultured in serum-free L-15 medium supplemented with epidermal growth factor and 2% dimethyl sulfoxide, it was very difficult to induce Cx26 in the primary hepatocytes. In the present study, we found that the addition of 10(-7) M glucagon into the culture medium could dramatically induce Cx26 mRNA and protein. Although the expression of Cx32 mRNA was also influenced by glucagon, the increase of the expression was small. Immunocytochemically, Cx26-positive spots were observed between most adjacent cells and were co-localized with the Cx32-positive spots. We also examined whether 0.5 mM dibutyl cyclic AMP could induce expression of Cx26 in the cells. The effect of dexamethasone on the expression of Cx26 mRNA compared to that of Cx32 mRNA was examined. For the induction and maintenance of Cx26 mRNA, more than 10(-7) M dexamethasone was necessary in this culture. These results suggest that expression of Cx26 in hepatocytes may be regulated by the concentrations of glucagon and glucocorticoid hormones.
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PMID:Induction and regulation of connexin26 by glucagon in primary cultures of adult rat hepatocytes. 759 18

The two forms of pituitary adenylate cyclase-activating polypeptide (PACAP), PACAP27 and PACAP38, are neuropeptide hormones related to the vasoactive intestinal peptide/secretin/glucagon family of peptides. PACAP receptors that are positively coupled to adenylyl cyclase and phospholipase C have been recently identified. We have investigated the expression of PACAP-Rs in undifferentiated and differentiated PC-12 cells. PACAP27 and PACAP38 failed to significantly increase cAMP or [3H]inositol monophosphate levels in undifferentiated PC-12 cells treated with vehicle, insulin-like growth factor I, or epidermal growth factor but greatly elevated levels after differentiation with nerve growth factor (NGF) or basic fibroblast growth factor. PACAP responsiveness increased significantly after 24 hr of NGF treatment, reaching a maximum within 4 days. At this time of differentiation, the effect of PACAP was dose dependent between 1 nM and 0.1 microM, whereas vasoactive intestinal peptide, at the maximal dose of 10 microM, slightly increased cAMP formation and failed to affect [3H]inositol monophosphate content. Radioreceptor assays, performed with 125I-PACAP27, revealed the induction of high affinity type I PACAP receptors in differentiated PC-12 cells. Using reverse transcription-polymerase chain reaction methodology, we showed the absence of type I PACAP receptor mRNAs in undifferentiated PC-12 cells and the expression of PACAP-R-hop mRNA after NGF or basic fibroblast growth factor treatment. The increased PACAP responsiveness induced by these growth factors in PC-12 cells may therefore result from the expression of the PACAP-R-hop isoform, positively coupled to both adenylyl cyclase and phospholipase C.
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PMID:Differentiation induces pituitary adenylate cyclase-activating polypeptide receptor expression in PC-12 cells. 762 75


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