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)

The effect of glucagon, Vasoactive Intestinal Polypeptide (VIP), secretin and gut glucagon on the cyclic adenosine 3'5' monophosphate (cAMP) level, and on the specific binding of these 125I-peptides to the adipocyte plasma membrane was measured in chicken adipocytes and compared to the results obtained in rat adipocytes. The displacement of 125I-glucagon from its specific sites was observed with about the same concentration of unlabeled hormone in fat cell plasma membranes of both species. However, the rise in cAMP induced by glucagon was much higher in chicken than in rat adipocytes. In chicken fat cells unlike rat fat cells, the cAMP accumulation elicited by glucagon was maintained during at least 60 min even in the absence of theophylline. Theophylline at 1-10 mM potentiated the glucagon-stimulated cAMP levels in rat fat cells, but had only a slight effect, if any, in chicken adiposyces. Porcine VIP, secretin or gut glucagon exerted no detectable action on the cAMP level of chicken adipocytes. The lack of cAMP accumulation was in good agreement with the absence of binding of 125I-VIP and 125I-secretin by chicken plasma membranes. These findings suggest that: 1) the difference of glucagon effect in rat and chicken fat cells results from variations in the rate of degradation of cAMP rather than from differences in the specific binding of glucagon between the two species; 2) the use of chicken fat cells is suitable to discriminate between glucagon and structurally related peptides from mammals.
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PMID:Interactions of glucagon and related peptides with chicken adipose tissue. 18 29

Polypeptide material displaying glucagon-like immunoreactivity was isolated from porcine colon using immunoaffinity chromatography. The immunoreactive material was tightly bound to high molecular weight proteins but was dissociated by 0.1% w/v sodium dodecyl sulphate solution into immunoreactive components of approximate molecular weights 12,000,8000,5000 and 3000. These components reacted at least 50 times more strongly with antibodies specific for the N-terminal region of glucagon than with antibodies specific for the C-terminal region of glucagon. While the 8000 and 3000 dalton fractions were homogeneous, the 12,000 and 5000 dalton fractions were resolved into multiple bands by isoelectric focusing. The 12,000 dalton fraction was devoid of glycogenolytic and lipolytic activity, was not insulin releasing and showed no ability to bind to receptor sites specific for glucagon on hepatic plasma membranes and to active hepatic adenylate cyclase. The 8000 and 5000 dalton components showed weak lipolytic activity. The possible significance of colonic glucagon-like immunoreactivity relative to pancreatic glucagon and immunoreactivity from other tissues is discussed.
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PMID:Physicochemical and biological properties of glucagon-like polypeptides from porcine colon. 45 44

Polypeptide antigen, glucagon, antibodies to glucagon and non-immune globulins were immobilised on agarose using CNBr and a bifunctional oxirane. Irrespective of the ligand immolilised, positively charged groups introduced to conjugates by CNBr caused electrostatic interactions with impurities and soluble biospecific ligands. Solvents required for elution of bound antibodies and antigens were more strongly deforming when immunoaffinity conjugates were prepared with CNBr than with the oxirane. This is attributed to compound affinity resulting from reinforcement of biospecific by non-biospecific interactions. Strongly deforming solvents were still required for oxirane conjugates, however, when antibodies had high affinity for antigen.
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PMID:Comparison of non-biospecific effects in immunoaffinity chromatography using cyanogen bromide and bifunctional oxirane as immobilising agents. 87 26

Polypeptide hormones and growth factors bind to cell surface receptors and are internalized by receptor-mediated endocytosis. Both [125I]insulin and [125I]epidermal growth factor (EGF) are internalized to a much greater extent than [125I]glucagon in freshly isolated rat hepatocytes. All three ligands bind initially and preferentially to the microvillous surface of the hepatocyte, but only [125I]insulin and [125I]EGF undergo significant redistribution to the nonvillous surface of the cell. Thus, the degree of lateral mobility of the ligand receptor complex is strongly correlated with the extent of internalization of the ligand. Since the beta-subunit of the insulin and the EGF receptors span the plasma membrane only once and both receptors are autophosphorylated, it is possible that these are important determinants of the receptor mobility.
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PMID:The relationship of ligand receptor mobility to internalization of polypeptide hormones and growth factors. 184 11

We investigated the ability of two forms of Pituitary Adenylate Cyclase Activating Polypeptide [PACAP-38, the 38 amino acid peptide isolated from ovine hypothalamus, and PACAP-27, a shorter N-terminal (1-27) amidated version] to interact with specific receptors in membranes from the human neuroblastoma cell line NB-OK. [125I]PACAP-27 bound rapidly and specifically to one class of high affinity sites (Kd 0.5 nM). VIP inhibited [125I]PACAP-27 binding 300- to 1000-fold less potently than PACAP-27 and PACAP-38. One microM PHI prevented tracer binding only partially and secretin, glucagon and GRF(1-29)NH2 were ineffective in this respect. PACAP-27 and PACAP-38 stimulated adenylate cyclase activity dose dependently and with similar efficacy (Kact 0.2-0.3 nM), this activation being compatible with the occupancy of specific high affinity PACAP receptor. VIP was markedly less potent and less efficient on this enzyme than PACAP. Chemical cross-linking of [125I]PACAP-27 followed by SDS-PAGE and autoradiography revealed specific cross-linking with a 68 kDa protein.
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PMID:The novel VIP-like hypothalamic polypeptide PACAP interacts with high affinity receptors in the human neuroblastoma cell line NB-OK. 217 43

Four endocrine cell types were identified using peroxidase-antiperoxidase (PAP) technique and ultrastructurally characterized in the pancreas of Mauremys caspica in both winter and summer. In winter, insulin-immunoreactive cells were more abundant and the cell groups larger in the splenic than in the duodenal region, whereas in summer, medium or small cell groups were evenly distributed. Glucagon- and somatostatin-immunoreactive cells were found throughout the gland; they were more numerous in the splenic than in the duodenal region. Polypeptide pancreatic (PP)-immunoreactive cells were found only in the duodenal region. Somatostatin-immunoreactive cells were mainly isolated in winter and grouped in summer. Glucagon- and PP-immunoreactive cells had a similar arrangement in both seasons. Somatostatin- and PP-containing cells showed cytoplasmic processes and could be found next to the pancreatic ducts; the latter were also observed near insulin-immunoreactive cells. Some large secretory granules and numerous, isolated and long rough endoplasmic reticulum (RER) cisternae were seen in winter B cells; in summer B cells numerous lysosomes and few, dilated RER cisternae were found. Summer A cells showed well-developed, dilated RER cisternae and numerous vacuoles; secretory granules were more numerous in winter A cells. In winter B cells and summer A cells some nuclear filamentous inclusions were observed. Few RER cisternae were observed in winter D cells and many in summer D cells; secretory granules were found, the shape and electron density of which differed with the season. PP cells were characterized by their small secretory granules, which were less numerous in winter than in summer, being clustered at the cell pole or dispersed in the cytoplasm, respectively; in winter, the well-developed RER cisternae were dilated and irregularly distributed.
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PMID:Comparative study on the endocrine cells in the pancreas of Mauremys caspica (chelonia) in summer and winter. 267 1

Catecholamines can induce rat hepatic zinc thionein to high levels via alpha 1- and beta 2-adrenoceptors. Polypeptide hormones (glucagon and angiotensin II) are also inducers, but only to the moderate levels attained by glucocorticoids (dexamethasone). Turpentine induced inflammation stimulates the synthesis of ZnMT, but this process is not mediated by catecholamines. Phorbol esters, which are tumor promoters, can stimulate protein kinase C. Angiotensin II and alpha 1-agonists activate protein kinase C via diacylglycerol release from phosphatidylinositol-4,5-diphosphate. Phorbol esters can also stimulate the synthesis of rat hepatic zinc thionein, implicating protein kinase C activation in this induction. The multihormonal modulation of metallothionein gene activation has become increasingly more complex.
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PMID:The involvement of catecholamines and polypeptide hormones in the multihormonal modulation of rat hepatic zinc thionein levels. 282 66

Vasoactive Intestinal Polypeptide (VIP) increased the release of insulin, glucagon and somatostatin from the perfused rat pancreas. The amount of these hormones released was dependent upon the prevailing glucose concentration. VIP stimulated glucagon release in the absence of glucose, while insulin and somatostatin release were increased by VIP only in the presence of glucose concentrations of 4.4 mmol/l and above. Glucagon secretion stimulated by arginine in the presence of 4.4 mmol/l glucose was potentiated by VIP. In contrast, VIP did not induce any further increase in the secretion of insulin and somatostatin over that stimulated by arginine. At higher concentrations of glucose (6.7, 16.7, and 33.3 mmol/l) VIP continued to stimulate insulin and somatostatin release, this effect being synergistic on early-phase insulin release. The effects of VIP on islet cells thus depend on the levels of modulating nutrients.
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PMID:The interaction of vasoactive intestinal polypeptide (VIP), glucose and arginine on the secretion of insulin, glucagon and somatostatin in the perfused rat pancreas. 610 16

The effect of four polypeptides, glucagon, Gastric Inhibitory Polypeptide (GIP), Pancreatic Polypeptide (PP) and somatostatin on beta-adrenoceptor stimulated insulin secretion in vivo in the mouse was investigated. The beta-adrenoceptor stimulation was induced by isoprenaline (IPNA). It was found that at dose levels without influence on basal insulin secretion the polypeptides produced the following pattern of interaction with IPNA. Insulin secretion induced by IPNA was increased by glucagon and inhibited by somatostatin. GIP and PP did not change IPNA-induced insulin release. It is concluded from this and earlier published studies that glucagon, but not always GIP, serves as a positive modulator of basal and stimulated insulin secretion, and that somatostatin is a general inhibitor of insulin release. beta-Adrenoceptor-induced insulin secretion however, seems to be less sensitive to somatostatin than insulin release induced by glucose.
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PMID:Influence of glucagon, gastric inhibitory polypeptide, pancreatic polypeptide and somatostatin on beta-adrenergically induced insulin secretion in the mouse. 612 64

Polypeptides are endogenous agents, involved in the regulation of many physiologic functions and the pathogenesis of several diseases. Polypeptide antagonists form a group of new chemical entities which may provide valid therapeutic agents. Some polypeptides (angiotensin, kinins) are released through the action of proteolytic enzymes (renin, kallikreins) and act as hormones or autacoids; others (substance P, neurotensin) are synthetized by nervous cells to serve as neurotransmitters or neuromodulators. The main homeostatic role of the renin-angiotensin system is to uphold high systemic arterial blood pressure. Overproduction of renin and insufficient checking of renin secretion are among the most common causes of arterial hypertension. Several forms of arterial hypertension (neurovascular, idiopathic) benefit from a reduction in renin-angiotensin system activity. This is achieved either through decreasing renin secretion, by inhibiting conversion of angiotensin I into angiotensin II, or through blocking the peripheral actions (at the receptor sites) of angiotensin II. Renin secretion is very significantly reduced by beta-blocking agents (propranolol); conversion of angiotensin I into angiotensin II is inhibited by teprotide, captopril and their derivatives; peripheral actions of angiotensin II are blocked by saralasin. Bradykinin and related agents produce vasodilation, increase vascular permeability and stimulate pain fibers. Kinins thus reproduce the cardinal features of inflammation and are held to be mediators of the inflammatory reaction. The substance P neuropeptide is found in the brain and bowel; it may act as a transmitter of the sensation of pain at the spinal cord and central nervous system sites. Among other effects outside of the brain, substance P is a potent vasodilator and inhibits renin secretion. Neurotensin is a neuropeptide which produces hypothermia, muscular relaxation and analgesia. Outside of the brain, this peptide is involved in the regulation of gastric secretion, intestinal motility and insulin and glucagon secretion. The vasoactive intestinal peptide, found in certain cholinergic nerve endings, is a large peptide which inhibits gastric secretion, intestinal motility and vascular tone.
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PMID:[Polypeptides and antagonists]. 620 6


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