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)

A growth hormone-releasing factor (GRF)-like peptide was isolated from the hypothalamus of common carp, Cyprinus carpio, by acid extraction, gel filtration chromatography, immunoaffinity chromatography using antiserum directed against rat GRF, and multiple steps of HPLC using octadecyl columns. Based on Edman degradation and peptide mapping, this teleost GRF was established to be a 45-residue peptide with the following primary structure: His-Ala-Asp-Gly-Met-Phe-Asn-Lys-Ala-Tyr-Arg-Lys-Ala-Leu-Gly-Gln-Leu-Ser- Ala-Arg - Lys-Tyr-Leu-His-Thr-Leu-Met-Ala-Lys-Arg-Val-Gly-Gly-Gly-Ser-Met-Ile-Glu- Asp-Asp-Asn-Glu-Pro-Leu-Ser. Carp GRF is closely related structurally to peptides of the glucagon-secretin superfamily, and more particularly to mammalian vasoactive intestinal peptide (VIP) precursors and the N-terminal portion of mammalian GRFs. A synthetic replicate of this peptide is highly potent [50% effective dose (ED50) approximately 0.08 nM] in stimulating GH release from cultured goldfish pituitary glands and in elevating serum GH levels 30 min after injection (0.1 micrograms/g) in goldfish.
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PMID:Isolation and characterization of hypothalamic growth-hormone releasing factor from common carp, Cyprinus carpio. 147 12

Plasma immunoreactive glucagon levels (IRG), plasma glucose levels and brain and liver glycogen concentrations were analyzed in carp (adapted to 15 degrees C) subjected to short-term temperature changes (1.6 or 11 h, at 5 degrees C or 28 degrees C, respectively) and to long-term temperature changes (21 months at 28 degrees C). The high temperature (28 degrees C) produced significant increases in IRG in both short and long-term experiments. Brain glycogen also decreased in both experiments whereas liver glycogen only changed in the long-term experiment. Low temperatures did not provoke any changes either in IRG or in liver glycogen, whereas brain glycogen decreased in the 1 h exposure. In short, under these conditions in carp, IRG did not respond to low temperature but could play an important role in high temperature acclimation.
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PMID:The effect of temperature on immunoreactive glucagon plasma level in carp Cyprinus carpio. 319 72

The effects of vasoactive intestinal peptide (VIP) and several other peptides have been examined on cyclic AMP accumulation in intact pieces and isolated horizontal cells of the teleost (carp) retina. VIP was the most effective peptide examined, inducing a dose-related response, and an approximately fivefold increase in cyclic AMP production when used at a concentration of 10 microM. Porcine histidine isoleucine-containing peptide and secretin, peptides structurally related to VIP, also stimulated cyclic AMP accumulation, but at concentrations of 10 microM induced responses which were only approximately 40% and 10%, respectively, of the response observed with 10 microM VIP. In contrast, several other peptides, including glucagon, neurotensin, somatostatin, luteinizing hormone-releasing hormone, alpha-melanocyte-stimulating hormone, cholecystokinin octapeptide26-33, gastrin-releasing peptide, thyrotropin-releasing hormone, and VIP10-28 were totally inactive. The response to 10 microM VIP was not antagonized by several dopamine antagonists, indicating the presence of a population of specific VIP receptors coupled to adenylate cyclase, distinct from the population of dopamine receptors coupled to adenylate cyclase also known to be present in this tissue. Finally, experiments involving the use of fractions of isolated horizontal cells indicate that these neurons possess a population of VIP receptors coupled to cyclic AMP production which would appear to share a common pool of adenylate cyclase with a population of similarly coupled dopamine receptors.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of vasoactive intestinal peptide and other peptides on cyclic AMP accumulation in intact pieces and isolated horizontal cells of the teleost retina. 619 61

Nineteen different antisera raised against mammalian hormones were used to identify the occurrence and distribution of endocrine cells in the gut of grass carp (Ctenopharyngodon idellus). Positive reactions were obtained in gut epithelium with antisera gastrin, glucagon, gastric inhibitory peptide, leucine enkephalin, substance P, and bovine pancreatic polypeptide. No immunoreactive product was formed using antisera against somatostatin, 5-hydroxytryptamine, insulin, avian pancreatic polypeptide, motilin, cholecystokinin, secretin, neurotensin, vasoactive intestinal polypeptide, bombesin, neuron-specific enolase, prochymosin, and pepsinogen. The exact distribution mapping of six kinds of immunoreactive endocrine cells throughout the gut of grass carp (C. idellus) is presented. The morphological characteristics of immunoreactive endocrine cells is described. Their distribution characteristics and possible modes of secretion and function are discussed. Finally, the possible relationship between the transplantation of these cells in the gastro-entero-pancreatic endocrine system is discussed.
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PMID:An immunocytochemical study of endocrine cells in the gut of a stomachless teleost fish, grass carp, Cyprinidae. 816 83

In fed and starved carp, Cyprinus carpio, ketone body metabolism and those metabolic and endocrine factors that are known to induce ketogenesis in starving mammals were investigated. Acetoacetate was detected in plasma and liver of both fed and starved carp. We could not detect 3-hydroxybutyrate, neither by 1H-NMR spectroscopy nor by spectrophotometric assay, in spite of low activities of hepatic 3-hydroxybutyrate dehydrogenase. Starvation of carp did not create metabolic conditions that would favor ketone body synthesis: Mobilization and hepatic catabolism of fatty acids were only moderately enhanced, the rate of gluconeogenesis was not elevated, and glucagon levels as well as the glucagon/insulin-ratio remained stable or declined. Therefore, the discrepancy in the effect of food deprivation on mammalian and teleostean ketogenesis appears to be caused not by the absence of the ketogenic pathway from teleosts but by major differences between mammals and fish in their metabolic response to starvation.
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PMID:Ketone body metabolism in the Carp Cyprinus carpio: biochemical and 1H NMR spectroscopical analysis. 915 88

The fruit-eating teleost fish, the pacu Piaractus mesopotamicus (Characiformes, Characidae) is classified along with the carp and the catfish in the superorder Ostariophysi. The pacu is able to survive and grow in captive conditions feeding exclusively on carbohydrates. Hormonal polypeptides in an extract of pacu Brockmann bodies were purified to homogeneity by reversed phase HPLC and their primary structures determined by automated Edman degradation. Pacu insulin contains only two substitutions, Glu-->Asp at A15 and Thr-->Ser at B24 (corresponding to B22 in mammalian insulins) compared with carp insulin. The B-chains of both insulins contain a dipeptide extension to the N-terminus and a deletion of the C-terminal residue compared with human insulin. Pacu glucagon differs from catfish glucagon by a single substitution at position 17 (Arg-->Gln. The primary structure of the 34 amino acid residue glucagon-like peptide (GLP) differs from catfish GLP only at positions 12 (Ser-->Ala) and 33 (Pro-->Gln). In common with other teleost species, the pacu expresses two somatostatin genes. Somatostatin-14, derived from preprosomatostatin-I (PSS-I), is identical to mammalian/catfish somatostatin-14. Although pacu somatostatin-II was not identified in this study, a peptide was purified that shows 67% sequence identity with residues (1-58) of catfish preprosomatostatin-II (PSS-II). This relatively high degree of sequence similarity contrasts with the fact that catfish PSS-II shows virtually no sequence identity with the corresponding PSS-II from anglerfish (Acanthopterygii) and trout (Protoacanthopterygii). A comparison of the primary structures of the islet hormones suggest that amino acid sequences may have been better conserved within the Ostariophysi than in other groups of the taxon Euteleostei that have been studied.
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PMID:Purification and characterization of insulin and peptides derived from proglucagon and prosomatostatin from the fruit-eating fish, the pacu Piaractus mesopotamicus. 1032 3

AIM:To study the cell types, localization, distribution density and morphology of APUD cells in the intestinal mucosa of stomachless teleost fishes.METHOD:By using the peroxidase antiperoxidase complex (PAP) immunocytochemical staining technique the identification, localization and morphology of immunoreactive (IR) endocrine cells seattered in the intestinal mucosa of grass carp (Cyenopharyngodon idellus), black carp ( Mylopharyngodon piceus ) and common carp (Cyprinus carpio) were investigated with 20 kinds of antisera prepared against mammalian peptide hormones of APUD cells, and likewise by using avidin-biotin-peroxidase complex (ABC) method those of silver carp (Hypophthalmichthys molitrix), bighead (Aristichthys nobilis), silver crucian carp (Carassius gibelio) and bluntnose black bream (Megalobrama amblyocephala ) were also studied with 5 different antisera. The replacement of the first antiserum by phosphate buffered saline (PBS) was employed as a control. IR endocrine cells were counted with a square-mesh ocular micrometer from 10 fields selected randomly in every section of each part of the intestine specimen. The average number of IR endocrine cells per mm(2) was counted to quantify their distribution density.RESULT:Gastrin (GAS), Gastric inhibitory peptide (GIP), glucagon (GLU), glucagons like immunorea-ctants (GLI), bovine pancreatic polypeptide (BPP), leucine-enkephalin (ENK) and substance P (SP)-IR endocrine cells were found in the gut of grass carp, black carp and common carp, and somatostatin (SOM) IR endocrine cells were only seen in common carp. GAS, GIP and GLU-IR endocrine cells were found in the intestinal mucosa of silver carp, bighead, silver crucian carp and bluntnose black bream. Most of IR endocrine cells had the higher distribution density in the foregut and midgut, and were longer in shape. They had a long apical cytoplasmic process extended to the gut lumen and a basal process extended to adjacent cells or basement membrane and touched with it. Sometimes, the basal cytoplasmic process formed an enlarged synapse-like structure in the contiguous part with basement membrane. This phenomenon provided new morpho-logical evidence for neuroendocrine and paracrine secretory function of these enteroendocrine cells.CONCLUTION:At least 8 kinds of IR endocrine cells were found in the gut of stomachless teleost species for the first time in China. These IR endocrine cells scattering in the gut mucosa belong to the APUD system. Among them, the hormones secreted by SP-, ENK-, SOM- and GLU-IR endocrine cells belong to the peptides of dual distribution in the brain and gut. This provided new evidence for the concept of brain-gut peptide. According to the cell types, distribution density, morphological characteristics and variety in shape of APUD cells in the gut of stomachless teleost fishes, it is deemed that the digestive tract of fishes is also an endocrine organ of great importance and complexity.
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PMID:Immunocytochemical identification and localization of APUD cells in the gut of seven stomachless teleost fishes. 1181 32

Pituitary adenylate cyclase-activating polypeptide (PACAP) is a member of the glucagon/secretin peptide family and its molecular structure is highly conserved among vertebrates. In this study, the role of PACAP in regulating growth hormone (GH) secretion in fish was examined in vitro using common carp pituitary cells under column perifusion. A dose-dependent increase in GH release was observed after exposing pituitary cells to increasing doses of ovine PACAP38 (oPACAP38) and PACAP27 (oPACAP27), but not vasoactive intestinal polypeptide (VIP). A lack of GH response to VIP stimulation is consistent with the pharmacological properties of PAC-1 receptors, suggesting that this receptor subtype may be involved in PACAP-induced GH secretion in carp species. Although the maximal GH responses induced by oPACAP38 and oPACAP27 were similar, the minimal effective dose and ED50 value for oPACAP38 were significantly lower than that for oPACAP27. These results may indicate that common carp PAC-1 receptors are more sensitive to stimulation by oPACAP38 than by oPACAP27. In parallel studies, oPACAP38 and oPACAP27 were also effective in increasing cAMP release, cellular cAMP content, total cAMP production, and intracellular Ca(2+) ([Ca(2+)](i)) levels in common carp pituitary cells. Besides, the rise in [Ca(2+)](i) induced by oPACAP38 was blocked by removing extracellular Ca(2+) ([Ca(2+)](e)) or by treatment with nifedipine, an inhibitor of voltage-sensitive Ca(2+) channels (VSCC). The dose dependence of PACAP-stimulated GH release in common carp pituitary cells was mimicked by activating adenylate cyclase using forskolin, inhibiting cAMP degradation using IBMX, increasing functional levels of intracellular cAMP using CPT-cAMP, or inducing [Ca(2+)](e) entry using the Ca(2+) ionophore A23187. In contrast, the GH-releasing effect of oPACAP38 was suppressed by treatment with the adenylate cyclase inhibitor MDL12330A, protein kinase A inhibitor H89, and VSCC blocker nifedipine, or by perifusion with a Ca(2+)-free culture medium. These results, as a whole, suggest that PACAP functions as a GH-releasing factor in common carp by activating pituitary receptors resembling mammalian PAC-1 receptors. Apparently, the GH-releasing action of PACAP is mediated through the adenylate cyclase/cAMP/protein kinase A pathway and [Ca(2+)](e) influx through VSCC.
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PMID:Regulation of growth hormone release in common carp pituitary cells by pituitary adenylate cyclase-activating polypeptide: signal transduction involves cAMP- and calcium-dependent mechanisms. 1245 43

The regional distribution and relative frequency of some endocrine cells in the pancreas of the carp, Cyprinus carpio Linnaeus, belonging to the family Cyprinidae in the order Cypriniformes, were observed using specific mammalian antisera against insulin, glucagon, somatostatin and human pancreatic polypeptide (hPP) by peroxidase antiperoxidase (PAP) method. The pancreas was divided into four regions (principal and secondary islets, exocrine and pancreatic duct regions). In addition, the pancreatic islet regions were further subdivided into three regions (central, mantle and peripheral regions) and the pancreatic duct regions were subdivided into two regions (epithelial and subepithelial regions). Spherical to spindle or occasionally round to oval shaped immunoreactive (IR) cells were demonstrated in the pancreatic islets, exocrine and pancreatic duct. In the principal islet regions, some cells were also detected in the other regions, most of insulin- and somatostatin-IR cells were located in the central regions, and glucagon- and hPP-IR cells were situated in the peripheral regions. In this regions, insulin-IR cells were most predominant cell types and then, glucagon, somatostatin and hPP in that order. In the secondary islet regions, the regional distribution and relative frequency of these four types of endocrine cells were quite similar to those of the principal islets except for cell clusters consisted of hPP-IR cells that were situated in the peripheral to mantle regions. In the pancreatic duct regions, all four major pancreatic endocrine cells were demonstrated in the inter-epithelial cells and/or basal regions of the epithelial linning. In addition, cell clusters composed of numerous insulin-, moderate glucagon- and somatostatin-IR cells of low frequency were also observed in the subepithelial regions of the pancreatic duct. In the exocrine regions, insulin-, glucagon-, somatostatin- and hPP-IR cells were located in the inter-acinus regions with rare, a few, moderate and moderate frequencies, respectively. In conclusion, the regional distribution and relative frequency of four major pancreatic endocrine cells, insulin-, glucagon-, somatostatin- and hPP-IR cells, in the pancreas of the carp showed general patterns which were observed in other stomachless teleost. However, some species- dependent different distributional patterns and/or relative frequencies were also demonstrated.
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PMID:Immunohistochemical study of the endocrine cells in the pancreas of the carp, Cyprinus carpio (Cyprinidae). 1281 80

Pituitary adenylate cyclase-activating polypeptide (PACAP), a member of the glucagon/secretin peptide family, has been recently proposed to be the ancestral GH-releasing factor. Using grass carp as a model for bony fish, we examined the mechanisms for PACAP regulation of GH synthesis and secretion at the pituitary level. Nerve fibers with PACAP immunoreactivity were identified in the grass carp pituitary overlapping with the distribution of somatotrophs. At the somatotroph level, PACAP was shown to induce cAMP synthesis and Ca(2+) entry through voltage-sensitive Ca(2+) channels (VSCC). In carp pituitary cells, PACAP but not vasoactive intestinal polypeptide increased GH release, GH content, total GH production, and steady-state GH mRNA levels. PACAP also enhanced GH mRNA stability, GH promoter activity, and nuclear expression of GH primary transcripts. Increasing cAMP levels, induction of Ca(2+) entry, and activation of VSCC were all effective in elevating GH secretion and GH mRNA levels. PACAP-induced GH secretion and GH mRNA expression, however, were abolished by inhibiting adenylate cyclase and protein kinase A, removing extracellular Ca(2+) or VSCC blockade, or inactivating calmodulin (CaM)-dependent protein kinase II (CaM kinase II). Similar sensitivity to VSCC and CaM kinase II blockade was also observed by activating cAMP production as a trigger for GH release and GH gene expression. These results suggest that PACAP stimulates GH synthesis and secretion in grass carp pituitary cells through PAC(1) receptors. These stimulatory actions probably are mediated by the adenylate cyclase/cAMP/protein kinase A pathway coupled to Ca(2+) entry via VSCC and subsequent activation of CaM/CaM kinase II cascades.
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PMID:Pituitary adenylate cyclase-activating polypeptide (PACAP) as a growth hormone (GH)-releasing factor in grass carp. I. Functional coupling of cyclic adenosine 3',5'-monophosphate and Ca2+/calmodulin-dependent signaling pathways in PACAP-induced GH secretion and GH gene expression in grass carp pituitary cells. 1612 57


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