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)

Insulin (INS)- and somatostatin (SST)-immunoreactive cells were demonstrated by light immunocytochemistry in the endocrine pancreas of sea bass (Dicentrarchus labrax). INS-immunoreactive cells were identified using bovine/porcine, bonito, and salmon (s) INS antisera; the immunostaining was abolished when each antiserum was preabsorbed with its respective peptide but not with unrelated peptides. These cells also reacted with mammal (m) SST-28 (4-14) antiserum. The immunoreaction did not change when this antiserum was preabsorbed by bovine INS. INS-immunoreactive cells were located in the central part of the endocrine areas of the principal, intermediate, and small islets. Two SST-immunoreactive cell types (D1 and D2) were revealed. D1 cells, immunoreactive to SST 14 (562) and sSST-25 antisera, were located next to the glucagon-immunoreactive cells in the peripheral part of the endocrine areas. D2 cells, immunoreactive to SST-14 (562), SST-14 (566), and mSST-28 (4-14) antisera, were found in apposition to the INS-immunoreactive cells. The specificity controls showed that D1 cells expressed sSST-25-like peptides, while D2 cells might contain SST-14 and/or mSST-28-like peptides. The close topographic association between the different SST-immunoreactive cells and both glucagon- and insulin-immunoreactive cells might indicate the existence of a specific paracrine regulation of each endocrine cell type in the sea bass endocrine pancreas.
Gen Comp Endocrinol 1991 Feb
PMID:Pancreatic endocrine cells in sea bass (Dicentrarchus labrax L.) II. Immunocytochemical study of insulin and somatostatin peptides. 167 43

A specific and sensitive radioimmunoassay (RIA) for the measurement of plasma levels of somatostatin-25 (SS-25) in salmon was developed using antisera raised against coho salmon (Oncorhynchus kisutch) SS-25. Somatostatin-25 was iodinated by the chloramine-T method and repurified on Sephadex G-25. The RIA was performed using a double antibody (goat anti-rabbit gammaglobulin as second antibody) method under disequilibrium conditions. Plasma from several salmonids (coho, chinook, rainbow trout, brook trout, arctic char, lake trout, and whitefish) as well as plasma from some nonsalmonids (sucker, bluegill) cross-reacted with the antisera; serial dilutions of plasma from rainbow trout, brook trout, chinook salmon, and coho salmon were parallel to the SS-25 standard curve. Plasma from catfish showed negligible cross-reactivity. None of the mammalian somatostatins (somatostatin-14, somatostatin-28). U II, or other pancreatic hormones (insulin, glucagon) tested showed significant cross-reactivity with the antibody in the assay system. The lowest detectable level of SS-25 was 5 pg/tube; especially reproducible results were obtained in the range of 0.15-1.20 ng/ml, which appears to be the normal range of SS-25 circulating in the plasma of salmonids. Intra- and interassay coefficients of variation were 5.7 and 12.6%, respectively. Injection of glucose into chinook salmon resulted in an elevation of plasma SS-25 titers within 30 min and was coincident with hyperglycemia.
Gen Comp Endocrinol 1991 Mar
PMID:Radioimmunoassay for salmon pancreatic somatostatin-25. 167 8

Immunohistochemistry on tissues of larval lampreys, Petromyzon marinus L., was used to determine the distribution of invariant somatostatin-14 (SST-14) and lamprey somatostatin-34 (SST-34) in the brain while antisera against porcine peptide tyrosine tyrosine (PYY), human neuropeptide Y (NPY), anglerfish peptide YG (aPY), salmon glucagon-like peptide (GLP), SST-14, and SST-34 were used in studies of the pancreas and anterior intestine. In the brain, SST-14 is the major form of somatostatin. SST-14- and SST-34-immunoreactive nerve fibers are distributed throughout the telencephalon, diencephalon, and mesencephalon. In the latter region SST-14 immunoreactivity is concentrated in nerve tracts in the nucleus interpeduncularis. Nerve cells within the olfactory bulbs are immunoreactive only to anti-SST-34. Cells immunostained with anti-SST-14 were localized within the ependymal and subependymal layers of the pars ventralis hypothalami and the subependymal layers of the pars dorsalis thalami. SST-14-immunoreactive perikarya are also distributed within the tegmentum mesencephali. Nerve fibers and cells immunoreactive to anti-SST-34 are detected in the pars ventralis hypothalami but these cells do not colocalize SST-14. Pancreatic islets, distributed within the epithelium and in the submucosal connective tissue at the esophageal-intestinal junction, are only immunoreactive to anti-insulin. The antisera revealed three distinct cell types in the intestinal epithelium: type 1 colocalizes aPY, NPY, and PYY; type 2 colocalizes SST-14 and SST-34; and type 3 demonstrates immunoreactivity only to anti-SST-34. Immunoreactivity to anti-GLP is absent.
Gen Comp Endocrinol 1991 Apr
PMID:Distribution of two forms of somatostatin and peptides belonging to the pancreatic polypeptide family in tissues of larval lampreys, Petromyzon marinus L.: an immunohistochemical study. 167 24

The simultaneous addition of epinephrine and salmon glucagon to catfish (Ictalurus melas) and trout (Salmo gairdneri) hepatocytes did not induce greater increases in glycogen phosphorylase a activity and in glucose release than those caused by epinephrine alone. The effects of epinephrine are greater than those of glucagon. Propranolol added to the hormonal pool blocked the epinephrine effects. In trout cells, epinephrine and glucagon-like peptide (GLP) had similar effects and when they were added simultaneously the stimulation of metabolic indices was higher compared to that obtained with either epinephrine or GLP. However, the effects were not additive. In the presence of epinephrine plus GLP the inhibitory effect of propranolol was not evident, due to the effect induced by GLP, on which propranolol was not effective. This may indicate that epinephrine masks the GLP effect. Results could mean that epinephrine and glucagon-family peptides act in catfish and trout hepatocytes through different receptors on the same pathway leading to glycogen phosphorylase a activation.
Gen Comp Endocrinol 1991 Apr
PMID:Interaction of salmon glucagon, glucagon-like peptide, and epinephrine in the stimulation of phosphorylase a activity in fish isolated hepatocytes. 187 82

Insulin was isolated from the pancreas of the American eel, Anguilla rostrata, and its primary structure was established as (Formula: see text). Eel insulin contains unusual substitutions at B-21, B-22, and B-26 in the putative receptor-binding region of the molecule compared with other mammalian and fish insulins. The A-chain of insulin from the European eel contains an asparagine rather than a serine residue at position A-12. Similarly, amino acid composition data indicate the B-chain of insulin from the European eel is appreciably different from that from the American eel. The primary structure of glucagon-like peptide (GLP) from the American eel is identical to that from the European eel, Anguilla anguilla. The primary structure of the peptide was established as (Formula: see text). Fast-atom bombardment mass spectrometry demonstrated that the COOH-terminal arginyl residue is alpha-amidated. The strong evolutionary pressure to conserve the structure of GLP provides further support for the assertion that the peptide plays an important regulatory role in teleost fish.
Gen Comp Endocrinol 1991 Apr
PMID:The primary structure of glucagon-like peptide but not insulin has been conserved between the American eel, Anguilla rostrata and the European eel, Anguilla anguilla. 187 85

Glucagon has been isolated from the endocrine pancreas of a tunid, Thunnus obesus. The primary structure of the glucagon molecule was established as H S E G T F S N D Y S K Y L E T R R A Q D F V Q W L K N S. The sequence is identical to those of sculpin and flounder glucagon and glucagon II from anglerfish. It also shows high homology to the mammalian hormone (76%). The mass determined by fast-atom bombardment (3508) was consistent with the proposed structure. Immunological properties of the tuna glucagon were analyzed by radioimmunoassay, showing a high degree of cross-reactivity with the 30K antibody.
Gen Comp Endocrinol 1991 Aug
PMID:Isolation and primary structure of glucagon from the endocrine pancreas of Thunnus obesus. 191 9

Norepinephrine (NOR) is a potent activator of carbohydrate metabolism in isolated hepatocytes from copper rockfish (Sebastes caurinus), increasing rates of glycogenolysis fourfold with an EC50 of 6.3 nM. Nanomolar concentrations of NOR also enhance gluconeogenesis. Epinephrine (EPI) activates both pathways to a smaller extent; the corresponding EC50 for glycogenolysis is 320 nM. There is no significant difference between the magnitude of glucose production in response to comparable doses of NOR, bovine glucagon, and catfish glucagon-like peptide. Experiments with an adrenergic agonist (isoproterenol) and antagonists (propranolol, prazosin, atenolol) indicate that NOR effects are mediated through beta-adrenoceptors. Catecholamine-activated glycogenolysis measured at 100 nM EPI or NOR is poorly correlated with a 30-50% rise in intracellular cAMP. Glucose production following catecholamine administration is not linear: 50% of the hourly glucose output is released within the first 17 min (NOR) and 5 min (EPI), respectively. During hepatocyte incubation (60 min at 15 degrees), added NOR and EPI (100 nM) were not degraded to any significant extent. In the absence of added hormones, rockfish hepatocytes produce 7.41 +/- 0.89 mumol glucose x g-1 packed cells x hr-1 at 15 degrees, with gluconeogenesis accounting for 35.0% of the total production. The rate of glucose output, which is linear for at least 60 min, is not correlated with the initial hepatocyte glycogen level.
Gen Comp Endocrinol 1990 Apr
PMID:Norepinephrine: a potent activator of glycogenolysis and gluconeogenesis in rockfish hepatocytes. 197 May 44

PP-, PYY-, and glucagon-immunoreactive cells were immunocytochemically identified in the pancreatic islets of Dicentrarchus labrax (sea bass). PYY cells also reacted with anti-PP serum. The specificity control showed that preabsorption of PP antiserum by PYY peptide abolished the immunostaining, while the reaction did not change when the PYY antiserum was preabsorbed by PP. These results suggested the existence of a PP/PYY molecule in the sea bass islets. The islet distribution of PP/PYY-immunoreactive cells differed markedly. Thus, in the principal islet and some intermediate islets few PP/PYY-immunoreactive cells are present (type I islets), whereas in the smaller and some intermediate ones they are numerous (type II islets). Adjacent sections stained by peroxidase-antiperoxidase (PAP) technique and individual sections stained by immunofluorescence double staining showed the coexistence of glucagon and PP/PYY-like immunoreactivities. Both islet types contained cells with PP/PYY coexisting with glucagon peptide, while cells showing solely glucagon immunoreactivity were found in type I islets only.
Gen Comp Endocrinol 1991 Feb
PMID:Pancreatic endocrine cells in sea bass (Dicentrarchus labrax L.) I. Immunocytochemical characterization of glucagon- and PP-related peptides. 201 94

Immunoreactivity of antisera directed against human neuropeptide Y (NPY), anglerfish polypeptide YG (aPY), bovine pancreatic polypeptide (bPP), salmon pancreatic polypeptide (sPP), porcine peptide tyrosine tyrosine (PYY), and salmon glucagon-like peptide (GLP) was investigated in the endocrine pancreas and anterior intestine of adult lampreys, Petromyzon marinus, by immunohistochemical analysis. There was no immunoreactivity to anti-sPP and anti-bPP in any tissue and anti-GLP immunostaining was only present in the anterior intestine. The immunoreactivity to antisera raised against NPY, aPY, and PYY was colocalized within the same small number of cells in the caudal and cranial pancreas of juveniles and the caudal pancreas of upstream migrant adults. These antibodies did not immunostain B- or D-cells and thus, NPY, aPY, and PYY were likely localized in a third cell type (3a) in the lamprey pancreas. Immunostaining of a few cells with only anti-aPY suggested the possibility of a fourth cell type (3b). Immunoreactivity was similar in the cranial and caudal pancreas of male upstream migrants; however, in the female cranial pancreas, a few cells demonstrated intense immunoreaction to anti-aPY, while weaker immunostaining with this antiserum was observed in B-cells. In the intestine of juvenile and upstream migrant lampreys, positive immunostaining to GLP, NPY, aPY, and PYY antibodies was colocalized within the same cell. We believe that this cell may contain PYY/glucagon family peptides. Other intestinal cells immunostained with either GLP or somatostatin-34 antiserum.
Gen Comp Endocrinol 1991 Jan
PMID:Immunoreactivity to peptides belonging to the pancreatic polypeptide family (NPY, aPY, PP, PYY) and to glucagon-like peptide in the endocrine pancreas and anterior intestine of adult lampreys, Petromyzon marinus: an immunohistochemical study. 202 16

Juvenile coho salmon (Oncorhynchus kisutch) were placed on five dietary regimes: fed 1 week, fasted 1 week, fed 3 weeks, fasted 3 weeks, and fasted 1 week/refed 2 weeks. Plasma levels of glucose, fatty acids, insulin, glucagon, and glucagon-like peptide (GLP) and the activities of key metabolic enzymes were determined. Plasma glucose levels in the fed control groups were 98.4 +/- 3.4 (SEM) and 104.8 +/- 4.7 mg/dl at 1 and 3 weeks, respectively. Plasma glucose in the fasted 1 week group was significantly elevated to 128.8 +/- 9.2 mg/dl. Animals fasted 3 weeks or fasted 1 week/refed 2 weeks displayed plasma glucose levels similar to those of fed animals. Fasted groups possessed significantly less liver glycogen than fed or fasted/refed groups. Plasma fatty acids were elevated only after 3 weeks of fasting (from 0.39 +/- 0.04 microEq/ml to 0.61 +/- 0.06 microEq/ml). This response was reflected in elevated liver lipase activity (from 6.02 +/- 0.44 nmol fatty acid released/hr/mg protein to 14.22 +/- 0.90 units). No significant alterations in liver lipogenesis, assessed by glucose-6-phosphate dehydrogenase activity and by 3H2O incorporation into fatty acids, were observed. Gluconeogenic flux, determined indirectly through kinetic parameters of pyruvate kinase, was enhanced in animals fasted 3 weeks and in animals recovering from a 1-week fast. Plasma insulin levels were highest in fed groups (7.7 +/- 2.3 and 5.9 +/- 1.4 ng/ml at 1 week and 3 weeks, respectively) and were significantly depressed in fasted groups. Plasma levels of glucagon and GLP were also depressed in fasted groups. These results indicate that plasma glucose levels are maintained in salmon during fasting and that fasting-induced hyperlipidemia is mediated by lipolytic enzyme activity. Insulin, glucagon, and GLP may interact with these enzyme systems to coordinate nutritional metabolism of fish.
Gen Comp Endocrinol 1991 Mar
PMID:Effects of nutritional state on in vivo lipid and carbohydrate metabolism of coho salmon, Oncorhynchus kisutch. 205 44


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