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 concentrations of immunoreactive (IR) corticotropin-releasing hormone (CRH) in 218 neuroendocrine tumors were determined by CRH radioimmunoassay. The tumors examined were 86 pancreatic endocrine tumors (PET), 22 neuroblastic tumors (NBT), 26 carcinoid tumors (CA), 24 pheochromocytomas (PHEO), 40 small cell lung carcinomas (SCLC) and 20 medullary thyroid carcinomas (MTC). IR-CRH was detectable in 21 neuroendocrine tumors (10 PET, four NBT, three CA, two PHEO and two SCLC) at levels of 10-2,700 ng/g wet weight (9.6%). The 21 patients with these CRH-producing tumors showed no clinical symptoms suggestive of Cushing's syndrome. The levels of plasma IR-CRH extracted by immunoaffinity chromatography were < 7.5 pg/ml in five normal subjects and a patient with a neuroblastic tumor containing 55 ng/g wet weight IR-CRH, but in a patient with a thymic carcinoid tumor containing 1,000 ng/g wet weight IR-CRH, the plasma level was elevated to 180 pg/ml. This patient did not have Cushing's syndrome nor an elevated plasma adrenocorticotropic hormone (ACTH) level. The concentrations of nine peptides (growth hormone-releasing hormone, somatostatin, ACTH, calcitonin, gastrin-releasing peptide, glucagon, vasoactive intestinal peptide, neuropeptide tyrosine and pancreatic polypeptide) were determined in extracts of the 21 IR-CRH-producing tumors. Some of these peptides were frequently found to be produced concomitantly with CRH. The results indicate IR-CRH to be produced by various neuroendocrine tumors, but Cushing's syndrome, due to the CRH, to be very rare. The results also show that CRH-producing tumors produce multiple hormones.
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PMID:Production of immunoreactive corticotropin-releasing hormone in various neuroendocrine tumors. 135 72

The coexistence of immunoreactivities to cholecystokinin, glucagon, glucagon-like peptide 1, salmon pancreatic polypeptide, neuropeptide tyrosine, and peptide tyrosine tyrosine was studied immunocytochemically, revealing for the first time in fish intestine the existence in the same cell of immunoreactivities to cholecystokinin-glucagon/glucagon-like peptide 1, cholecystokinin-salmon pancreatic polypeptide, glucagon/glucagon-like peptide 1-salmon pancreatic polypeptide, glucagon/glucagon-like peptide 1-neuropeptide tyrosine, salmon pancreatic polypeptide tyrosine tyrosine, and glucagon/glucagon-like peptide 1-peptide tyrosine tyrosine. Colocalization of cholecystokinin-salmon pancreatic polypeptide was observed only in the pyloric caeca of the rainbow trout Oncorhynchus mykiss, while the other colocalizations also occurred in proximal and middle intestinal segments. In all cases, endocrine cells immunoreactive to only one of the paired antisera were detected except for anti-glucagon and anti-glucagon-like peptide 1, which always immunostained the same cells.
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PMID:Some peptide-like colocalizations in endocrine cells of the pyloric caeca and the intestine of Oncorhynchus mykiss (Teleostei). 142 2

Neuropeptide Y (NPY) concentrations were measured by radioimmunoassay in eight microdissected hypothalamic regions of obese (fa/fa) and lean (Fa/?) Zucker rats. Freely fed obese rats showed significant (40-100%) increases in NPY concentrations in several regions, notably the paraventricular, ventromedial, and dorsomedial nuclei and the arcuate nucleus/median eminence, compared with lean rats. Hypothalamic NPY concentrations were not affected in either obese or lean rats by food restriction, which caused 25% weight loss over 3 wk. Refeeding to initial weight significantly increased NPY levels in the ventromedial and dorsomedial nuclei in lean rats but did not significantly alter NPY concentrations in any hypothalamic region in obese rats. These observations indicate fundamental differences in the regulation of hypothalamic NPY between obese and lean Zucker rats. NPY injected into the paraventricular nucleus and other regions causes hyperphagia, obesity, and increased secretion of insulin, glucagon, ACTH, and corticosterone. These behavioral and neuroendocrine abnormalities all occur in the obese Zucker syndrome and may be due to increased NPY-ergic activity in the hypothalamus.
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PMID:Altered neuropeptide Y concentrations in specific hypothalamic regions of obese (fa/fa) Zucker rats. Possible relationship to obesity and neuroendocrine disturbances. 165 67

Neuropeptide Y (NPY)-nerves occur in the pancreas. We therefore infused synthetic porcine NPY directly into the pancreatic artery in anaesthetized pigs to study its direct in vivo influence on pancreatic blood flow and on insulin and glucagon secretion. NPY was given both under basal, normoglycemic conditions, and during an ongoing intravenous infusion of glucose, which raised plasma glucose levels to 20 mM. NPY was infused at 0.5 (n = 2), 5 (n = 3), 35 (n = 7), or 175 (n = 5) pmol/min. We found that NPY at 5, 35, and 175 pmol/min inhibited glucagon secretion. Furthermore, at 35 and 175 pmol/min, NPY also reduced pancreatic blood flow. In contrast, only at 175 pmol/min, NPY inhibited basal and glucose-stimulated insulin secretion. We conclude that in the pig NPY might participate in the regulation of glucagon secretion (as an inhibitor) and of pancreatic blood flow (as a vasoconstrictor). In contrast, NPY does not seem to be involved in the regulation of insulin secretion.
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PMID:Effects of neuropeptide Y on insulin and glucagon secretion in the pig. 179 25

Neuropeptide Y (NPY) and calcitonin gene-related peptide (CGRP) are both intrapancreatic neuropeptides that are known to inhibit stimulated insulin secretion. In the present study, we examined their influences on basal and stimulated glucagon and insulin secretion in the mouse. Either NPY or CGRP was injected intravenously at two dose levels (0.85 or 4.25 nmol/kg). When injected alone, neither of them did affect basal plasma glucagon levels but CGRP reduced basal plasma insulin levels. Glucagon secretion stimulated by the cholinergic agonist carbachol was modestly inhibited by NPY at 4.25 nmol/kg (P less than 0.01) but not affected by CGRP. In contrast, glucagon secretion stimulated by the beta 2-adrenoceptor agonist terbutaline was markedly inhibited by NPY already at the lower dose level (P less than 0.01) and potentiated by CGRP (P less than 0.01). Insulin secretion stimulated by carbachol was inhibited by CGRP (P less than 0.01) but not affected by NPY, whereas terbutaline-induced insulin secretion was inhibited by both NPY (P less than 0.05) and CGRP (P less than 0.01). We conclude that the two intrapancreatic neuropeptides NPY and CGRP have opposite actions on stimulated glucagon secretion in the mouse: NPY in an inhibitory and CGRP in a potentiatory direction. Both peptides, however, inhibit insulin secretion stimulated by terbutaline.
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PMID:Neuropeptide Y and calcitonin gene-related peptide: effects on glucagon and insulin secretion in the mouse. 332 90

The immunogold-silver staining technique is shown to be of great value in the detection of regulatory peptide-containing nerves and endocrine cells in routinely fixed, paraffin-wax-embedded tissues. The method appears to be better for this system than peroxidase anti-peroxidase (PAP) which can yield poor or variable results. Antibodies to regulatory peptides, including calcitonin gene-related peptide (CGRP), substance P, neuropeptide tyrosine (NPY), glucagon, pancratic polypeptide, and somatostatin 14 and 28, as well as to neurofilaments, neuron-specific enolase (NSE) and S-100, were used on sections of a variety of tissues from rat and pig including respiratory tract, skin, gut, pancreas, vagina, uterus, fallopian tube and kidney. In all cases, stronger immunostaining of nerves was obtained with the immunogold-silver technique than with PAP. The inherent density of the staining was also found to improve the visibility of endocrine cells in the section, and to permit the use of routine histological stains for counterstaining. As immunogold-silver staining is sensitive, rapid, cheap and avoids hazardous reagents, we feel it has great potential for the immunostaining of nerves and endocrine cells that contain regulatory peptides in routinely fixed and embedded tissues and may prove useful in pathology.
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PMID:The potential of the immunogold-silver staining method for paraffin sections. 608 58

Neuropeptide Y (NPY) is a 36 amino acid peptide known to inhibit glucose-stimulated insulin secretion. NPY has recently been shown to be synthetized within rat islets of Langerhans and to be secreted in a differentiated rat insulin-secreting cell line, and as to this date the localization of NPY in human endocrine pancreas has not been reported. As NPY shares high amino acid sequence homology with peptide YY (PYY) and pancreatic polypeptide (PP), the polyclonal antibodies raised against these peptides often cross-react with each other. To demonstrate the presence of NPY in the human endocrine pancreas, we used a highly specific monoclonal antibody raised against NPY and another against its C-flanking peptide (CPON). We studied three cases of hyperplasia of Langerhans islets and 11 cases of endocrine tumors of the pancreas. NPY and CPON were detected in all three cases of hyperplasia. For the 11 pancreatic tumors, five and nine of the tumors were positive for the antibodies NPY and CPON, respectively. The two negative tumors for CPON immunoreactivity were differentiated insulinomas, which showed no evidence of other hormonal secretion. In normal Langerhans islet, NPY and CPON immunoreactivities were colocalized in glucagon-producing cells (alpha-cells) and in a few insulin-secreting cell (beta-cells).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Immunolocalization of neuropeptide Y in human pancreatic endocrine tumors. 747 36

The endocrine pancreas from 2 genera of lacertid lizards (Pedioplanis and Meroles) was investigated immunocytochemically for the presence of immunoreactivity to mammalian antisera to insulin (I), glucagon (G), pancreatic polypeptide (PP), peptide tyrosine tyrosine (PYY), neuropeptide tyrosine (NPY), somatostatin 14 (SRIF 14) and somatostatin 28 (SRIF 28), pancreastatin (Pst), galanin (Gl), oxytocin (OT). Cells immunoreactive (IR) to all the antisera used, and nerve fibers IR only to anti-galanin were found. Moreover, three types of colocalized immunoreactivities were detected: type 1 (PP/PYY/NPY), type 2 (G/PP/PYY/NPY), and type 3 (G/PYY/NPY/Pst).
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PMID:The endocrine pancreas of lacertids: an immunocytochemical study of the genera Pedioplanis and Meroles. 754 43

The endocrine pancreas of Rana arvalis studied by immunochemistry consisted of islets and diffuse endocrine cells. The islets showed a mammalian-like arrangement with a central core of B cells and a peripheral mantle of A/PP cells. A few D and vasoactive intestinal polypeptide cells were also present. Consecutive sections or double-labeling studies allowed us to detect several regulatory peptides colocalized in the same endocrine cells. The so-called A/PP cells contained subpopulations of cells showing various types of immunoreactivity and varying degrees of immunolabeling. Generally, glucagon/pancreatic polypeptide, glucagon/pancreatic polypeptide/phe-met-arg-phe-amide, glucagon/pancreatic polypeptide/peptide tyrosine tyrosine, glucagon/pancreatic polypeptide/peptide tyrosine tyrosine/phe-met-arg-phe-amide immunoreactivities were present in the islets, while peptide tyrosine tyrosine/neuropeptide tyrosine colocalization was also found in the parenchyma.
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PMID:Cell composition and co-stored peptides in the endocrine pancreas of Rana arvalis. 761 58

Neuropeptide Y (NPY) is known to occur in the autonomic nervous system, including the pancreatic islet innervation. We now present evidence that NPY is also expressed in endocrine islet cells in hamster pancreas. Thus, NPY-immunoreactivity and gene expression were detected in peripheral islet cells, using immunocytochemistry (ICC), in situ hybridization (ISH), and a combination of these techniques. Double immunostaining for NPY and somatostatin enabled localisation of NPY ot the vast majority of the somatostatin cells. However, a few somatostatin cells were devoid of NPY immunoreactivity and an occasional NPY-immunoreactive cell was devoid of somatostatin. ISH with an NPY mRNA specific probe, showed labelling of cells in the islet periphery. Furthermore, combined ISH for NPY mRNA and ICC for somatostatin showed autoradiographic labelling of somatostatin cells to a varying degree. Both somatostatin and NPY are inhibitors of insulin and/or glucagon secretion. Thus, in the islets these two peptides may be coreleased and cooperate in the regulation of islet hormone secretion. The role for NPY emanating from islet cells is probably paracrine rather than endocrine.
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PMID:Neuropeptide Y is expressed in islet somatostatin cells of the hamster pancreas: a combined immunocytochemical and in situ hybridization study. 764 4


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