Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To validate the adequacy of saliva as a biological specimen for the study of glucocorticoid adrenal function, the concentrations of salivary cortisol (SC) and serum total cortisol (TC) were measured by radioimmunoassay (RIA) in several groups of individuals in baseline state and during stimulation tests. The study of diurnal variations of SC in the reference population (n = 29) showed a nyctohemeral rhythm similar to that of TC, with maximal concentrations at 08.00-09.00 h (18 +/- 9 nmol/L) and 61% and 80% decreases at 15.30 and 23.00 h, respectively. After the administration of 1 mg of dexamethasone, SC was reduced in a 95% of its baseline value (n = 18). In all patients with Cushing's syndrome (n = 8) SC was increased whereas TC was normal in 3. All patients with adrenal failure (n = 11) had subnormal SC levels, while TC was normal in 4. The SC response to stimulation with intravenous synthetic adrenocorticotropin (Nuvacthen) (with and without previous suppression with 1 mg dexamethasone), insulin hypoglycemia and glucagon were qualitatively similar to those of TC, although more marked in proportion. These results, together with the practical advantages of saliva as a biological sample (easy obtention of specimen, absence of stress during its collection, and stability of cortisol in it), indicate that SC represents a more reliable measurement than TC as a useful clinical test to detect glucocorticoid dysfunction.
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PMID:[Usefulness of the determination of saliva cortisol in the study of adrenal gland glucocorticoid function]. 260 98

We investigated the effects of sevoflurane anesthesia and of surgery, on the endocrine functions as reflected by plasma levels of cortisol, aldosterone, ACTH, beta-endorphin-like immunoreactivity, prolactin, insulin, growth hormone, glucagon and glucose in surgical patients.
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PMID:Endocrine evaluation of sevoflurane, a new inhalation anesthetic agent. 262 72

A 7-year-old spayed female Cocker Spaniel was hospitalized with a history of chronic vomiting, anorexia, and weight loss. Laboratory abnormalities included leukocytosis, metabolic alkalosis, hypoglycemia, hypoproteinemia, and hyperinsulinemia. Gastroscopy and ultrasonography revealed multiple gastric masses and a possible pancreatic mass, respectively. Examination of tissues obtained at necropsy showed a pancreatic adenocarcinoma with hepatic metastasis, gastric hypertrophy, and multiple duodenal ulcers. Immunocytochemical staining of the neoplasia was positive for pancreatic polypeptide (PP) and insulin and negative for gastrin, calcitonin, adrenocorticotropic hormone (ACTH), serotonin, L-enkephalin, chromagranin, glucagon, and somatostatin. Subsequent serum gastrin and PP assays showed a fasting hypergastrinemia with a normal response of gastrin to provocative testing and extremely increased PP values. The high PP values may have resulted in the vomiting and gastrointestinal ulceration. A PP-secreting tumor has not previously been reported in the dog.
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PMID:Pancreatic polypeptide and insulin-secreting tumor in a dog with duodenal ulcers and hypertrophic gastritis. 267 25

An enkephalin-binding protein was found in human plasma and serum. The protein was partially purified by DEAE-cellulose column chromatography. The binding of [3H]leucine-enkephalin to this protein was competitively inhibited by unlabeled leucine- and methionine-enkephalin and various peptide hormones such as beta-endorphin and glucagon, but not by Leu-enkephalin-amide. The fact that amide derivatives of leucine-enkephalin and methionine-enkephalin did not inhibit the binding suggests that c-terminuses of enkephalins might have an important part in binding the protein. From these results, physiological roles of the enkephalin-binding protein are discussed.
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PMID:Enkephalin-binding protein in human blood. 281 10

Intracisternal administration of synthetic human beta-endorphin to conscious, ambulatory adult male rats caused dose-related increases in plasma glucose concentration. The largest dose of beta-endorphin examined, 7.25 nmol, increased plasma glucose concentration within 7 min and this effect lasted 2.5 h. On the other hand, only 58 pmol was required to induce transient hyperglycemia, when compared to the response observed in saline-injected control rats. This hyperglycemic effect of beta-endorphin was prevented by prior systemic administration of naloxone, thus supporting the hypothesis that this beta-endorphin-induced effect is mediated at opioid receptors. beta-Endorphin also markedly increased plasma concentrations of epinephrine, norepinephrine and, to a lesser extent, dopamine. A significant positive correlation was demonstrated between plasma glucose and plasma epinephrine responses to increasing doses of intracisternally administered beta-endorphin. In addition, intracisternal beta-endorphin also increased plasma glucagon concentration without significantly increasing plasma insulin concentration. Thus, it is probable that epinephrine and glucagon are the major factors mediating this hyperglycemic effect. beta-Endorphin-induced hyperglycemia was prevented by ganglionic blockade with chlorisondamine. This further supports the thesis that intracerebral beta-endorphin increases plasma glucose concentration by activation of the central autonomic outflow. In addition to these effects on short-term regulators of glycemia, intracisternal beta-endorphin increased plasma concentrations of corticosterone and growth hormone. Both of these glucose counterregulatory hormones may play minor roles in modulating beta-endorphin-induced hyperglycemia.
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PMID:Autonomic and endocrine participation in opioid peptide-induced hyperglycemia. 282 68

Concentrations of insulin, glucagon, growth hormone, adrenocorticotropin, and cortisol were determined in plasma samples obtained at 20-min intervals for 6 h from low and high producing dairy cows at d 30 and 90 postpartum. Four nonpregnant, nonlactating cows also were sampled. Insulin concentrations were reduced at d 30 in both groups of lactating cows compared with concentrations in nonlactating cows; glucagon concentrations were unchanged. The molar insulin: glucagon was reduced at d 30 in both groups and at d 90 for low, but not high producers. Growth hormone concentrations were higher at d 30 in high producers than at d 90, in low producers at d 30, and higher than in nonlactating cows. Cortisol concentrations were lower in high producing cows at d 30 than at d 90 or in nonlactating cows due to a reduced pulse amplitude. No differences were observed for adrenocorticotropin. Reduced molar insulin: glucagon may be an integral response of the cow to lactation, while the difference in the insulin: glucagon for high and low producers at d 90 postpartum may indicate a continued need for a gluconeogenic stimulus in low producers. The elevated growth hormone and low cortisol concentrations likely participate in the enhanced production observed in high producing dairy cows.
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PMID:Plasma concentrations of metabolic hormones in high and low producing dairy cows. 283 86

Acute insulin-induced hypoglycaemia in humans provokes autonomic neural activation and counterregulatory hormonal secretion mediated in part via hypothalamic stimulation. Many patients with Type 1 (insulin-dependent) diabetes have acquired deficiencies of counterregulatory hormonal release following hypoglycaemia. To study the integrity of the hypothalamic-pituitary and the sympatho-adrenal systems, the responses of pituitary hormones, beta-endorphin, glucagon and adrenaline to acute insulin-induced hypoglycaemia (0.2 units/kg) were examined in 16 patients with Type 1 diabetes who did not have autonomic neuropathy. To examine the effect of duration of diabetes these patients were subdivided into two groups (Group 1: 8 patients less than 5 years duration; Group 2: 8 patients greater than 15 years duration) and were compared with 8 normal volunteers (Group 3). The severity and time of onset of hypoglycaemia were similar in all 3 groups, but mean blood glucose recovery was slower in the diabetic groups (p less than 0.01). The mean responses of glucagon, adrenaline, adrenocorticotrophic hormone, prolactin and beta-endorphin were similar in all 3 groups, but the mean responses of growth hormone were lower in both diabetic groups than in the normal group (p less than 0.05). The mean increments of glucagon and adrenaline in the diabetic groups were lower than the normal group, but these differences did not achieve significance; glucagon secretion was preserved in several diabetic patients irrespective of duration of disease. Various hormonal responses to hypoglycaemia were absent or diminished in individual diabetic patients, and multiple hormonal deficiencies could be implicated in delaying blood glucose recovery.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Counterregulatory hormonal responses to hypoglycaemia in type 1 (insulin-dependent) diabetes: evidence for diminished hypothalamic-pituitary hormonal secretion. 285 69

Five antisera against insulin (Ins), glucagon (Glu), somatostatin (SRIF), met-enkephalin (met-enk), and serotonin (5-HT) were used for immunofluorescence detection of endocrine cells in pancreas and gastrointestinal tract (GIT) of the European eel (Anguilla anguilla L.) at three stages of development (leptocephalic larva, glass-eel, and adult eel). Comparable distribution of endocrine cells was observed for adults and glass-eels. In their pancreatic islets, positive immunoreactions were obtained only for Ins, SRIF, and Glu; this later was also present in the pancreatic ducts. 5-HT cells were present throughout the GIT. SRIF cells were situated mostly in the stomach and less in the intestine. Met-enk cells were abundant in the pyloric cecum, but less frequent in the intestinal mucosa. Glu cells were present only in the intestine. No insulin-immunoreactive cells could be detected in the GIT. The pancreatic islets of leptocephalic larvae exhibited a strong reaction for SRIF, a weak reaction for Glu, and none at all for Ins, met-Enk, or 5-HT. The GIT of these larvae contained numerous met-enk cells, mainly in the foregut. In the fore- and midgut, cells exhibited a weak fluorescence after treatment with Glu antiserum. No positive immunoreactive cells were observed with 5-HT, SRIF, or Ins antisera.
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PMID:Detection of endocrine cells by immunofluorescence method in the gastroenteropancreatic system of the adult eel, glass-eel, and leptocephalic larva (Anguilla anguilla L.). 286 Nov 42

Specific somatostatin (SRIH) receptors on human pituitary adenoma cell membranes were characterized using [125I]Tyr11-SRIH as the radioligand. Specific binding of [125I] Tyr11-SRIH to adenoma cell membranes reached a steady state within 30 min at 25 C, and semilogarithmic analysis of the data revealed that the rate of the binding was linear at 25 C with a t1/2 of 13.2 min. Specific binding increased linearly with 5-160 micrograms plasma membrane protein. SRIH-14 and SRIH-28 inhibited [125I]Tyr11-SRIH binding to adenoma cell membranes with ID50S of 0.32 and 0.50 nM, respectively, while secretin, glucagon, gastrin, cholecystokinin-8, bombesin, TRH, LHRH, human GH-releasing factor-(1-44)-NH2, D-Ala2-met-enkephalin, gamma-aminobutyric acid and taurine did not significantly inhibit binding. All of 13 GH-secreting adenomas investigated had specific and high affinity SRIH receptors, with a dissociation constant (Kd) of 0.80 +/- 0.15 nM (mean +/- SEM) and a maximal binding capacity (Bmax) of 234.2 +/- 86.9 fmol/mg protein (mean +/- SEM). Among five of the nonsecreting pituitary adenomas examined, two had SRIH receptors with Kd values of 0.18 and 0.32 nM and Bmax values of 17.2 and 48.0 fmol/mg protein, respectively. In the remaining three, SRIH receptors were not detected. These results indicate that GH-secreting adenomas as well as some nonfunctioning adenomas have specific SRIH receptors, and hence, the function of the adenomas could be altered by SRIH.
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PMID:Specific somatostatin receptors on human pituitary adenoma cell membranes. 286 81

We surveyed retinas of Raja erinacea, Mustelus canis, and Squalus acanthias for neurotransmitter substances by using antisera directed against the substances themselves or against their synthesizing enzymes. Both the peroxidase-antiperoxidase (PAP) and indirect fluorescent techniques were employed to visualize the primary antisera. In all three species positive results were obtained with antisera directed against tyrosine hydroxylase (TOH), glutamic acid decarboxylase (GAD), serotonin (5-HT), and leucine enkephalin (Lenk). Antisera directed against glucagon, neurotensin, beta-endorphin, vasoactive intestinal peptide, or bombesin failed to show any specific staining. Immunoreactivity was located in amacrine, interplexiform, and horizontal cells as well as in axons of the optic fiber layer. The four antisera labelled different amacrine cell classes, distinguished on the bases of perikaryal morphology and the distribution of cell processes in the inner plexiform layer (IPL). Amacrine cells that labelled with the same marker were seen to have different morphologies in the species studied. Thus, TOH-like immunoreactivity was distributed in layers 1, 3, and 5 of the IPL in Mustelus but only in layers 1 and 3 in Raja retina. GAD-like immunoreactivity was found diffusely over all layers of the IPL in Raja, but in Mustelus it was confined primarily to layers 1, 3, and 5 of the IPL. Lenk- and 5-HT-like immunoreactivities showed similar species variations. Two neurochemical classes of interplexiform cell were identified in this study. In Mustelus GAD-like and Lenk-like immunoreactive interplexiform cells were seen whereas in Raja only GAD-positive interplexiform cells were detected. In squalus no unequivocal demonstration of any interplexiform cell was made with these antisera. The GAD antiserum also labelled a subset of the horizontal cells in the dorsal retina of Raja. TOH and 5-HT-antisera labelled axons in the optic fiber layer of all three species but reactive ganglion cell perikarya were not identified.
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PMID:Retinal neurochemistry of three elasmobranch species: an immunohistochemical approach. 286 65


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