Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P61278 (somatostatin)
 22,083 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A prospective study was carried out to evaluate the efficacy of somatostatin in the treatment of acute pancreatitis. Seventy one patients were randomised to control (h = 36), or to the somatostatin group (h = 35) who received somatostatin 100 micrograms/h after a 250 microgram bolus for the first two days. The following were compared in the two groups on admission and two days later: laboratory tests of prognostic significance, severity of pancreatitis, and also morbidity and mortality. Of the nine laboratory tests compared, the white blood cell count, lactate dehydrogenase, and urea concentrations were significantly lower in the somatostatin group two days after admission. Severity of pancreatitis after hospitalisation increased in fewer patients given somatostatin (NS). There was a trend toward fewer complications, especially local, in the somatostatin group. Mortality in both groups was low. Somatostatin appeared to reduce the local complications of acute pancreatitis. A larger trial is necessary to show its beneficial effect conclusively.
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PMID:Somatostatin in the treatment of acute pancreatitis: a prospective randomised controlled trial. 256 34

N intake in the form of protein has neither got an upper nor a lower limit for agricultural working animals within a diet and there is no control mechanism for it. A high surplus of certain amino acids results in a reduction of feed intake. N excretion in faeces depends on 1) the excretion of N containing indigestible feedstuffs, 2) bacterial nitrogen synthesis in the large intestine and 3) the excretion of true endogenous N containing substances (digestion enzymes, intestinal epithelium, N containing endogenous secretion). There are no other control mechanisms for N excretion in faeces. N excretion in urine mainly comprises the nitrogen from the degeneration of amino acids and nucleic acids. The interrelations between urea, NH3, allantoin, creatine and creatinine, uric acid and hippuric acid depend on the species (monogastric or ruminants), on the nitrogen and N amount consumed and on the recycling ratio of the amino acids. The absolute amount of N excretion is not subject to any control mechanism, it depends on the intake of protein and NPN substances, the interim stages, however, which lead to the formation of excretory products, are intermediately controlled. The most important interim stage is protein biosynthesis, which is a fixed, intermediately controlled value in maintenance level. Under growth conditions only, the protein synthesis quota can exceed the protein degradation quota of the total organism (positive N balance). The control mechanisms of protein biosynthesis have, according to current knowledge, the following structure: Stimulation: 1) growth hormone (STH) stimulates protein synthesis by means of somatomedins; 2) hormones of the thyroid gland (T4 and T3) are controlled by the hormone stimulating the thyroid gland (TSH); 3) insulin. Inhibition: 1) somatostatin inhibits STH, TSH and insulin; 2) cortisol directly inhibits protein synthesis and stimulates protein degradation. The control mechanisms of protein turnover in addition to genetic coding and proteolysis extend in the framework of evolution over the period of 3,400 million years from the existence of the bacterial cell to the development of mammals, which is 74% of the age of the earth and approximately 90% since the existence of the first traces of life. The control mechanisms of protein turnover in mammals do not permit gene manipulation in protein synthesis as in bacterial cells since the control mechanisms mentioned are missing there.
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PMID:[Nitrogen metabolism and its control mechanisms]. 266 79

The main purpose of the present study was to characterize the tissue and releasable molecular forms of somatostatin-28[1-12]-like immunoreactivity (S-28[1-12]LI) in rat median eminence (ME) fragments and to compare them with somatostatin-14-like immunoreactivity (S-14 LI) forms. Acetic acid extracts of ME were fractionated on Sephadex G-50 columns (in 6 M urea). The column eluate was monitored for S-28[1-12] LI by RIA with antibody R21 which detects S-28[1-12], S-28, and higher molecular weight forms of S-28[1-12] LI, but not S-14. The S-14 LI RIA utilized recognizes S-14, S-28, and prosomatostatin (pro-S). Rat ME contained 221 +/- 25 pmol S-14 LI/mg protein and 407 +/- 51 pmol S-28[1-12] LI/mg protein. By gel filtration S-14 LI was resolved into three peaks corresponding to S-14, S-28, and a higher mol wt form (14,000) corresponding to pro-S. S-28[1-12] LI consisted of at least five forms corresponding to pro-S, S-28, S-28[1-12], a form which represented pro-S without the S-14 sequence, and a form slightly smaller than S-28[1-12]. Pools of 20 ME incubated in 56 mM K+ solution showed 4.6-fold Ca++-dependent release of S-14 LI and 4-fold release of S-28[1-12] LI. Gel chromatographic analysis of the released material showed all three tissue S-14 LI forms and each of the tissue S-28[1-12] LI forms. HPLC analysis and RIAs further confirmed the release of S-14, S-28, S-28[1-12], and the S-28[1-12] LI form smaller than S-28[1-12]. These data suggest the presence of at least six molecular forms of somatostatin in ME. The release of this large number of peptides, presumably from mature secretory granules in ME in response to depolarization, suggests that they are products of the normal posttranslational processing of pro-S.
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PMID:Characterization of tissue and releasable molecular forms of somatostatin-28[1-12]-like immunoreactivity in rat median eminence. 285 91

We have used the primed-constant infusion of stable isotopes of glucose ([6,6-d2]glucose), alanine([3-13C] alanine), and urea ([15N2]urea) to investigate their kinetic interrelationships in normal volunteers in the postabsorptive state and during the infusion of unlabeled glucose at two rates. Each glucose infusion was tested with and without the simultaneous infusion of somatostatin (S), insulin (I), and glucagon (G) to clamp those hormonal levels. When glucose was infused at 1 mg X kg-1 X min-1, endogenous glucose production was suppressed almost exactly 1 mg X kg-1 X min-1, regardless of whether S plus I plus G were infused. The 4 mg X kg-1 X min-1 glucose infusion suppressed endogenous glucose production, both with and without hormonal control. The plasma concentration of glucose also increased to the same extent during the 4 mg X kg-1 X min-1 infusion in both protocols, which indicated that the spontaneous insulin response to the glucose infusion (an increase from 11 +/- 2 to 24 +/- 3 microU/ml) did not stimulate the peripheral clearance of glucose. The high rate of glucose infusion, both with or without hormonal control, stimulated alanine flux and inhibited urea production. These results indicate that glucose, per se, is an important direct controller of normal metabolic interactions of endogenous alanine, glucose, and urea kinetics.
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PMID:Response to glucose infusion in humans: role of changes in insulin concentration. 286 94

Peripheral plasma somatostatin-like immunoreactivity (SLI) was estimated in non-extracted plasma using a specific somatostatin-14 (SS-14) antiserum. The basal plasma SLI level in healthy subjects (n = 18) was 43 +/- 2.9 pg/ml (mean +/- SE) and rose significantly to 8.3 +/- 2.7, 7.3 +/- 1.1 and 5.8 +/- 2.1 pg/ml above the mean basal level 20, 30, and 40 min after a mixed meal, respectively (P less than 0.05). Basal plasma SLI levels in diet (n = 8), sulfonyl urea (n = 8), and insulin groups (n = 8) of non-insulin-dependent maturity onset diabetics (NIDDM) were 50 +/- 1.6, 59 +/- 4.5, and 74 +/- 5.8 pg/ml, respectively. The basal levels for patients with NIDDM were significantly higher than those for healthy subjects (P less than 0.05). No significant increases in plasma SLI were observed after a mixed meal in any group of NIDDM subjects. Elevated plasma SLI levels are considered to be closely related to the severity of the diabetes. The ratios of SS-14 and SS-28 to the total amount of basal plasma SLI were analyzed using high pressure liquid chromatography (HPLC). The ratio of SS-14 to the total SLI was 71-80% in healthy subjects. The ratio of SS-28 to the total SLI increased from 26-30% in the diet group to 50-55% in the group on insulin. These findings suggest a possible pathophysiological role for gastrointestinal somatostatin in NIDDM.
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PMID:Plasma somatostatin-like immunoreactivity responses to a mixed meal and the heterogeneity in healthy and non-insulin-dependent (NIDDM) diabetics. 287 28

The relationship between insulin concentration (32-980 mU/l) and the capacity of urea-N synthesis (CUNS) was investigated with alanine as nitrogen source in 26 nephrectomized rats. The blood glucose concentration was kept constant by the 'glucose clamp' technique, and the endocrine pancreatic response was controlled by somatostatin. The CUNS was determined as the accumulation of urea corrected for intestinal hydrolysis at a constant amino acid concentration within the interval 7.3-11.6 mmol/l. At insulin concentration above 200 mU/l CUNS was decreased from 10 to 6 mumol (min X 100 g body wt)-1. At lower insulin concentrations the decrease was proportional. Hyperglycaemia 14.8 mmol/l decreased CUNS to 6.3 mumol (min X 100 g body wt)-1. The basal rate of urea-N synthesis was reduced from 3.8 to 1.9 mumol (min X 100 g body wt)-1 by insulin concentrations above 200 mU/l. The estimated alanine elimination (5.8 mumol(min X 100 g body wt)-1) was unchanged by insulin and reduced to 3.3 mumol(min X 100 g body wt)-1) by hyperglycaemia. Somatostatin infusion had no effect on CUNS or alanine elimination. It is suggested that the capacity of urea-N synthesis is subject to short term regulation independently by insulin and glucose.
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PMID:Insulin and glucose decreases the capacity of urea-N synthesis in the rat. 287 87

Holstein calves were used to investigate the effects of immunization procedures against somatostatin (SRIF) on growth and concentrations of somatotropin in plasma. In Trial 1, eight heifers 37 weeks of age were inoculated with cyclic-SRIF conjugated to human alpha-globulin. Final body weight, average daily gain, and measurements of body size were not significantly different between control and SRIF-immunized calves. Apparent total tract nutrient digestibilities and efficiency of feed utilization also were not significantly different between treatments. Plasma concentrations of somatotropin were increased and plasma concentrations of urea nitrogen were decreased in calves immunized against SRIF compared to controls, but these mean differences were not significant. In Trial 2, eleven bull calves seven weeks of age were inoculated with cyclic-SRIF conjugated to keyhole limpet hemocyanin. Calves immunized against SRIF had larger average daily gains (P less than .06) than did control calves. Body size, efficiency of feed utilization, and concentrations of somatotropin in plasma were not significantly different for SRIF immunized calves and control calves. Urea nitrogen in plasma was lower (P less than .04) for calves immunized against somatostatin than for control calves. Data indicate that Holstein calves can produce auto-antibodies against SRIF; however, additional research will be required before such immunization techniques can be effectively used to improve weight gains in cattle.
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PMID:The effect of immunization against somatostatin on growth and concentration of somatotropin in plasma of Holstein calves. 290 84

Using a radioimmunoassay with labeled synthetic tetradecapeptide somatostatin, a large amount of immunoreactive somatostatin was found in the principal pancreatic islet of the channel catfish (Ictalurus punctata). The purpose of these experiments was to isolate and characterize the somatostatin-like material. Extracts of islets were chromatographed on a Bio-Gel P-30 column, and over 90% of the immunoreactive somatostatin migrated with proteins at least twice the size of synthetic tetradecapeptide somatostatin. This fraction was further purified by ion-exchange chromatography on carboxymethyl-cellulose and DEAE-cellulose columns. Two peptides were obtained with identical immunoreactivity, which was approximately 25% that of the synthetic somatostatin. Each peptide was judged to be >95% pure by thin-layer electrophoresis, polyacrylamide gel electrophoresis at pH 8.9, and highpressure liquid chromatography. Further criteria of purity included amino-terminal analysis of fraction IV yielding only aspartic acid. A total of 1.3 mg of fraction II, and 3.8 mg of fraction IV somatostatin-like peptides were obtained from 10 g of fresh frozen islets. Characterization of the two peptides revealed both peptides slightly more acidic than synthetic tetradecapeptide somatostatin. Fraction II had an isoelectric point of 8.0-8.3, and fraction IV 8.3-9.0. Molecular weight estimation by sodium dodecyl sulfate-urea polyacrylamide gel electrophoresis revealed similar mobility of both peptides, between pancreatic polypeptide (mol wt 4,500) and glucagon (mol wt 3,500). The mobility was not altered by reduction, and was approximately twice the size of synthetic tetradecapeptide somatostatin (mol wt 1,800). This confirmed that the peptides were single polypeptide chains and not aggregates, or somatostatin bound to larger proteins. Molecular weight determination by gel filtration chromatography on Bio-Gel P-6 in 8 M urea gave an estimated mol wt of 3,700. Amino acid analysis of the two immunoreactive somatostatins indicated that they were very similar in composition. Both pancreatic somatostatins (1 muM) had full biological activity relative to synthetic somatostatin measured as inhibition of growth hormone release from rat anterior pituitary cells.
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PMID:Isolation and characterization of immunoreactive somatostatin from fish pancreatic islets. 610 73

We determined the effect of somatostatin on water, glucose, sodium, and urea transport by utilizing an in vivo perfusion technique in the rat jejunum. Somatostatin (2.5-37.5 micrograms/kg . min) infused intravenously had no effect on basal absorption of water, sodium, or urea. However, infusion of somatostatin at the rate of 10 micrograms/kg . min completely blocked prostaglandin E1-induced inhibition of water absorption (P less than 0.01) and partially blocked net water secretion induced by theophylline (P less than 0.001). This effect of somatostatin occurred despite unchanged basal or theophylline and prostaglandin E1-stimulated cyclic AMP levels. In contrast, somatostatin did not affect glucose absorption in the rat jejunum. These results demonstrate that somatostatin may affect water and electrolyte movement by blocking the action of cyclic AMP in the rat jejunum.
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PMID:Somatostatin inhibits fluid secretion in the rat jejunum. 610 48

A substance with somatostatin-like immunoreactivity (SLI) was found in extracts of goldfish, frog, and cow retina. Dilutions of retinal SLI parallel the standard curve for radioimmunoassay obtained with synthetic somatostatin. Chromatography of goldfish retinal extract on Sephadex G-50 revealed two peaks of SLI, one that coeluted with synthetic somatostatin and one that eluted as a larger molecule. Incubation in 8 M urea did not alter the chromatographic pattern of the extract. SLI was present in extracts of frog optic nerve and tectum in concentrations higher than those found in the retina. In goldfish retina, SLI was localized by immunofluorescence to four types of processes in the inner plexiform layer; their origins could be traced to three classes of SLI-containing cell bodies in the proximal row of the inner nuclear layer and one class in the ganglion cell layer. Localization of SLI to cells of the retina and characterizations of the molecular forms of retinal SLI suggest that the retina is a promising model system for studies on the potential neurotransmitter function of somatostatin.
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PMID:Somatostatin-like immunoreactivity in the retina. 610 39


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