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Query: UMLS:C0432222 (SEM)
 47,337 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Liver affects the release and clearance of many hormones, but the interactions between gastrointestinal peptides and liver function are obscure. Aim of this study was to evaluate plasma concentrations of gastrointestinal peptides during acute hepatic cytonecrosis and during liver regeneration in man. The study was performed in ten patients with viral hepatitis (8 virus A, 2 virus B) in the acute phase (alanine transaminase = 3073 +/- 739 U/L; mean +/- SEM), and at days 7, 45 and 52 after the initial evaluation, during clinical and biochemical recovery (52nd day, alanine transaminase = 77 +/- 26). Plasma concentrations of the following hormones were evaluated by radioimmunoassay: glucagon, insulin, gastrin, vasoactive intestinal peptide, bombesin, neurotensin, cholecystokinin, secretin and motilin. Only serum bombesin and cholecystokinin were significantly (p < 0.01) increased in the acute phase of hepatitis (bombesin: 138 +/- 21 pg/ml; cholecystokinin: 57 +/- 7 pg/ml); they returned to normal values during convalescence (bombesin: 60 +/- 8; cholecystokinin: 31 +/- 4). During hepatocellular necrosis, plasma concentrations of cholecystokinin and bombesin, which are both cellular growth factors and regulatory signals of food introduction and satiety state, were increased by 83% and 130%, respectively. Increase of these hormones may cause the dyspepsia and lack of appetite that characterizes the initial phase of acute viral hepatitis.
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PMID:Gastrointestinal peptide hormones in acute viral hepatitis. 878

Phospholipase A2 has been suggested to be involved in the pathogenesis and pathophysiology of acute pancreatitis. We determined phospholipase A2 and amylase activities in duodenal juice collected during a secretin test from 30 consecutive patients who were suspected to have chronic pancreatitis or biliary disease. The patients underwent endoscopic retrograde cholangiopancreatography (ERCP) the following day. In the 8 patients with ERCP findings of advanced chronic pancreatitis, the mean outputs of phospholipase A2, amylase, and bicarbonate were reduced by 74%, 72%, and 60% compared to the respective values in the 13 (control) patients without a diagnosis of any pancreatic disorder or jaundice. In the 3 patients with recurrent pancreatitis but normal ERCP findings and in the 6 patients with jaundice the output values were not significantly reduced compared to those in the patients without any pancreatic disorder or jaundice. The outputs of amylase and phospholipase A2 were not significantly interrelated, whereas the outputs of phospholipase A2 and bicarbonate correlated well. Receiver characteristic (ROC) curves confirmed the high specificity and sensitivity of phospholipase A2 or bicarbonate output in patients with ERCP findings of advanced chronic pancreatitis compared to those with no changes in pancreatic ducts, with similar probability values of 0.880 +/- 0.111 (SEM), compared to the respective lower value of amylase, 0.676 +/- 0.118. Phospholipase A2 and bicarbonate output proved of equal value as markers of chronic pancreatitis and were superior to amylase output in the secretin test.
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PMID:Duodenal secretion of phospholipase A2, amylase, and bicarbonate in chronic pancreatitis. 960 59

Xenin is a 25-amino-acid peptide extractable from mammalian tissue. This peptide is biologically active. It stimulates exocrine pancreatic secretion and intestinal motility and inhibits gastric secretion of acid and food intake. Xenin circulates in the human plasma after meals. In this study, the cellular origin of xenin in the gastro-entero-pancreatic system of humans, Rhesus monkeys, and dogs was investigated by immunohistochemistry and immunoelectron microscopy. Sequence-specific antibodies against xenin detected specific endocrine cells in the duodenal and jejunal mucosa of all three species. These xenin-immunoreactive cells were distinct from enterochromaffin, somatostatin, motilin, cholecystokinin, neurotensin, and secretin cells, and comprised 8.8% of the chromogranin A-positive cells in the dog duodenum and 4.6% of the chromogranin A-positive cells in human duodenum. In all three species, co-localization of xenin was found with a subpopulation of gastric inhibitory polypeptide (GIP)-immunoreactive cells. Immunoelectron microscopy in the canine duodenal mucosa demonstrated accumulation of gold particles in round, homogeneous, and osmiophilic secretory granules with a closely adhering membrane of 187 +/- 19 nm diameter (mean +/- SEM). This cell type was found to be identical to the previously described canine GIP cell. Immunocytochemical expression of the peptide xenin in a subpopulation of chromogranin A-positive cells as well as the localization of xenin immunoreactivity in ultrastructurally characterized secretory granules permitted the identification of a novel endocrine cell type as the cellular source of circulating xenin.
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PMID:Localization of xenin-immunoreactive cells in the duodenal mucosa of humans and various mammals. 1110 30

The sphincter of Oddi (SO) may not function as a single structure. We aimed to determine the response of the proximal and distal segments of the bile duct (BD-SO) and pancreatic duct (PD-SO) components of the SO to secretin, with and without neural blockade with tetrodotoxin (TTX). In anaesthetized Australian possums, separate manometry catheters were placed in the proximal and distal BD-SO or PD-SO segments to record motility. Secretin, 50-1000 ng kg(-1), was administered, followed by TTX, and re-administration of secretin, 500 and 1000 ng kg(-1). Changes in the motility index (MI, frequency x mean amplitude) were determined. Statistical analysis utilized repeated-measures ANOVA. Secretin produced a dose-dependent decrease in MI from the proximal and distal BD-SO and PD-SO (all P < 0.001). The maximum inhibition, at 1000 ng kg(-1), was 21 +/- 4%, 33 +/- 6% and 42 +/- 5% of control (mean +/- SEM), for proximal and distal BD-SO, and distal PD-SO, respectively. The proximal PD-SO MI, however, was inhibited to 62 +/- 6% of control, at 1000 ng kg(-1). TTX enhanced the secretin-induced response to the same level at the four sites (P < 0.02). We conclude that secretin inhibits the motility of the possum SO in a nonuniform manner and is modulated by neural activity.
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PMID:Secretin induces variable inhibition of motility in different parts of the Australian possum sphincter of Oddi. 1169 6

The purpose of this study was to evaluate whether circulating ghrelin and growth hormone (GH) concentrations in cattle are regulated by endothelin-1 (ET-1), endothelin-3 (ET-3), and secretin. Six Holstein steers (242+/-1 d old, 280.5+/-4.4 kg body weight [BW]; mean+/-SEM) were allocated randomly in an incomplete Latin square design to receive each of 4 treatment compounds (vehicle, ET-1, ET-3, and secretin) with 1-d intervals between successive treatments. The treatment compounds were injected intravenously via a catheter inserted into the external jugular vein of each steer. Blood was sampled from the indwelling catheter at -30, -15, 0, 5, 10, 15, 20, 30, 45, 60, 90, 120, 150, and 180 min. Plasma ghrelin and GH responses to the treatment compounds were measured by a double-antibody radioimmunoassay system. Data were analyzed by using a MIXED procedure of SAS, version 9.1. Plasma acyl ghrelin, total ghrelin, and GH concentrations were increased by both ET-1 and ET-3 injection (ET-1 injection: 311+/-15 pg/mL vs 245+/-15 pg/mL, 2.4+/-0.2 ng/mL vs 1.61+/-0.05 ng/mL, 4.73+/-0.92 ng/mL vs 1.17+/-0.09 ng/mL for acyl ghrelin, total ghrelin, and GH, respectively; ET-3 injection: 337+/-27 pg/mL vs 245+/-15 pg/mL, 2.6+/-0.1 ng/mL vs 1.61+/-0.05 ng/mL, 5.56+/-0.97 ng/mL vs 1.17+/-0.09 ng/mL for acyl ghrelin, total ghrelin, and GH, respectively; P<0.01). Ghrelin and GH concentrations were not changed by secretin injection throughout the experimental periods. These results indicate that ET-1 and ET-3 stimulate ghrelin and GH secretion in cattle and demonstrate for the first time that endogenous ghrelin released in response to endothelin injection stimulates GH secretion in vivo in cattle.
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PMID:Endogenous ghrelin released in response to endothelin stimulates growth hormone secretion in cattle. 1973 62


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