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At least 19 recordsLinked to original sources
PubMed1980

Effects of glicentine on insulin secretion.

The glucagon-like immunoreactivity of the gastrointestinal tract is heterogeneous, probably including several different peptides. One of these peptides, glicentine, has recently been extracted and highly purified. Furthermore, by immunocytochemistry a glicentine-like peptide has been reported to occur in the glucagon cell of the pancreatic islets. In the present study we investigated the effects of pure glicentine on insulin release in vivo in mice. The effects were compared with effects of two other peptides, glucagon and GIP. It was found that glicentine had no influence on basal insulin secretion. This was in contrast to equimolar doses of glucagon and GIP, which both stimulated the secretion of insulin. Glucose-induced insulin release was partially inhibited by glicentine. D-glucose, in a dose selected to give a response of 25% of its maximal, raised the plasma insulin concentrations by 44.0 +/- 5.9 microU/ml. The corresponding rise for glicentine plus D-glucose was 22.3 +/- 3.7 microU/ml, i.e. glicentine inhibited glucose-induced insulin released by about 50% (p < 0.01). GIP, on the other hand, enhanced glucose-induced insulin release. This enhancement was diminished by glicentine, a reflection of the inhibition by glicentine of the glucose-induced insulin release. Neither glicentine nor GIP in the doses tested had any effect on insulin secretion induced by cholinergic stimulation. In conclusion, glicentine seems to have no effect on basal insulin release in the mouse, but it partially inhibits glucose-induced insulin secretion. Thus, if the recently demonstrated glicentine-like peptide in the glucagon cell is authentic glicentine, the glucagon cell of the pancreatic islets may contain peptides with stimulatory (glucagon) as well as inhibitory (glicentine) effects on insulin secretion induced by glucose.

Animals↗
PubMed2005

Contraction induced by glicentin on smooth muscle cells from the human colon is abolished by exendin (9-39).

UNLABELLED: Glicentin and glucagon-like peptide-1 (7-36) amide (GLP-1) are gut hormones released during digestion. Glicentin and GLP-1 slow down gastric emptying and glicentin can switch off the duodenojejunal fed motor pattern. The effect of glicentin on the motor activity of colon has never been reported in humans. Our aim was to determine if circular smooth muscle cells (SMC) from the human colon are target cells for glicentin or GLP-1, and if their motility is dependent upon these digestive hormones. METHODS: Twenty-two resections were performed on patients operated for colon adenocarcinoma. The SMC were isolated from colonic circular muscle layer and cell contraction was assessed. RESULTS: Glicentin caused a dose-related contraction of SMC, when GLP-1 determined a contraction of weak amplitude. Exendin-(9-39), described as a GLP-1 receptor antagonist, inhibited contraction due to glicentin or GLP-1. In contrast, on antral SMC from rabbit, GLP-1 exerts neither relaxation nor contraction; however, exendin-(9-39) dose dependently reduced the contractile activity of glicentin [glicentin EC(50) = 5 pM, exendin-(9-39) pA(2) = -9.36]. CONCLUSIONS: The circular muscle from the human colon is a target tissue for glicentin and GLP-1. Whereas glicentin is a long-life digestive hormone which would contribute to segmental contraction, the biological activity of GLP-1 remains unknown on this tissue. On the digestive smooth muscle, exendin-(9-39) behaved as an antagonist for two members of the glucagon-receptor family, GLP-1 and glicentin.

Adult↗
PubMed1995

Insulinotropic action of human glicentin in dogs.

Glicentin has been demonstrated to be released in response to the intraluminal administration of nutrients, but its biological action remains unknown. To clarify the effect of glicentin on the endocrine function of the pancreas, the present study was performed using an in vivo local circulation system of the canine pancreas. During infusion of 0.5% solution of glucose or arginine, 100 and 400 pmol glicentin and 400 pmol glucagon were administered into the pancreaticoduodenal artery (PA) within 10 minutes at 40-minute intervals successively. During glucose infusion, blood glucose in the femoral artery did not change following administration of 100 pmol glicentin, but slightly increased following 400 pmol glicentin. Plasma insulin (immunoreactive insulin [IRI]) in the pancreaticoduodenal vein (PV) increased significantly only following infusion of 400 pmol glicentin. Plasma glucagon (immunoreactive glucagon [IRG]), measured with a specific antiserum to the C-terminal portion of glucagon, did not change following administration of 100 pmol glicentin, but was slightly elevated following 400 pmol glicentin. Plasma total IRG, measured with a nonspecific antiserum, increased promptly after administration of 100 and 400 pmol glicentin. During arginine infusion, the response of plasma IRI to glicentin was markedly exaggerated both in dosages of 100 and 400 pmol. From the present study it was concluded that human glicentin clearly increases insulin release from the canine pancreas.

Animals↗
PubMed2003

Postnatal and postprandial changes in plasma concentrations of glicentin in term and preterm infants.

AIM: To examined the changes in basal plasma concentrations of glicentin in developing children and the postnatal and postprandial changes in plasma glicentin levels in infants. METHODS: Glicentin, an active component of enteroglucagon, is considered to have a significant trophic action on the intestinal mucosa. Fasting plasma concentrations of glicentin in healthy children and in term and preterm infants were measured before and 30 min after feeding during the first 14 d of life. RESULTS: Plasma basal concentrations of glicentin in children under 1 y of age were significantly higher than those in children aged 1 to 15 y. Plasma basal concentrations of glicentin at 5 or 6 d (2496 and 2190 pg/ml) and at 14 d (2987 and 2817 pg/ml) after birth were significantly higher than those at 1 or 2 d (1098 and 1240 pg/ml) after birth in normal birthweight (NBW) and low-birthweight (LBW) infants. There was no significant difference in the glicentin level between infants at 1 or 2 d (1864 pg/ml) and at 5 or 6 d (1910 pg/ml) after birth in very-low birthweight (VLBW) infants, but the levels at 14 d (3310 pg/ml) after birth were significantly higher than either of those levels. Plasma glicentin concentrations after feeding were significantly higher than those before feeding at 1 or 2 d and at 5 or 6 d after birth in NBW and LBW infants, but a significant increase in the plasma glicentin level after feeding was first observed at 14 d after birth in VLBW infants. There were no significant differences in the basal plasma (2401 and 2718 pg/ml) and postprandial (3007 and 3912 pg/ml) glicentin levels between breastfed and formula-fed infants. CONCLUSION: The results of the study suggest that glicentin may play an important role in intestinal mucosal growth in the early period of life, although its role in VLBW infants should be further investigated.

Breast Feeding↗
PubMed1986

Effect of glicentin-related peptides on glucagon secretion in anaesthetized dogs.

Recent studies have demonstrated that glicentin is released during nutrient ingestion. However, the biological function of glicentin remains unclear. In order to clarify the role of glicentin in the enteroinsular axis, the effect of glicentin-related peptides was investigated using in vivo local circulation of canine pancreas. Peaks I and II of gut glucagon-like immunoreactivity, partially purified from porcine intestinal extract by affinity chromatography and gel filtration, synthesized hexadecapeptide of N-terminal glicentin (1-16) and synthesized octapeptide of C-terminal glicentin (62-69) were administered for 10 min into the pancreaticoduodenal artery of canine pancreas. Blood samples were then drawn from the pancreaticoduodenal vein. The administration of peak I of glucagon-like immunoreactivity during arginine infusion in a dosage of 20 ng reduced the glucagon secretion by 42 pmol/l (p less than 0.05), whereas peak II of glucagon-like immunoreactivity (20 ng) slightly increased the plasma level of insulin, although not significantly. The administration of glicentin (1-16) in a dosage of 400 ng during saline infusion did not alter the plasma insulin level, but reduced the plasma glucagon level in the pancreaticoduodenal vein by 29 pmol/l (p less than 0.05). In addition, glicentin [62-69] in a dosage of 400 ng exerted a decrease in both the plasma insulin (40 mU/l, p less than 0.05) and glucagon level (27 pmol/l, p less than 0.05). The present study demonstrates the suppression of pancreatic glucagon release during the infusion of peak I glucagon-like immunoreactivity and N- or C-terminal glicentin-related peptide. Therefore, it is suggested that glicentin released during nutrient intake might inhibit the secretion of glucagon.

Animals↗
PubMed1999

Plasma glicentin in diabetic and gastrectomized patients.

Recent successful synthesis of human glicentin prompted us to establish an immunoassay method for determination of human glicentin in plasma. Human glicentin in plasma was measured using a newly developed sandwich ELISA. The mean fasting levels of human glicentin were 18.6+/-2.4 and 19.7+/-2.1 pM in normal subjects and diabetic patients, respectively. In diabetic patients with renal failure, plasma glicentin was elevated, exceeding 100 pM. In normal subjects, plasma glicentin increased to a peak level of about 130 pM at 60 min after an oral glucose load, and then decreased. In patients who underwent gastrectomy, plasma glicentin rapidly increased to a peak of about 300 pM at 30 min after oral glucose load. In a patient with short bowel syndrome plasma glicentin did not change following an oral glucose load. These results correspond with previous findings for gut glucagon-like immunoreactive materials (GLI) or enteroglucagon. We conclude that glicentin is secreted from the small intestine in response to intraluminal glucose stimulation in humans.

Blood Glucose↗
PubMed2003

Effect of glicentin on gut mucosal growth in rats with jejunal and ileal Thiry-Vella fistulas.

BACKGROUND/PURPOSE: Glicentin stimulates growth of normal and atrophic small bowel mucosa; the mechanisms for this trophic effect of glicentin are not completely known. The purpose of this study was to determine whether the trophic effect of glicentin is mediated by mechanism involving luminal or nonluminal factors and determine whether glicentin exerts a differential trophic effect on either jejunal or ileal mucosa. METHODS: Thirty-two male Wistar rats underwent construction of either a jejunal or ileal Thiry-Vella fistula (TVF). After 10 days recovery period, rats were further subdivided into groups to receive either saline (control) or glicentin (100 microg/kg/d). Rats were killed on day 8, and TVF as well as corresponding segments of intact jejunum or ileum were removed. Mucosa was scraped, weighed, and analyzed for protein content and Alp activity. In addition, representative sections of full-thickness bowel from each group were examined histologically. RESULTS: In the jejunal TVF group, glicentin increased mucosal growth measurements in both the TVF and the intact jejunum. However, in the ileal TVF group, glicentin stimulated proliferation of intact ileal mucosa only; it had no effect on ileal mucosa in the TVF. CONCLUSIONS: These results suggest that glicentin exerts a systemic effect independent of luminal factors on the proliferation of proximal gut mucosa in addition to an indirect effect produced by stimulation of endogenous luminal secretions. In contrast, an indirect mechanism appears to be the predominant action of glicentin on growth of distal gut mucosa.

Anastomosis, Surgical↗
PubMed1988

Effect of glicentin-related peptides upon the secretion of insulin and glucagon in the canine pancreas.

In order to clarify responses of the endocrine pancreas to glicentin, four glicentin-related peptides were investigated in a local circulation preparation of the canine pancreas. These peptides were administered in a dosage of 200 pmole for 10 min into the pancreaticoduodenal artery under the continuous infusion of 0.5% arginine solution. In a group of six dogs, the administration of glicentin-related pancreatic peptide (GRPP) and glicentin 1-16 resulted in an increase in plasma insulin (IRI) and a decrease in plasma glucagon (IRG). In the other group of six dogs, the administration of glicentin 62-69 induced an increase in plasma IRI and a decrease in plasma IRG. Following the successive infusion of oxyntomodulin, both plasma IRI and IRG increased slightly. Porcine glucagon administered at the end of each experiment exerted a rise in blood glucose and plasma IRI in addition to an increase in plasma IRG. In comparison of the maximal responses of plasma IRI and IRG to these glicentin-related peptides, the administration of glicentin 1-16, 62-69 or GRPP elicited an increase in plasma IRI and a decrease in plasma IRG. In contrast, oxyntomodulin and glucagon increased both plasma IRI and IRG. The present study indicates that glicentin-related peptides, both the N- and C-terminal portions, affect the endocrine function of the pancreas and suggests that glicentin released by nutrient ingestion plays an important role in the enteroinsular axis.

Animals↗
PubMed1981

Relationship of glicentin to proglucagon and glucagon in the porcine pancreas.

We have previously isolated from porcine small intestine a peptide known as glicentin. The C-terminal portion of glicentin consists of the sequence of glucagon extended at its C terminus by an octapeptide, and differs slightly from the sequence of a proposed fragment of proglucagon. Glicentin-like material has been demonstrated in the pancreatic A cell, wherein it is located in the periphery of the secretory granules, whereas glucagon is located in the centre of the granules. To study the relationship of glicentin to the biosynthesis of glucagon, we have now investigated the glucagon-like and glicentin-like peptides in extracts and perfusates of the porcine pancreas. Our findings that a peptide with glicentin-like immunoreactivity, and intermediate in size between glicentin and glucagon, is secreted synchronously with glucagon suggest that this glicentin-related peptide is a major cleavage product of proglucagon.

Animals↗
PubMed1997

Trophic effects of glicentin on rat small-intestinal mucosa in vivo and in vitro.

To define the role of glicentin the active site of enteroglucagon, we evaluated the trophic effects of recombinant rat glicentin on rat small intestine and IEC-6 cells. In vivo, a significant increase was observed in jejunal wet weight, protein content, DNA content, and alkaline phosphatase activity after the subcutaneous administration of 100 micrograms/kg per day of glicentin for 2 weeks. In the ileum, however, there were no significant differences between the control versus glicentin groups in any of these parameters. Ornithine decarboxylase (ODC) activity 3.5 h after an intraperitoneal injection of glicentin was increased in the jejunal mucosa, but not in the ileal mucosa. In vitro, glicentin, at a dose of more than 100 ng/ml, significantly increased both tritium-thymidine incorporation and the number of IEC-6 cells. These findings indicate that glicentin exerts direct trophic effects on the rat small-intestinal mucosa and on the rat small-intestinal cell line, IEC-6, and that this peptide appears to be an active site of enteroglucagon.

Alkaline Phosphatase↗
PubMed2001

Glicentin, an active enteroglucagon, has a significant trophic role on the small intestine but not on the colon in the rat.

BACKGROUND: Many experiments have indicated that the gut glucagons (enteroglucagons) are associated with cell proliferation in the small intestine. However, recent studies have failed to show trophic effects of glicentin (enteroglucagon) on the intestine. AIMS: To examine the effects of glicentin on intestinal proliferation in vivo in the rat. METHODS: Rats were established on total parenteral nutrition for 6 days. Four experimental groups were given daily doses of 1, 4, 20 and 80 microg/rat of glicentin via the jugular vein. Rats fed by total parenteral nutrition and rats fed chow ad libitum were used as controls. Tissues taken from the duodenum, jejunum, ileum and colon were fixed in Carnoy's fluid and microdissected to determine the metaphase arrest scores and crypt fission ratios. RESULTS: The mean metaphase arrest scores per crypt of the small intestine were significantly increased in the rats given 4, 20 and 80 microg of glicentin. These responses were dose-dependent, and were most prominent in the ileum. Crypt fission of the ileum was significantly decreased in the 20 and 80 microg glicentin groups. Glicentin had no effects on proliferation or fission in the colon. CONCLUSIONS: Glicentin is trophic to the rat small intestine, but not the colon.

Animals↗
PubMed2006

Effects of extremely early enteral feeding on plasma glicentin levels in very-low-birthweight infants.

AIM: Glicentin, an active component of enteroglucagon, is considered to have a significant trophic action on the intestinal mucosa. We examined the effects of extremely early enteral feedings on the postnatal and postprandial changes in plasma glicentin levels in very-low-birthweight (VLBW) infants. METHODS: We measured the plasma glicentin concentrations before and after feedings at 1 or 2 days, 5 or 6 days and 14 days after birth in 21 VLBW infants. The subjects were randomly divided into an extremely early feeding group, which was started on breast milk within 24 h after birth, and a control group, which was started on breast milk more than 24 h after birth. RESULTS: Plasma basal concentrations of glicentin at 5 or 6 days and at 14 days after birth were significantly higher than those at 1 or 2 days after birth in the early feeding group. The basal glicentin level at 14 days after birth was significantly higher than that at 1 or 2 days. The basal levels at 5 or 6 days and at 14 days after birth in the early feeding group were significantly higher than those in the control group. Plasma glicentin concentrations after feeding were significantly higher than those before feeding at 5 or 6 days and 14 days after birth in the early feeding group, but those levels were significantly higher only at 14 days after birth in the control group. CONCLUSION: Our results suggest that extremely early enteral feedings may play an important role in the development of glicentin secretion and intestinal mucosal growth in the early period of life in VLBW infants.

Enteral Nutrition↗
PubMed1980

Glucagon- and glicentin-immunoreactive cells in the human digestive tract.

The distribution and cellular location of substances reacting with anti-glucagon or anti-glicentin sera, i.e., glucagon-like and glicentin-like immunoreactivities, were studied in the human digestive tract using the immunofluorescence and immunoperoxidase methods. Both types of immunoreactivity were (1) absent in the antrum, (2) abundant in cells located at the periphery of pancreatic islets, (3) unevenly present in cells scattered in the epithelium of the small intestinal mucosa, the glicentin-immunoreactive cells being particularly abundant in the ileum. In the pancreas, and, when simultaneously present, in the intestine, both glucagon and glicentin immunoreactivities were located in the same cells. The precise ultrastructural location of each immunoreactivity was readily made using colloidal gold and ferritin tracers on ultrathin sections of glutaraldehyde-osmium fixed and epoxy resin-embedded tissues. In the pancreas, both glucagon and glicentin immunoreactivities were found in the granules of the A-type cells; the glucagon immunoreactivity was only present in the core of the granule, whereas the glicentin immunoreactivity was found either in the peripheral halo only, or throughout the entire granule. In the small intestine, both immunoreactivities were located inside the granules of the L-type cells. Quantitative specificity tests suggested that the glucagon- and the glicentin-like substances of the pancreas differ from those found in the intestine.

Cytoplasmic Granules↗
PubMed1984

Immunohistochemical studies on glucagon, glicentin and pancreatic polypeptide in human stomach: normal and pathological conditions.

Endocrine-like cells containing glucagon, glicentin or pancreatic polypeptide immunoreactivity in human foetal and adult stomach, with or without disease, were studied with the indirect immunoperoxidase method and mirror sectioning technique. In foetal and neonatal oxyntic mucosae, there were endocrine-like cells with glucagon and glicentin immunoreactivities and argyrophilia. Cells containing glicentin immunoreactivity alone were detected earlier than glucagon cells during foetal development, and were also distributed throughout foetal to neonatal life. Bovine pancreatic polypeptide immunoreactivity coexisted in a subpopulation of the glucagon-glicentin cells. These cells were absent from normal oxyntic mucosa in the postneonatal period and from normal antral mucosa throughout life. Hamartomatous polyp in adult oxyntic mucosa, hyperplastic oxyntic mucosa in Menetrier's disease and atrophic oxyntic mucosa in a remnant stomach with cancer showed scattered glucagon-glicentin cells, but few or no cells containing bovine pancreatic polypeptide. Intestinalized mucosa showed plentiful glicentin cells with occasional glucagon and/or bovine pancreatic polypeptide immunoreactivity. Some gastric cancer cells of both diffuse and adenoplastic types contained immunoreactive glicentin and, less frequently, glucagon. Bovine pancreatic polypeptide immunoreactivity was detected in a few adenoplastic cancer cells, but not in diffuse type cells. Three different anti-pancreatic polypeptide sera against bovine, porcine or human pancreatic polypeptide detected basically the same cells mentioned above, but pancreatic polypeptide cells lacking human pancreatic polypeptide immunoreactivity were also present in foetal oxyntic mucosa. Immunoabsorption tests revealed that the bovine pancreatic polypeptide immunoreactivity was remote from peptide YY and neuropeptide Y.

Adolescent↗
PubMedDate not supplied

Response of plasma glicentin to intraduodenal administration of glucose in piglets.

Controversial results concerning the secretion of glicentin prompted us to investigate the response of circulating glicentin to intraduodenal administration of glucose in piglets. A 20% solution of glucose (2 g/kg) was administered into the duodenum of six piglets in a fully conscious state. As blood glucose rose, plasma insulin increased to a peak of 21 +/- 4 microU/ml. Plasma glucagon, determined by C-terminal-specific antiserum, was 70 +/- 30 pg/ml at fasting and slightly increased after the glucose load. Plasma immunoreactive glucagon measured by cross-reacting glucagon antiserum increased from the baseline of 1563 +/- 260 to a peak of 4738 +/- 415 pg/ml at 120 min. Plasma glicentin determined by antiserum R 64 was 463 +/- 81 pmol/l at baseline and reached a peak level of 1081 +/- 174 pmol/l at 90 min. The percent changes of plasma glucagon from the fasting level measured by cross-reacting antiserum and glicentin were 296 and 233%, respectively. There was a significant correlation between plasma glucagon measured by cross-reacting antiserum and glicentin (r = 0.817, P less than 0.001). Chromatography of plasma obtained during glucose load revealed the heterogeneity of glicentin. It can be concluded from the present study that glicentin is clearly secreted in response to intraluminal administration of glucose.

Animals↗
PubMedDate not supplied

Response of plasma glicentin to fat ingestion in piglets.

In order to elucidate the response of plasma glicentin to fat ingestion, butter, glycerol or palmitate was administered into the duodenum of piglets in a fully conscious state and plasma glicentin and glucagon were determined. Butter instillation did not change blood glucose. Plasma triglyceride rose gradually 120 min after butter loading. Plasma insulin and glucagon measured by antiserum specific to the C-terminal slightly increased following butter administration and plasma total glucagon and glicentin increased gradually and significantly. The increments of total glucagon and glicentin were 179 and 158%, respectively. However, chromatography of porcine plasma obtained during fat loading revealed heterogeneity of glicentin-related peptides. Glycerol ingestion induced a slight rise of plasma total glucagon. Administration of palmitate revealed an increase in plasma total glucagon and glicentin. The present study clearly demonstrates the secretion of glicentin following fat ingestion, which might be caused by the hydrolysates of triglyceride, as suggested in previous dog experiments.

Animals↗
PubMed1986

Renal catabolism of 125I-glicentin.

The renal catabolism of 125I-glicentin has been studied in vivo by the disappearance of this peptide from the plasma of bilaterally nephrectomized, ureteral-ligated, or normal rats and by using tubular microinfusion techniques. In addition the catabolism of glicentin by the isolated, perfused kidney has been studied. Results from in vivo studies demonstrated that half-disappearance time was lower in control (59.5 +/- 1.8 min) than in bilaterally nephrectomized rats (97.2 +/- 2.6 min), and this value was significantly higher than that of ureteral-ligated animals (83.2 +/- 1.1 min, P less than 0.005). Microinfusion experiments revealed that when 125I-glicentin was injected into the proximal tubule, no trichloroacetic-precipitable radioactivity was recovered in the urine, whereas most of inulin injected was recovered. By contrast most of the 125I-glicentin injected into the distal tubule was recovered in the urine. In isolated kidney experiments, organ clearance rate of 125I-glicentin averaged 0.88 +/- 0.10 ml/min, a value significantly higher than that of glomerular filtration rate (0.72 +/- 0.06 ml/min, P less than 0.005, paired data), and both parameters showed a close linear relationship (r = 0.90). Urinary clearance of glicentin was negligible. These results demonstrate that the kidney plays a major role in the catabolism of glicentin, mainly by glomerular filtration and tubular catabolism. The site of tubular catabolism appears to be the proximal tubule. Peritubular uptake was minimal.

Animals↗
PubMed1979

Glicentin immunoreactive cells: their relationship to glucagon-producing cells.

The cellular and subcellular localization of one of the gut glucagon-like immunoreactants (GLI-1 or glicentin) and the relative distribution of glicentin- and glucagon-containing cells were investigated by immunocytochemistry. By immunofluorescence, the antiglicentin serum, which does not react with glucagon, revealed positive cells in the islets of Langerhans and in the gut mucosa, particularly in the terminal ileum and colon. In the intestinal mucosa, it was proven ultrastructurally that the glicentin immunoreactive cells correspond to the L cell and that the secretory granules represent the storage compartment of the immunoreactive material. In pancreatic islets, consecutive semithin sections treated with antiglicentin and specific antiglucagon sera showed that the same A cell population reacted with both sera, while immunoperoxidase staining on thin sections revealed that the immunoreactive material was confined to the secretory granules. The same results were obtained on dog oxyntic mucosa, where the glicentin- and glucagon-containing cells were identified as the gastric A cell. The immunocytochemical demonstration of a common glicentin-like material in the A and L cells together with the known presence of a common immunoreactant in glicentin and glucagon strongly support the idea that the A and L cells are ontogenetically related and synthesize their secretory product via a glicentin-like precursor which, by specific cleavage, could yield glucagon and gut glucagon-like immunoreactants.

Animals↗