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  • 1
    Electronic Resource
    Electronic Resource
    Effects of a transplantable insulinoma upon regulatory peptide concentrations in the gastrointestinal tract of the rat (1986)
    Springer
    Diabetologia 29 (1986), S. 334-338 
    Details
    ISSN: 1432-0428
    Keywords: Insulinoma ; substance P ; neurokinin A ; vasoactive intestinal polypeptide ; somatostatin ; gastrin-releasing peptide ; enteroglucagon
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The rapid growth (0.8±0.3 g/day) of a transplantable insulinoma, which also contained substance P (2.9±2.3 pmol/g) and gastrin-releasing peptide (3.2± 2.1 pmoll/g), resulted in the development of hyperphagia, hyperinsulinaeinia and hypoglycaemia in rats (n=8). After a 14-day growth period, the insulinoma-bearing rats showed an increase (49%; p〈0.01) in the weight of the small intestine but no significant change in stomach weight compared with control animals. The content (pmol/organ) of somatostatin, substance P, neurokinin A and vasoactive intestinal peptide in the stomachs of the tumour rats was unchanged. A depletion in the content (53% p〈0.01) and concentration (57%; p〈0.01) of gastrin-releasing peptide, however, suggested either hypersecretion, possibly mediated through hypoglycaemia-induced vagal stimulation, or inhibition of synthesis. The concentration and content of glucagon-like immunoreactivity (enteroglucagon) in the small intestine of the insulinoma rats increased markedly (47%; p〈0.01 and 120%; p〈0.01). This increase is consistent with a proposed role of this peptide as a factor trophic to the intestinal mucosa. No significant changes in the concentrations of somatostatin, substance P, neurokinin A, vasoactive intestinal peptide and gastrin-releasing peptide in the small intestine were observed. However, the increase in gut weight resulted in a greater content of vasoactive intestinal peptide (40%; p〈0.01) and substance P (37%; p〈0.05) in the insulinoma rats.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00452072
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Glycation of glucagon-like peptide-1(7–36)amide: characterization and impaired action on rat insulin secreting cells (1998)
    Springer
    Diabetologia 41 (1998), S. 1187-1193 
    Details
    ISSN: 1432-0428
    Keywords: Keywords GLP-1(7 ; 36)amide ; glycation ; insulin secretion ; BRIN-BD11 cells.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Glucagon-like peptide-1(7–36)amide (truncated GLP-1, tGLP-1) is a potent insulin releasing hormone of the enteroinsular axis. This study has examined glycation of tGLP-1 and effects of such structural modification on insulin secretion. Monoglycated tGLP-1 (Mr 3463.8, determined by plasma desorption mass spectrometry) was prepared by incubation with glucose under reducing conditions and purified by reversed-phase high performance liquid chromatography. Automated Edman degradation indicated that tGLP-1 was specifically glycated at the amino terminal His7 site. In extracts from mouse small intestine, glycated tGLP-1 represented approximately 14 % of the total tGLP-1 content. Effects of glycated and non-glycated tGLP-1 on insulin secretion were examined using glucose-responsive clonal BRIN-BD11 cells. In acute (20 min) incubations, 10–9 mol/l tGLP-1 enhanced insulin release by 2.2-fold and 1.5-fold at 5.6 and 11.1 mmol/l glucose, respectively. In contrast, 10–9 mol/l glycated tGLP-1 failed to stimulate secretion and insulin output was decreased by 34–73 % following glycation. At 5.6 mmol/l glucose, non-glycated tGLP-1 (3 × 10–10 mol/l–10–8 mol/l) exerted a 2.3-fold to 3.2-fold increase in insulin secretion compared with controls. The effect of glycated tGLP-1 at 10–9 mol/l and 3 × 10–9 mol/l was reduced by 51–55 % compared with non-glycated peptide, and its insulinotropic action was effectively abolished. These data indicate that when tGLP-1 is glycated at the amino terminal His7, this modification substantially reduces the glucose-dependent insulinotropic action of the peptide. [Diabetologia (1998) 41: 1187–1193]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250051050
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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