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198 results on '"Gingerich, R"'

18. Report of the American Diabetes Association's Task Force on standardization of the insulin assay

Author

Robbins, D. C., primary, Andersen, L., additional, Bowsher, R., additional, Chance, R., additional, Dinesen, B., additional, Frank, B., additional, Gingerich, R., additional, Goldstein, D., additional, Widemeyer, H. M., additional, Haffner, S., additional, Hales, C. N., additional, Jarett, L., additional, Polonsky, K., additional, Porte, D., additional, Skyler, J., additional, Webb, G., additional, and Gallagher, K., additional

Published
1996
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27. Insulin response, glucose homeostasis and glut4 levels in muscle after pancreas transplant: Comparison of initial study with one year follow-up

Author

Hanks, J, primary, McAloon-Dyke, M, additional, Clark, B, additional, Kahn, B, additional, Weinreb, J, additional, Minaker, KL, additional, Wong, G, additional, Morse, L, additional, Brown, R, additional, Shapiro, M, additional, Gingerich, R, additional, Rosenlof, L, additional, Pruett, T, additional, Andersen, DK, additional, and Elahi, D, additional

Published
1992
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30. Islet cell responses to glucose in human transplanted pancreas

Author

Elahi, D., primary, Clark, B. A., additional, McAloon-Dyke, M., additional, Wong, G., additional, Brown, R., additional, Shapiro, M., additional, Minaker, K. L., additional, Flanagan, T. L., additional, Pruett, T., additional, Gingerich, R., additional, and et, al., additional

Published
1991
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34. Effect of glucagon-like peptide 1 on non-insulin-mediated glucose uptake in the elderly patient with diabetes.

Author

Meneilly, Graydon S., McIntosh, Christopher H. S., Pederson, Raymond A., Habener, Joel F., Gingerich, Ronald, Egan, Josephine M., Finegood, Diane T., Elahi, Dariush, Meneilly, G S, McIntosh, C H, Pederson, R A, Habener, J F, Gingerich, R, Egan, J M, Finegood, D T, and Elahi, D

Subjects
GLUCAGON-like peptide 1, GLUCOSE, DIABETES in old age, ANALYSIS of variance, BLOOD sugar, CLINICAL trials, COMPARATIVE studies, DIABETES, GLUCAGON, GLYCOSYLATED hemoglobin, HYPOGLYCEMIC agents, INSULIN, RESEARCH methodology, MEDICAL cooperation, ORAL drug administration, PEPTIDES, RESEARCH, EVALUATION research, PATIENT selection, GLUCAGON-like peptides, GLUCOSE clamp technique
Abstract

An important cause of elevated glucose levels in elderly patients with diabetes is an alteration in non-insulin-mediated glucose uptake (NIMGU). Glucagon-like peptide 1 (GLP-1) is an intestinal insulinotropic hormone. It has been proposed that this hormone also lowers glucose levels by enhancing NIMGU. This study was conducted to determine whether GLP-1 augments NIMGU in elderly patients with diabetes, a group in which NIMGU is known to be impaired. Studies were conducted on 10 elderly patients with type 2 diabetes (aged 75 +/- 2 years, BMI 27 +/- 1 kg/m(2)) who underwent paired 240-min glucose clamp studies. In each study, octreotide was infused to suppress endogenous insulin release, and tritiated glucose methodology was used to measure glucose production and disposal rates. For the first 180 min, no glucose was infused. From 180 to 240 min, glucose was increased to 11 mmol/l using the glucose clamp protocol. In the GLP-1 study, GLP-1 was infused from 30 to 240 min. In a subsequent control study, insulin was infused using the glucose clamp protocol from 30 to 240 min to match the insulin levels that occurred during the GLP-1 infusion study. During hyperglycemia, GLP-1 enhanced glucose disposal (control study: 2.52 +/- 0.19 mg x kg(-1) x min(-1); GLP-1 study: 2.90 +/- 0.17 mg x kg(-1) x min(-1); P < 0.0001). Hepatic glucose output was not different between studies. We conclude that GLP-1 may partially reverse the defect in NIMGU that occurs in elderly patients with diabetes. [ABSTRACT FROM AUTHOR]

Published
2001
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41. Des-(27-31)C-peptide. A novel secretory product of the rat pancreatic beta cell produced by truncation of proinsulin connecting peptide in secretory granules.

Author

Verchere, C B, Paoletta, M, Neerman-Arbez, M, Rose, K, Irminger, J C, Gingerich, R L, Kahn, S E, and Halban, P A

Abstract

Insulin and connecting peptide (C-peptide) are produced in equimolar amounts during proinsulin conversion in the pancreatic beta cell secretory granule. To determine whether insulin and C-peptide are equally stable in beta cell granules (and thus secreted in equimolar amounts), neonatal and adult rat beta cells were pulse-chased, and radiolabeled insulin and C-peptide analyzed by high performance liquid chromatography. A novel truncated C-peptide was identified and shown by mass spectrometry to be des-(27-31)C-peptide (loss of 5 C-terminal amino acids). Des-(27-31)C-peptide is a major beta cell secretory product, accounting for 37.4 +/- 1.6% (neonatal) and 8.5 +/- 0.6% (adult) of total labeled C-peptide in secretory granules after 10 h of chase. Des-(27-31)C-peptide is also secreted in a glucose-sensitive manner from the perfused adult rat pancreas, accounting for approximately 10% of total C-peptide immunoreactivity secreted. Human C-peptide is also a substrate for truncation in granules. Thus, when human proinsulin was expressed (infection with recombinant adenovirus) in transformed (INS) rat beta cells, human des-(27-31)C-peptide was secreted along with the intact human peptide and both intact and truncated rat C-peptide. In addition to truncation, 33.1 +/- 1.2% of C-peptide in neonatal but not adult rat beta cell granules was further degraded. Such degradation was completely inhibited by ammonium chloride (known to neutralize intra-granular pH), whereas truncation was only partially inhibited by approximately 50%. In conclusion, a novel beta cell secretory product, des-(27-31)C-peptide, has been identified and should be considered as a potential bioactive peptide. Both truncation and degradation of C-peptide are responsible for non-equimolar secretion of insulin and C-peptide in rat beta cells.

Published
1996

42. Ultrastructural localization of pancreatic polypeptide in the F cell of the dog pancreas.

Author

Greider, M H, Gersell, D J, and Gingerich, R L

Abstract

The F cell of the dog pancreas has been identified as the specific cell type containing pancreatic polypeptide. This localization of pnacreatic polypeptide was accomplished by immunocytochemical staining of ultrathin sections and direct electron microscopic identification. Verification of the specificity of the reaction was obtained by blocking experiments on serial sections of the same cell. It is proposed that the name F cell be used for defining in all species the islet cell that contains pancreatic polypeptide.

Published
1978
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43. Characterization of specific pancreatic polypeptide receptors on basolateral membranes of the canine small intestine.

Author

Gilbert, W R, Frank, B H, Gavin, J R, and Gingerich, R L

Abstract

We have identified specific binding sites for pancreatic polypeptide (PP) on the mucosal lining of canine small intestine. The present study was undertaken to further characterize these binding sites (receptors) on purified intestinal membranes and to establish their location on the brush border or basolateral surface of the intestinal enterocyte. Basolateral and brush border membranes were prepared by sorbitol density centrifugation. PP receptors were localized predominantly to the vascular surface, and thus binding of PP 125I-labeled on Tyr-27 to the basolateral preparation was used to evaluate receptor characteristics. Binding of PP was calcium, time, temperature, and pH dependent. Maximum specific binding of labeled PP occurred after an 8-hr incubation at 4 degrees C with 5 mM calcium at pH 6.8. Data analysis by Scatchard plot showed high- and low-affinity binding sites with relative affinities of 1.5 x 10(-9) M and 2.6 x 10(-8) M and with corresponding binding capacities of 0.23 pmol/mg and 0.84 pmol/mg of protein, respectively. This receptor was specific for PP since peptide YY and neuropeptide Y, peptides of the PP family, cross-reacted by less than 3%, as judged from comparisons of half-maximal displacement of label. Structurally dissimilar peptides, insulin and glucagon, did not compete for binding. Specific 125I-labeled PP binding was localized primarily to basolateral membranes (9.8 +/- 0.8%) with little binding by brush border membranes (0.8 +/- 0.2%). Thus, we have identified highly specific receptors for PP, located predominantly on the vascular surface of the small intestinal mucosa. These data suggest that the mucosal lining of the small intestine is a target tissue for PP and that PP participates in the hormonal regulation of fuel metabolism and substrate transport in the small intestinal mucosa.

Published
1988
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