Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture

Yasser Abdel-Wahab, Finbarr O'Harte, CR Barnett, Peter Flatt

Research output: Contribution to journal › Article

36 Citations (Scopus)

Abstract

Characteristics of cellular insulin glycation were examined in the pancreatic B-cell line, BRIN-BD11. The extent of insulin glycation increased stepwise during 72 h of culture at 5.6-33.3 mmol/l glucose, attaining levels up to 27%. Glycation of insulin at 33.3 mmol/l glucose was rapid, reaching maximal values within 2 h, and not readily reversible during 2 to 24 h of subsequent exposure to 5.6 mmol/l glucose. Glycated insulin was readily secreted by BRIN-BD11 cells upon active stimulation with glucose and other secretagogues. Cellular insulin glycation was decreased by 66-80% by inhibitors of protein glycation, vitamin C, aminoguanidine or acetylsalicylic acid. Modulation of insulin-secretory activity of BRIN-BD11 cells by co-culture at high glucose with diazoxide, L-alanine or glibenclamide indicated that long-term stimulation of secretion was associated with a decrease in the extent of insulin glycation. Glycation of insulin in vitro was substantially less extensive than in BRIN-BD11 cells, although glucose-6-phosphate and glyceraldehyde-3-phosphate were 1.4- to 2.0-fold more reactive than glucose per se. These observations indicate that insulin is readily glycated and secreted from insulin-secreting cells under hyperglycaemic conditions in culture.
LanguageEnglish
Pages59-67
JournalJournal of Endrocrinology
Volume152
Issue number1
Publication statusPublished - Jan 1997

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Insulin-Secreting Cells
Insulin
Glucose
Glyceraldehyde 3-Phosphate
Diazoxide
Glucose-6-Phosphate
Glyburide
Coculture Techniques
Alanine
Aspirin
Ascorbic Acid
Cell Culture Techniques
Cell Line

Cite this

Abdel-Wahab, Yasser ; O'Harte, Finbarr ; Barnett, CR ; Flatt, Peter. / Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture. In: Journal of Endrocrinology. 1997 ; Vol. 152, No. 1. pp. 59-67.
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abstract = "Characteristics of cellular insulin glycation were examined in the pancreatic B-cell line, BRIN-BD11. The extent of insulin glycation increased stepwise during 72 h of culture at 5.6-33.3 mmol/l glucose, attaining levels up to 27{\%}. Glycation of insulin at 33.3 mmol/l glucose was rapid, reaching maximal values within 2 h, and not readily reversible during 2 to 24 h of subsequent exposure to 5.6 mmol/l glucose. Glycated insulin was readily secreted by BRIN-BD11 cells upon active stimulation with glucose and other secretagogues. Cellular insulin glycation was decreased by 66-80{\%} by inhibitors of protein glycation, vitamin C, aminoguanidine or acetylsalicylic acid. Modulation of insulin-secretory activity of BRIN-BD11 cells by co-culture at high glucose with diazoxide, L-alanine or glibenclamide indicated that long-term stimulation of secretion was associated with a decrease in the extent of insulin glycation. Glycation of insulin in vitro was substantially less extensive than in BRIN-BD11 cells, although glucose-6-phosphate and glyceraldehyde-3-phosphate were 1.4- to 2.0-fold more reactive than glucose per se. These observations indicate that insulin is readily glycated and secreted from insulin-secreting cells under hyperglycaemic conditions in culture.",
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Abdel-Wahab, Y, O'Harte, F, Barnett, CR & Flatt, P 1997, 'Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture', Journal of Endrocrinology, vol. 152, no. 1, pp. 59-67.

Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture. / Abdel-Wahab, Yasser; O'Harte, Finbarr; Barnett, CR; Flatt, Peter.

In: Journal of Endrocrinology, Vol. 152, No. 1, 01.1997, p. 59-67.

Research output: Contribution to journal › Article

TY - JOUR

T1 - Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture

AU - Abdel-Wahab, Yasser

AU - O'Harte, Finbarr

AU - Barnett, CR

AU - Flatt, Peter

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N2 - Characteristics of cellular insulin glycation were examined in the pancreatic B-cell line, BRIN-BD11. The extent of insulin glycation increased stepwise during 72 h of culture at 5.6-33.3 mmol/l glucose, attaining levels up to 27%. Glycation of insulin at 33.3 mmol/l glucose was rapid, reaching maximal values within 2 h, and not readily reversible during 2 to 24 h of subsequent exposure to 5.6 mmol/l glucose. Glycated insulin was readily secreted by BRIN-BD11 cells upon active stimulation with glucose and other secretagogues. Cellular insulin glycation was decreased by 66-80% by inhibitors of protein glycation, vitamin C, aminoguanidine or acetylsalicylic acid. Modulation of insulin-secretory activity of BRIN-BD11 cells by co-culture at high glucose with diazoxide, L-alanine or glibenclamide indicated that long-term stimulation of secretion was associated with a decrease in the extent of insulin glycation. Glycation of insulin in vitro was substantially less extensive than in BRIN-BD11 cells, although glucose-6-phosphate and glyceraldehyde-3-phosphate were 1.4- to 2.0-fold more reactive than glucose per se. These observations indicate that insulin is readily glycated and secreted from insulin-secreting cells under hyperglycaemic conditions in culture.

AB - Characteristics of cellular insulin glycation were examined in the pancreatic B-cell line, BRIN-BD11. The extent of insulin glycation increased stepwise during 72 h of culture at 5.6-33.3 mmol/l glucose, attaining levels up to 27%. Glycation of insulin at 33.3 mmol/l glucose was rapid, reaching maximal values within 2 h, and not readily reversible during 2 to 24 h of subsequent exposure to 5.6 mmol/l glucose. Glycated insulin was readily secreted by BRIN-BD11 cells upon active stimulation with glucose and other secretagogues. Cellular insulin glycation was decreased by 66-80% by inhibitors of protein glycation, vitamin C, aminoguanidine or acetylsalicylic acid. Modulation of insulin-secretory activity of BRIN-BD11 cells by co-culture at high glucose with diazoxide, L-alanine or glibenclamide indicated that long-term stimulation of secretion was associated with a decrease in the extent of insulin glycation. Glycation of insulin in vitro was substantially less extensive than in BRIN-BD11 cells, although glucose-6-phosphate and glyceraldehyde-3-phosphate were 1.4- to 2.0-fold more reactive than glucose per se. These observations indicate that insulin is readily glycated and secreted from insulin-secreting cells under hyperglycaemic conditions in culture.

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Abdel-Wahab Y, O'Harte F, Barnett CR, Flatt P. Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture. Journal of Endrocrinology. 1997 Jan;152(1):59-67.