Endogenous glucagon-cells are necessary for the glucose-responsiveness of the HIT-T15 hamster β-cell line
type: CreativeWork
description: The role of glucagon in glucose-stimulated insulin release was investigated using the hamster insulinoma cell line, HIT-T15, as a model of the pancreatic β-cell. Glucose-stimulated insulin release from HIT-T15 cells was concentration-dependent over a range of glucose concentrations between 0 and 15 mM, with immunoreactive-insulin release (IRI) rising significantly above the basal level (zero glucose) when cells were exposed to glucose concentrations of 5, 10 and 15 mM (p < 0.02). Minimum (zero glucose) and maximum (15 mM glucose) insulin release was 1.6 ± 0.5 % and 12.0 ± 2.9 % of total cell content (TCC), respectively. In HIT-T15 cells, glucagon secretion was 5-9 % of total cell content during a 1 h release experiment. There was no significant difference between glucagon released in the presence of zero- or high (15 mM)-glucose. The addition of a glucagon antibody completely abolished glucose-stimulated insulin release, while antibodies raised against somatostatin and glucose-dependent insulinotropic polypeptide (GIP) had no effect. When HIT-T15 cells were incubated in conditions of zero-glucose and glucose plus glucagon-Ab there was no significant difference in insulin release (p >0.05). Furthermore, glucagon-Ab inhibited glucose-stimulated insulin secretion over the full range of glucose responsiveness (5 to 15 mM; p < 0.03). The abolition of glucose-stimulated insulin secretion by an antibody to glucagon indicates that glucose-stimulated insulin secretion is dependent on glucagon, probably acting via a receptor-dependent pathway. HIT-T15 cells that were co-cultured with glucagon producing InR1-G9 cells, displayed basal insulin release that was elevated, with an absence of glucose potentiation. HIT-T15 cells were immunoperoxidase stained for the following peptide hormones: insulin, somatostatin, glucagon, glucagon-like polypeptide-I, GIP, secretin, pancreatic polypeptide (PP) and peptide-tyrosine-tyrosine (PYY). Staining was positive for all peptide hormones test…
abstract: The role of glucagon in glucose-stimulated insulin release was investigated using the hamster insulinoma cell line, HIT-T15, as a model of the pancreatic β-cell. Glucose-stimulated insulin release from HIT-T15 cells was concentration-dependent over a range of glucose concentrations between 0 and 15 mM, with immunoreactive-insulin release (IRI) rising significantly above the basal level (zero glucose) when cells were exposed to glucose concentrations of 5, 10 and 15 mM (p < 0.02). Minimum (zero glucose) and maximum (15 mM glucose) insulin release was 1.6 ± 0.5 % and 12.0 ± 2.9 % of total cell content (TCC), respectively. In HIT-T15 cells, glucagon secretion was 5-9 % of total cell content during a 1 h release experiment. There was no significant difference between glucagon released in the presence of zero- or high (15 mM)-glucose. The addition of a glucagon antibody completely abolished glucose-stimulated insulin release, while antibodies raised against somatostatin and glucose-dependent insulinotropic polypeptide (GIP) had no effect. When HIT-T15 cells were incubated in conditions of zero-glucose and glucose plus glucagon-Ab there was no significant difference in insulin release (p >0.05). Furthermore, glucagon-Ab inhibited glucose-stimulated insulin secretion over the full range of glucose responsiveness (5 to 15 mM; p < 0.03). The abolition of glucose-stimulated insulin secretion by an antibody to glucagon indicates that glucose-stimulated insulin secretion is dependent on glucagon, probably acting via a receptor-dependent pathway. HIT-T15 cells that were co-cultured with glucagon producing InR1-G9 cells, displayed basal insulin release that was elevated, with an absence of glucose potentiation. HIT-T15 cells were immunoperoxidase stained for the following peptide hormones: insulin, somatostatin, glucagon, glucagon-like polypeptide-I, GIP, secretin, pancreatic polypeptide (PP) and peptide-tyrosine-tyrosine (PYY). Staining was positive for all peptide hormones test…
author: Väänänen, Jeffrey Eric
language: eng
date published: 1993
date modified: 2026-07-24T05:07:26Z
provider: University of British Columbia
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of British Columbia

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2429/1513