Modulation of neuronal pentraxin 1 expression in rat pancreatic β-cells submitted to chronic glucotoxic stress

Mol Cell Proteomics. 2012 Aug;11(8):244-54. doi: 10.1074/mcp.M112.018051. Epub 2012 Mar 16.

Abstract

Insulin secretory granules are β-cell vesicles dedicated to insulin processing, storage, and release. The secretion of insulin secretory granule content in response to an acute increase of glucose concentration is a highly regulated process allowing normal glycemic homeostasis. Type 2 diabetes is a metabolic disease characterized by chronic hyperglycemia. The consequent prolonged glucose exposure is known to exert deleterious effects on the function of various organs, notably impairment of insulin secretion by pancreatic β-cells and induction of apoptosis. It has also been described as modifying gene and protein expression in β-cells. Therefore, we hypothesized that a modulation of insulin secretory granule protein expression induced by chronic hyperglycemia may partially explain β-cell dysfunction. To identify the potential early molecular mechanisms underlying β-cell dysfunction during chronic hyperglycemia, we performed SILAC and mass spectrometry experiments to monitor changes in the insulin secretory granule proteome from INS-1E rat insulinoma β-cells cultivated either with 11 or 30 mm of glucose for 24 h. Fourteen proteins were found to be differentially expressed between these two conditions, and several of these proteins were not described before to be present in β-cells. Among them, neuronal pentraxin 1 was only described in neurons so far. Here we investigated its expression and intracellular localization in INS-1E cells. Furthermore, its overexpression in glucotoxic conditions was confirmed at the mRNA and protein levels. According to its role in hypoxia-ischemia-induced apoptosis described in neurons, this suggests that neuronal pentraxin 1 might be a new β-cell mediator in the AKT/GSK3 apoptotic pathway. In conclusion, the modification of specific β-cell pathways such as apoptosis and oxidative stress may partially explain the impairment of insulin secretion and β-cell failure, observed after prolonged exposure to high glucose concentrations.

MeSH terms

  • Animals
  • Blotting, Western
  • C-Reactive Protein / genetics
  • C-Reactive Protein / metabolism*
  • Cell Line, Tumor
  • Gene Expression / drug effects
  • Gene Expression Profiling / methods
  • Glucose / pharmacology
  • Glycogen Synthase Kinase 3 / antagonists & inhibitors
  • Glycogen Synthase Kinase 3 / metabolism
  • Hyperglycemia / genetics
  • Hyperglycemia / metabolism
  • Immunohistochemistry
  • Insulin / metabolism
  • Insulin Secretion
  • Insulin-Secreting Cells / drug effects
  • Insulin-Secreting Cells / metabolism*
  • Insulin-Secreting Cells / pathology
  • Islets of Langerhans / drug effects
  • Islets of Langerhans / metabolism
  • Mass Spectrometry
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Proteome / genetics
  • Proteome / metabolism*
  • Proteomics / methods
  • Proto-Oncogene Proteins c-akt / metabolism
  • Pyridines / pharmacology
  • Pyrimidines / pharmacology
  • Rats
  • Reverse Transcriptase Polymerase Chain Reaction
  • Secretory Vesicles / drug effects
  • Secretory Vesicles / metabolism*
  • Signal Transduction / drug effects
  • Time Factors

Substances

  • Chir 99021
  • Insulin
  • Nerve Tissue Proteins
  • Proteome
  • Pyridines
  • Pyrimidines
  • neuronal pentraxin
  • C-Reactive Protein
  • Proto-Oncogene Proteins c-akt
  • Glycogen Synthase Kinase 3
  • Glucose