Interaction of interleukin-1 with islet beta-cells. Distinction between indirect, aspecific cytotoxicity and direct, specific functional suppression

Diabetes. 1993 Jan;42(1):56-65. doi: 10.2337/diab.42.1.56.

Abstract

A 5-day culture of adult rat islets with human recombinant IL-1 beta (3 U/ml) resulted in the death of most alpha-cells and 50% of beta-cells. The IL-1--exposed islet tissue contained--in addition to poorly granulated beta-cells--patches of outgrowing monolayers and dispersed activated macrophages. In purified alpha- and beta-cell preparations, no cytodestructive effects of IL-1 (as high as 30 U/ml) were noticed, indicating that the cytokine is in itself not a beta-cell--selective killer. Pure beta-cells were, on the other hand, more sensitive (from 0.3 U/ml on) than intact islets to an IL-1--induced suppression of hormone synthesis. This inhibitory action was reversible and affected predominantly the production of insulin, leading to degranulated cells with modified shape and attachment. Further studies with IL-1 should take into account that isolated islet preparations do not allow distinction between its irreversible, indirect, and aspecific beta-cell toxicity and its reversible, direct, and specific suppression of beta-cell functions. It is not yet known whether IL-1--suppressed beta-cells exhibit an altered sensitivity to beta-cell--toxic conditions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Aggregation / drug effects
  • Cell Survival / drug effects*
  • Cells, Cultured
  • Cytoplasmic Granules / drug effects
  • Cytoplasmic Granules / ultrastructure
  • Fluorescent Antibody Technique
  • Glucagon / metabolism
  • Insulin / biosynthesis
  • Insulin / metabolism
  • Interleukin-1 / pharmacology*
  • Islets of Langerhans / cytology
  • Islets of Langerhans / drug effects*
  • Islets of Langerhans / physiology
  • Male
  • Microscopy, Electron
  • Rats
  • Rats, Wistar
  • Recombinant Proteins / pharmacology

Substances

  • Insulin
  • Interleukin-1
  • Recombinant Proteins
  • Glucagon