Recombinant interleukin 1 suppresses lipoprotein lipase activity in 3T3-L1 cells

J Immunol. 1985 Dec;135(6):3969-71.

Abstract

Recombinant murine interleukin 1 (rIL 1) inhibits 3T3-L1 cell expression of lipoprotein lipase (LPL) activity when present in exceedingly dilute concentration (less than 10(-15) M). The extreme sensitivity of the adipocyte system to rIL 1 far exceeds that of the standard lymphocyte-activating factor assay. However, enzyme suppression is incomplete; even at micromolar concentrations, rIL 1 causes only about a 50% reduction in LPL activity. By contrast, cachectin (tumor necrosis factor) achieves nearly complete LPL suppression at subnanomolar concentrations. Concentrated solutions of rIL 1 are incapable of competing with radiolabeled cachectin for binding sites on 3T3-L1 cells. rIL 1-induced LPL suppression is abolished by the addition of a specific IL 1 neutralizing antiserum to the assay system. rIL 1 appears capable of influencing adipocyte expression of LPL, but apparently acts through a different mechanism than cachectin/TNF.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adipose Tissue / cytology
  • Adipose Tissue / enzymology*
  • Adipose Tissue / metabolism
  • Animals
  • Binding, Competitive
  • Cell Line
  • Glycoproteins / metabolism
  • Immune Sera / pharmacology
  • Interleukin-1 / immunology
  • Interleukin-1 / physiology*
  • Lipoprotein Lipase / antagonists & inhibitors*
  • Lipoprotein Lipase / metabolism
  • Mice
  • Proteins / metabolism
  • Receptors, Cell Surface / metabolism
  • Receptors, Lipoprotein
  • Recombinant Proteins / physiology*
  • Tumor Necrosis Factor-alpha

Substances

  • Glycoproteins
  • Immune Sera
  • Interleukin-1
  • Proteins
  • Receptors, Cell Surface
  • Receptors, Lipoprotein
  • Recombinant Proteins
  • Tumor Necrosis Factor-alpha
  • Lipoprotein Lipase