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

B. A. Beutler, A. Cerami

Research output: Contribution to journalArticle

174 Scopus citations

Abstract

Recombinant murine interleukin 1 (rIL 1) inhibits 3T3-L1 cell expression of lipoprotein lipase (LPL) activity when present in exceedingly dilute concentration (<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 (tumour 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.

Original languageEnglish (US)
Pages (from-to)3969-3971
Number of pages3
JournalJournal of Immunology
Volume135
Issue number6
StatePublished - Dec 1 1985

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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