Molecular identification of the human tumor necrosis factor receptor on interleukin-2-stimulated peripheral blood lymphocytes

William L. Crump, Laurie B. Owen-Schaub, Elizabeth Ann Grimm

Research output: Contribution to journalArticlepeer-review

Abstract

The human tumor necrosis factor (TNF) receptor on interleukin (IL)-2-stimulated lymphocytes was characterized by binding and crosslinking techniques. The TNF receptor on IL-2-activated lymphocytes has an affinity of approximately 50 pm. Conventional crosslinking studies with the DSS analog bis(sulfosuccinimidyl) suberate demonstrated a ligand-receptor complex molecular weight of 106-108 kDa. Lectin precipitation experiments indicated that the receptor is a glycoprotein with an affinity for lectin isolated from Ricinus communis. Affinity crosslinking studies with the iodinateable, cleavable crosslinker sulfosuccinimidyl 2-(p-azido-salicylamido) ethyl 1,3′-dithiopropionate demonstrated that the TNF receptor, by itself, in the absence of bound ligand, has a molecular weight of approximately 90 kDa. Furthermore, these results indicate that the crosslinked TNF:TNF-receptor complexes observed at 104-108 kDa are composed of receptor and monomeric TNF.

Original languageEnglish (US)
Pages (from-to)150-158
Number of pages9
JournalCellular Immunology
Volume131
Issue number1
DOIs
StatePublished - Nov 1990

ASJC Scopus subject areas

  • Immunology

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