Phosphorylation of the 26 kDa TNF precursor in monocytic cells and in transfected HeLa cells

E. Pocsik, E. Duda, D. Wallach

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Tumor necrosis factor (TNF) functions both as a soluble molecule and as a cell surface 26 kDa transmembrane protein, from which the soluble form is proteolytically derived. The 26 kDa TNF molecules isolated from 32P labeled HeLa cells that had been transfected with the cDNA of a partially clearable TNF mutant were found labeled. Phosphorylated 26 kDa TNF molecules could also be isolated from human LPS stimulated monocytic Mono Mac 6. Phosphoaminoacid analysis revealed that the labeled phosphate is bound to serine residues. No label was found incorporated in soluble 17 kDa TNF, indicating that the phosphorylated residue(s) of membrane-associated TNF occur in the cytoplasmic portion of the molecule. Phosphorylation of the intracellular domain of the 26 kDa TNF molecules may play a role in the regulation of expression or proteolytic processing of TNF, modulate TNF bioactivity, or take part in intracellular signaling by cell-surface TNF.

Original languageEnglish
Pages (from-to)152-160
Number of pages9
JournalJournal of Inflammation
Volume45
Issue number3
Publication statusPublished - 1995

Fingerprint

HeLa Cells
Tumor Necrosis Factor-alpha
Phosphorylation
tumor necrosis factor precursor
Serine
Complementary DNA
Phosphates
Membranes

Keywords

  • cytokines
  • macrophages
  • membrane
  • shedding
  • signaling

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine

Cite this

Phosphorylation of the 26 kDa TNF precursor in monocytic cells and in transfected HeLa cells. / Pocsik, E.; Duda, E.; Wallach, D.

In: Journal of Inflammation, Vol. 45, No. 3, 1995, p. 152-160.

Research output: Contribution to journalArticle

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