Leptin induces tyrosine phosphorylation of cellular proteins including STAT-1 in human renal adenocarcinoma cells, ACHN

Biochem Biophys Res Commun. 1996 Nov 21;228(3):859-64. doi: 10.1006/bbrc.1996.1744.

Abstract

Several lines of evidence from in vivo animal experiments and human studies suggest that leptin, a peptide secreted from adipose tissue, plays a role in regulating food intake and energy expenditure. However, the signal transduction mechanism of leptin in its target cells remains unknown thus far since leptin-responsive cell lines have not been available yet. We found that leptin caused the tyrosine phosphorylation of several proteins in human renal cell carcinoma cells, ACHN cells, in which STAT-1, but neither STAT-3 nor STAT-5, was involved. An ACHN cell line would serve as a useful tool for analyzing the signal transduction mechanism of leptin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenocarcinoma / metabolism*
  • Adenocarcinoma / pathology
  • Blotting, Western
  • DNA-Binding Proteins / metabolism*
  • Humans
  • Kidney Neoplasms / metabolism*
  • Kidney Neoplasms / pathology
  • Leptin
  • Obesity / metabolism
  • Phosphorylation
  • Proteins / metabolism*
  • Recombinant Proteins / metabolism
  • STAT1 Transcription Factor
  • Trans-Activators / metabolism*
  • Tumor Cells, Cultured
  • Tyrosine / metabolism*

Substances

  • DNA-Binding Proteins
  • Leptin
  • Proteins
  • Recombinant Proteins
  • STAT1 Transcription Factor
  • STAT1 protein, human
  • Trans-Activators
  • Tyrosine