Leptin induces tyrosine phosphorylation of cellular proteins including STAT-1 in human renal adenocarcinoma cells, ACHN.
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.
Takahashi
Y
Y
Department of Medicine, Kobe University School of Medicine, Japan.
Okimura
Y
Y
Mizuno
I
I
Takahashi
T
T
Kaji
H
H
Uchiyama
T
T
Abe
H
H
Chihara
K
K
D000230:Adenocarcinoma / Q000378:metabolism* / Q000473:pathology; D015153:Blotting, Western; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006801:Humans; D007680:Kidney Neoplasms / Q000378:metabolism* / Q000473:pathology; D020738:Leptin; D009765:Obesity / Q000378:metabolism; D010766:Phosphorylation; D011506:Proteins / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D050794:STAT1 Transcription Factor; D015534:Trans-Activators / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D014443:Tyrosine / Q000378:metabolism*
D004268:DNA-Binding Proteins; D020738:Leptin; D011506:Proteins; D011994:Recombinant Proteins; D050794:STAT1 Transcription Factor; C494079:STAT1 protein, human; D015534:Trans-Activators; D014443:Tyrosine