Hepatic zonation of insulin‐stimulated tyrosine phosphorylation

FEBS Letters

Quistorff, Bjørn²  Bianchi, Antonella¹  Witters, Lee A.¹ 

[1] Endocrine-Metabolism Division, Departments of Medicine and Biochemistry, Dartmouth Medical School, Hanover, NH 03756, USA;Department of Biochemistry A, The Panum Institute, University of Copenhagen, DK-2200, Copenhagen N, Denmark

关键词: Tyrosine phosphorylation;    Insulin receptor;    Hepatic zonation;    Acetyl-CoA carboxylase;   

DOI  :  10.1016/0014-5793(90)81210-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Zonal distribution of insulin stimulation of hepatic protein tyrosine phosphorylation, detected by immunoblotting with an anti-phosphotyrosine antibody, has been studied in the in situ perfused rat liver by dual-digitonin-pulse perfusion. Insulin promotes the rapid and sustained tyrosine phosphorylation of two proteins (pp150 and pp69) that are present only in the perivenous hepatocytes, while three others (pp46, pp48 and pp96) are stimulated identically in the periportal and perivenous cells. The ability of insulin to rapidly activate acetyl-CoA carboxylase is indistinguishable between the hepatic zones. Hepatic zonation of insulin-stimulated tyrosine phosphorylation could underly differential hepatic insulin responses and might provide clues to the identification of tyrosine phosphorylated proteins linked to insulin regulation of intracellular events.

【 授权许可】

Unknown