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Glycerol transport and phosphorylation by rat hepatocytes
Author(s) -
Li ChienChung,
Lin E. C. C.
Publication year - 1983
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041170214
Subject(s) - phosphorylation , glycerol , microbiology and biotechnology , chemistry , hepatocyte , protein phosphorylation , biochemistry , biology , in vitro , protein kinase a
The entry of glycerol into isolated rat hepatocytes appears to be catalyzed by a specific carrier. At a physiological concentration of 0.1 mM, glycerol utilization is rate limited by the permeation step. Intracellular glycerol is trapped by an excess of glycerol kinase, which has a higher apparent affinity for the substrate than that of the membrane carrier. The entry of glycerol into the hepatocytes is highly sensitive to inhibition by monoacetin and cytochalasin B, but not by DL‐1,2‐propanediol, erythritol, D‐glucose, D‐galactose, D‐mannose, or D‐fructose.