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Metabolic function of hepatic hexokinase in perch, Perca fluviatilis
Author(s) -
Borrebaek B,
Christophersen B,
Sundby A
Publication year - 2003
Publication title -
aquaculture research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.646
H-Index - 89
eISSN - 1365-2109
pISSN - 1355-557X
DOI - 10.1046/j.1365-2109.2003.00809.x
Subject(s) - hexokinase , biology , glycogen , perch , glucokinase , medicine , endocrinology , malic enzyme , carbohydrate , insulin , enzyme , biochemistry , dehydrogenase , metabolism , glycolysis , fish <actinopterygii> , fishery
Feeding previously fasted perch with a carbohydrate‐rich pelleted diet resulted in a rapid transient insulin response followed by a transient increase in the activity of the hepatic low‐affinity hexokinase (glucokinase, GK). The activity of the high‐affinity hexokinase (hexokinase, HK) increased more slowly and steadily to about seven times the fasting value on the 10th day after start of feeding, in parallel with an increase in the hepatic glycogen content. An insulin response was also observed when fasted perch were fed a diet consisting of boiled fillet of cod (a high‐protein, very low‐fat and practically carbohydrate‐free diet). In this case no GK activity was observed, whereas the glycogen content increased steadily from the start of feeding to about the same level as when fish were given the carbohydrate‐rich diet. There was a delayed increase in the activity of HK, starting on about the sixth day (after the glycogen stores were filled), concomitant with increased activities of lipogenic enzymes (glucose‐6‐phosphate dehydrogenase, ATP citrate lyase and malic enzyme). The results are in line with the hypothesis that the mitochondria‐bound hepatic HK has a particular anabolic function in glycogen and fat synthesis.