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First published online September 14, 2007
Journal of Experimental Biology 210, 3494-3504 (2007)
Published by The Company of Biologists 2007
doi: 10.1242/jeb.007146
Regulation of glycogen metabolism in gills and liver of the euryhaline tilapia (Oreochromis mossambicus) during acclimation to seawater
1 Institute of Cellular and Organismic Biology, Academia Sinica, Nankang,
Taipei, Taiwan, Republic of China
2 Department of Aquatic Biosciences, National Chiayi University, Chiayi,
Taiwan, Republic of China
3 Institute of Zoology, National Taiwan University, Taipei, Taiwan, Republic
of China
4 Department of Hard Tissue Engineering, Tokyo Medical and Dental
University, Tokyo, Japan
* Author for correspondence (e-mail: pphwang{at}gate.sinica.edu.tw)
Accepted 18 June 2007
Glucose, which plays a central role in providing energy for metabolism, is
primarily stored as glycogen. The synthesis and degradation of glycogen are
mainly initialized by glycogen synthase (GS) and glycogen phosphorylase (GP),
respectively. The present study aimed to examine the glycogen metabolism in
fish liver and gills during acute exposure to seawater. In tilapia
(Oreochromis mossambicus) gill, GP, GS and glycogen were
immunocytochemically colocalized in a specific group of glycogen-rich (GR)
cells, which are adjacent to the gill's main ionocytes, mitochondrion-rich
(MR) cells. Na+/K+-ATPase activity in the gills, protein
expression and/or activity of GP and GS and the glycogen content of the gills
and liver were examined in tilapia after their acute transfer from freshwater
(FW) to 25
seawater (SW). Gill Na+/K+-ATPase
activity rapidly increased immediately after SW transfer. Glycogen content in
both the gills and liver were significantly depleted after SW transfer, but
the depletion occurred earlier in gills than in the liver. Gill GP activity
and protein expression were upregulated 1–3 h post-transfer and
eventually recovered to the normal level as determined in the control group.
At the same time, GS protein expression was downregulated. Similar changes in
liver GP and GS protein expression were also observed but they occurred later
at 6–12 h post-transfer. In conclusion, GR cells are initially
stimulated to provide prompt energy for neighboring MR cells that trigger
ion-secretion mechanisms. Several hours later, the liver begins to degrade its
glycogen stores for the subsequent energy supply.
Key words: glycogen phosphorylase, glycogen synthase, Na+/K+-ATPase, osmoregulation, mitochondrion-rich cells, salinity