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Journal of Experimental Biology, Vol 204, Issue 5 991-1002, Copyright © 2001 by Company of Biologists
JOURNAL ARTICLES |
RP Henry
Department of Biological Sciences, Auburn University, Auburn, AL 36849, USA. henryrp@mail.auburn.edu
The enzyme carbonic anhydrase appears to be a central molecular component in the suite of physiological and biochemical adaptations to low salinity found in euryhaline crustaceans. It is present in high activities in the organs responsible for osmotic and ionic regulation, the gills, and more specifically, the individual gills that are specialized for active ion uptake from dilute sea water. Within those gills carbonic anhydrase is distributed among different subcellular pools, the cytoplasm, mitochondria and microsomes. The cytoplasmic pool represents the largest subcellular fraction of carbonic anhydrase activity, and it is this fraction that undergoes a tenfold induction during acclimation to low salinity. Carbonic anhydrase activity is present in excess of that needed to support the general ion-transport processes, and so it is doubtful that carbonic anhydrase activity itself is a point of short-term regulation in response to salinity changes. Rather, upregulation of carbonic anhydrase appears to be a result of selective gene expression, representing a permanent response to long-term adaptation to low salinity. The exact signal that initiates the induction of carbonic anhydrase, and the pathway through which that signal is transduced to the activation of the carbonic anhydrase gene, are unknown, but two promising avenues of research exist. First, induction of carbonic anhydrase is immediately preceded by hemodilution and subsequent cell swelling, a potential initiating event in the process. Second, recent work indicates that expression of carbonic anhydrase is under the control of a repressor substance, located in the eyestalk, whose effect is removed upon exposure to low salinity.
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