NDLI: Sodium dependent ion transporters in trout gills

Content Provider	Springer Nature Link
Author	Flik, G. Kaneko, T. Greco, A.M. Li, J. Fenwick, J.C.
Copyright Year	1997
Abstract	Biochemical procedures developed to isolate plasma membranes from the branchial epithelium of rainbow trout (Oncorhynchus mykiss) yield membrane fractions that are specifically enriched in the plasma membrane marker enzyme Na+/K+-ATPase. As the bulk of the branchial Na+/K+-ATPase is assumed to be confined to the mitochondria-rich chloride cells, such membrane preparations must contain the essence of the enzymatic machinery of the chloride cells. Basal Na+ activity in branchial (chloride) cells is around 10 millimolar and, accordingly, we find a Km for Na+ of the Na+/K+-ATPase of 13 millimolar, indicating that the enzyme may be regulated by changes in cytosolic sodium. The Na+-gradient across the serosal plasma membrane created by this pump provides energy for 3Na+/Ca2+-exchange and bumetanide-sensitive Na+/K+/2Cl--cotransport. Here we further postulate the presence of a Na+/Cl--cotransporter, indicated by thiazide-sensitive, bumetanide-insensitive transport of Na+ and Cl-; this cotransporter activity awaits the characterization of its kinetics. The Na+/Ca2+-exchanger has kinetic characteristics compatible with a regulatory role of cytosolic Na+ in the activity of this carrier. Both Na+/Ca2+-exchange and Ca2+-ATPase activity may contribute to transport of Ca2+, the former having lower affinity for calcium but a higher capacity than the latter carrier. The Na+/K+/2Cl--cotransporter has kinetics that favor a regulatory role for plasma K+ in the activity of this carrier. Seawater adaptation leads to increased activity of cotransporter molecules in the plasma membrane fractions (the activity increases relative to that of the Na+/K+-ATPase) and this may reflect a function in Cl--extrusion performed by the chloride cells in a seawater environment. A function for the cotransporter in the gills of freshwater fish may be the regulation of cell volume.
Starting Page	385
Ending Page	396
Page Count	12
File Format	PDF
ISSN	09201742
Journal	Fish Physiology and Biochemistry
Volume Number	17
Issue Number	1-6
e-ISSN	15735168
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1997-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Animal Biochemistry Hydrobiology Zoology Animal Anatomy / Morphology / Histology Animal Physiology
Content Type	Text
Resource Type	Article
Subject	Physiology Medicine Biochemistry Aquatic Science

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