NHE3 activity and trafficking depend on the state of actin organization in proximal tubule

The present study was addressed to define the contribution of cytoskeleton elements in the kidney proximal tubule Na+/H+ exchanger 3 (NHE3) activity under basal conditions. We used luminal membrane vesicles (LMV) isolated from suspensions of rat cortical tubules pretreated with either colchicine (Co...

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Bibliographic Details
Published in:American journal of physiology. Renal physiology 2001-02, Vol.280 (2), p.F283-F290
Main Authors: Chalumeau, C, du Cheyron, D, Defontaine, N, Kellermann, O, Paillard, M, Poggioli, J
Format: Article
Language:English
Subjects:
Actins - drug effects
Actins - metabolism
Animals
Colchicine - pharmacology
Cytochalasin D - pharmacology
Cytoskeleton - drug effects
Cytoskeleton - metabolism
Gout Suppressants - pharmacology
Kidney Cortex - cytology
Kidney Cortex - drug effects
Kidney Cortex - metabolism
Kidney Tubules, Proximal - drug effects
Kidney Tubules, Proximal - metabolism
Mice
Microtubules - drug effects
Microtubules - metabolism
Nucleic Acid Synthesis Inhibitors - pharmacology
Rats
Sodium-Hydrogen Exchanger 3
Sodium-Hydrogen Exchangers - drug effects
Sodium-Hydrogen Exchangers - metabolism
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Summary:The present study was addressed to define the contribution of cytoskeleton elements in the kidney proximal tubule Na+/H+ exchanger 3 (NHE3) activity under basal conditions. We used luminal membrane vesicles (LMV) isolated from suspensions of rat cortical tubules pretreated with either colchicine (Colch) or cytochalasin D (Cyto D). Colch pretreatment of suspensions (200 microM for 60 min) moderately decreased LMV NHE3 activity. Cyto D pretreatment (1 microM for 60 min) elicited an increase in LMV NHE3 transport activity but did not increase Na-glucose cotransport activity. Cyto D pretreatment of suspensions did not change the apparent affinity of NHE3 for internal H+. In contrast, after Cyto D pretreatment of the suspensions, NHE3 protein abundance was increased in LMV and remained unchanged in cortical cell homogenates. The effect of Cyto D on NHE3 was further assessed with cultures of murine cortical cells. The amount of surface biotinylated NHE3 increased on Cyto D treatment, whereas NHE3 protein abundance was unchanged in cell homogenates. In conclusion, under basal conditions NHE3 activity depends on the state of actin organization possibly involved in trafficking processes between luminal membrane and intracellular compartment.
ISSN:1931-857X
1522-1466
DOI:10.1152/ajprenal.2001.280.2.f283