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Regular Article |
2,a
ab
a Unit of Molecular Toxicology and
b Unit of Mineral Metabolism, Institute for Medical Research and Occupational Health, 10001 Zagreb, Croatia
c BioCurrents Research Center, Marine Biology Laboratory, Woods Hole, Massachusetts 02543
d Renal Unit and Program in Membrane Biology, Massachusetts General Hospital, Charlestown, Massachusetts 02129
e Departments of Pathology and
f Medicine, Harvard Medical School, Boston, Massachusetts 02215
ABSTRACT
In rats, an acidic luminal pH maintains sperm quiescence during storage in the epididymis. We recently showed that vacuolar H+ATPase-rich cells in the epididymis and vas deferens are involved in the acidification of these segments. Treatment of rats with cadmium (Cd) leads to alkalinization of this fluid by an unknown mechanism. Because Cd may affect H+ATPase function, we examined 1) the in vivo effect of Cd poisoning on H+ATPase-rich cell morphology and on the abundance and distribution of the 31-kDa H+ATPase subunit in cells along the rat epididymis, and 2) the in vitro effect of Cd on H+ATPase activity and function in the isolated vas deferens. Immunofluorescence and immunoblotting data from rats treated with Cd for 14–15 days (2 mg Cd/kg body mass/day) showed that 1) H+ATPase-positive cells regressed to a prepubertal phenotype, and 2) H+ATPase was lost from the apical pole of the cell and was redistributed into an intracellular compartment. In experiments in vitro, Cd inhibited bafilomycin-sensitive ATPase activity in isolated total cell membranes and, as measured using a proton-selective extracellular microelectrode, inhibited proton secretion in isolated vas deferens. We conclude that alkalinization of the tubule fluid in the epididymis and vas deferens of Cd-treated rats may result from the loss of functional H+ATPase enzyme in the cell apical domain as well as from a direct inhibition of H+ATPase function by Cd.
1 This work was supported by grants 0022111 (C.M.H.K.) and 00220101 (I.S.) from the Croatian Ministry of Science and Technology, by a Fogarty International Research Collaborative Award 1-R03-TW01057-01 (I.S. and D.B.), and by NIH grant DK 38452 (D.B. and S.B.). S.B. was partially supported by a Claflin Distinguished Scholar Award from the Massachusetts General Hospital.
2 Correspondence: Ivan Saboli, Unit of Molecular Toxicology, Institute for Medical Research and Occupational Health, Ksaverska cesta 2, P.O. Box 291, 10001 Zagreb, Croatia. FAX: 385 1 4673-303; sabolic{at}mimi.imi.hr
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