QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

This Article Full Text (PDF) References Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kuppers, J. Articles by Bunse, I. Search for Related Content PubMed PubMed Citation Articles by Kuppers, J. Articles by Bunse, I. Social Bookmarking                         What's this?

Journal of Experimental Biology, Vol 199, Issue 6 1327-1334, Copyright © 1996 by Company of Biologists

JOURNAL ARTICLES

A primary cation transport by a V-type ATPase of low specificity

J. Kuppers and I. Bunse

The enzyme involved in outward K+ transport in insect epithelia belongs to the family of V-ATPases. Evidence has been reported relating the generation of the K+ gradient to a primary electrogenic proton transport via a distinct electrophoretic nH+/K+ antiport. The subject of this paper is the transport of K+ at a thread hair sensillum of the cockroach in situ. We recorded changes in the voltage and resistance of the ion-transporting membrane and of shifts in pH caused by inhibition of energy metabolism and by putative inhibitors of a proton/cation exchanger. The results are supplemented by previous determinations of the K+ activities in the same preparation. 1. In cockroach hair sensilla, the ion transport generates a membrane voltage of 105 mV. We found that the transport rendered the positive output compartment alkaline with respect to the cytoplasm by 1.0 pH unit compared with the pH at equilibrium distribution, and we infer that proton transport cannot be the process that energizes the generation of the K+ gradient. 2. The ion transport created an electrochemical potential difference for protons, DeltaetaH, of approximately 4.5 kJ mol-1, while the potential difference for K+, DeltaetaK, amounted to approximately 11 kJ mol-1. Both potential differences are directed to the cytosol. It follows from DeltaetaK/DeltaetaH that an antiport would have to be electrophoretic to drive K+ by DeltaetaH and it should, therefore, contribute to the membrane conductance. Amiloride and harmaline did not significantly change the pH in the adjacent spaces and did not affect the voltage or the resistance of the transporting membrane. Previous determinations of the impedance have shown that the ATP-independent conductance of this membrane is small, supporting the conclusion that it lacks an electrophoretic antiport. From these results, we deduce that K+ transport in cockroach sensilla is not secondary to a proton transport and an electrochemical proton gradient. The phenomena observed match the performance of a primary, electrogenic, cation-translocating ATPase of the type deduced from analyses of the short-circuit current at the midgut epithelium of lepidopteran larvae. The validity of the H+ transport/antiport hypothesis is discussed.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

				H. Onken, S. B. Moffett, and D. F. Moffett The transepithelial voltage of the isolated anterior stomach of mosquito larvae (Aedes aegypti): pharmacological characterization of the serotonin-stimulated cells J. Exp. Biol., May 1, 2004; 207(11): 1779 - 1787. [Abstract] [Full Text] [PDF]

				D. Boudko, L. Moroz, P. Linser, J. Trimarchi, P. Smith, and W. Harvey In situ analysis of pH gradients in mosquito larvae using non-invasive, self-referencing, pH-sensitive microelectrodes J. Exp. Biol., January 2, 2001; 204(4): 691 - 699. [Abstract] [PDF]