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Journal of Experimental Biology, Vol 106, Issue 1 91-117, Copyright © 1983 by Company of Biologists
JOURNAL ARTICLES |
WR Harvey, M Cioffi, JA Dow and MG Wolfersberger
K+ transport by the epithelia of midgut, salivary glands, Malpighian tubules, sensory sensilla, possibly rectum, and other organs of certain insects appears to use a unique K+ ATPase. Ouabain inhibition of transport-related events has not been demonstrated in these epithelia. The K+ pump is unlike the Na-K;ump but resembles the H;ump of phosphorylating membranes in its transport orientation, efficient thermodynamics, speculated two K+ per one MgATP2- stoichiometry, electrogenicity, and structure. Older electrochemical, tracer flux, and conductance evidence suggested that the K+ pump was on the apical plasma membrane of transporting cells in these epithelia. New X-ray microanalytical studies (XMA), reveal that the K+ concentration in all cells is more than 100 mM. Together with new microelectrode data these XMA results confirm the apical K+ pump location, resolve the K+ transport sport route, and suggest that the goblet cell cavity facilitates the generation of a large apical PD which may be used in nutrient absorption and pH regulation. K+ portasomes, which resemble F1-Fo ATPase particles, stud these K+ transporting apical membranes and are though to be the unit of active K+ transport. We have suggested a K+ transport mechanism in which two cations (2K+) are abandoned in an isolated domain of the portasomes during ATP2-hydrolysis and are repelled to the opposite membrane side via a K+ channel. Small peptides hydrolysed from the delta-endotoxin of Bacillus thuringiensis inhibit the K+ transport and may be useful as K+ pump inhibitors, apical membrane probes and insecticides. Goblet cell apical membrane fragments (GCAM) as well as fragments from columnar cell apical membrane (CCAM), lateral membrane (LM) and basal membranes (BM) were isolated as clean fractions using ultrasound, aspiration, and both differential and density gradient centrifugation; purification was monitored by electron microscopy. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS PAGE) reveals that GCAM, CCAM, LM and BM have very different protein compositions. Preliminary enzymology is consistent with the K+ ATPase being on the apical plasma membrane of the goblet cells of midgut and enveloping cells of sensilla.
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 S. A. Davies, S. F. Goodwin, D. C. Kelly, Z. Wang, M. A. Sozen, K. Kaiser, and J. A.T. Dow Analysis and Inactivation of vha55, the Gene Encoding the Vacuolar ATPase B-subunit in Drosophila melanogaster Reveals a Larval Lethal Phenotype J. Biol. Chem., November 29, 1996; 271(48): 30677 - 30684. [Abstract] [Full Text] [PDF]
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R. Graf, W. R. Harvey, and H. Wieczorek Purification and Properties of a Cytosolic V1-ATPase J. Biol. Chem., August 23, 1996; 271(34): 20908 - 20913. [Abstract] [Full Text] [PDF]
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