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Journal of Experimental Biology, Vol 203, Issue 1 127-135, Copyright © 2000 by Company of Biologists
JOURNAL ARTICLES |
H Wieczorek, G Grber, WR Harvey, M Huss, H Merzendorfer and W Zeiske
Department of Biology, University of Osnabruck, D-49069 Osnabruck, Germany. wieczorek@biologie.uni-osnabrueck.de
H(+) V-ATPases (V-ATPases) are found in two principal locations, in endomembranes and in plasma membranes. The plasma membrane V-ATPase from the midgut of larval Manduca sexta is the sole energizer of all transepithelial secondary transport processes. At least two properties make the lepidopteran midgut a model tissue for studies of general aspects of V-ATPases. First, it is a rich source for purification of the enzyme and therefore for structural studies: 20 larvae provide up to 0.5 mg of holoenzyme, and soluble, cytosolic V(1) complexes can be obtained in even greater amounts of up to 2 mg. Second, midgut ion-tranport processes are strictly controlled by the regulation of the V-ATPase, which is the sole energizer of all ion transport in this epithelium. Recent advances in our understanding the structure of the V(1) and V(o) complexes and of the regulation of the enzyme's biosynthesis and ion-transport activity will be discussed.
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