V-ATPase-energized epithelia and biological insect control.
نویسنده
چکیده
Background is provided for the experimentally detailed contributions concerning the structure, distribution and function of V-ATPase-based ion pumps in insect epithelia. The mode of action of an insecticidal bacterial protein, which is dependent upon the V-ATPase-energized state in larval lepidopteran midgut for activity, is discussed.
منابع مشابه
THE INSECT V-ATPase, A PLASMA MEMBRANE PROTON PUMP ENERGIZING SECONDARY ACTIVE TRANSPORT: IMMUNOLOGICAL EVIDENCE FOR THE OCCURRENCE OF A V-ATPase IN INSECT ION-TRANSPORTING EPITHELIA.
Active electrogenic K+ transport in insects serves as the energy source for secretion or absorption in gastrointestinal epithelia or for the receptor current in sensory epithelia. In the larval midgut of the tobacco hornworm Manduca sexta, a vacuolar-type proton pump (V-ATPase) and a K+/nH+ antiport represent the functional elements of the potassium pump. Several immunological findings support ...
متن کاملPhylogeny and cloning of ion transporters in mosquitoes.
Membrane transport in insect epithelia appears to be energized through proton-motive force generated by the vacuolar type proton ATPase (V-ATPase). However, secondary transport mechanisms that are coupled to V-ATPase activity have not been fully elucidated. Following a blood meal, the female mosquito regulates fluid and ion homeostasis through a series of characteristic behaviors that require b...
متن کاملThe insect V-ATPase, a plasma membrane proton pump energizing secondary active transport: molecular analysis of electrogenic potassium transport in the tobacco hornworm midgut.
Goblet cell apical membranes in the larval midgut of Manduca sexta are the site of active and electrogenic K+ secretion. They possess a vacuolar-type ATPase which, in its immunopurified form, consists of at least nine polypeptides. cDNAs for the A and B subunits screened by monoclonal antibodies to the A subunit of the Manduca V-ATPase or by hybridisation with a cDNA probe for a plant V-ATPase ...
متن کاملH(+) V-ATPase-energized transporters in brush border membrane vesicles from whole larvae of Aedes aegypti.
Brush border membrane vesicles (BBMVs) from Whole larvae of Aedes aegypti (AeBBMVWs) contain an H(+) V-ATPase (V), a Na(+)/H(+) antiporter, NHA1 (A) and a Na(+)-coupled, nutrient amino acid transporter, NAT8 (N), VAN for short. All V-ATPase subunits are present in the Ae. aegypti genome and in the vesicles. AgNAT8 was cloned from Anopheles gambiae, localized in BBMs and characterized in Xenopus...
متن کاملVacuolar-type proton pumps in insect epithelia.
Active transepithelial cation transport in insects was initially discovered in Malpighian tubules, and was subsequently also found in other epithelia such as salivary glands, labial glands, midgut and sensory sensilla. Today it appears to be established that the cation pump is a two-component system of a H(+)-transporting V-ATPase and a cation/nH(+) antiporter. After tracing the discovery of th...
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ورودعنوان ژورنال:
- The Journal of experimental biology
دوره 172 شماره
صفحات -
تاریخ انتشار 1992