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Animal plasma membrane energization by proton‐motive V‐ATPases
Author(s) -
Wieczorek Helmut,
Brown Dennis,
Grinstein Sergio,
Ehrenfeld Jordi,
Harvey William R.
Publication year - 1999
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/(sici)1521-1878(199908)21:8<637::aid-bies3>3.0.co;2-w
Subject(s) - membrane , atpase , f atpase , extracellular , secretion , microbiology and biotechnology , homeostasis , proton pump , biology , v atpase , biophysics , biochemistry , chemistry , enzyme , thylakoid , chloroplast , gene
Proton‐translocating, vacuolar‐type ATPases, well known energizers of eukaryotic, vacuolar membranes, now emerge as energizers of many plasma membranes. Just as Na + gradients, imposed by Na + /K + ATPases, energize basolateral plasma membranes of epithelia, so voltage gradients, imposed by H + V‐ATPases, energize apical plasma membranes. The energized membranes acidify or alkalinize compartments, absorb or secrete ions and fluids, and underwrite cellular homeostasis. V‐ATPases acidify extracellular spaces of single cells such as phagocytes and osteoclasts and of polarized epithelia, such as vertebrate kidney and epididymis. They alkalinize extracellular spaces of lepidopteran midgut. V‐ATPases energize fluid secretion by insect Malpighian tubules and fluid absorption by insect oocytes. They hyperpolarize external plasma membranes for Na + uptake by amphibian skin and fish gills. Indeed, it is likely that ion uptake by osmotically active membranes of all fresh water organisms is energized by V‐ATPases. Awareness of plasma membrane energization by V‐ATPases provides new perspectives for basic science and presents new opportunities for medicine and agriculture. BioEssays 21:637–648, 1999. © 1999 John Wiley & Sons, Inc.