(10, 29). These disparate findings are thus unlikely to stem from a dysfunctional Cl- channel. Alternate paradigms are currently sought. CFTR is a member of the superfamily of -binding cassette (ABC) transport proteins, including the multidrug-resistant gene product, P-glycoprotein, and yeast and bacterial transporters (15). The common feature of these proteins is the conserved cytoplasmic binding fold regions thought to bind and/or hydrolyze . We recently demonstrated that P-glycoprotein is a novel -conductive channel (1). It is possible, therefore, that both P-glycoprotein and CFTR are multifunctional proteins with more than one transport capability, including the possibility that CFTR also behaves as an channel, as we have recently demonstrated (9,23). This hypothesis may provide a novel mechanistic explanation for the disease that is based on a feedback loop linking the CFTR-mediated delivery of cellular to other transport mechanisms. Increased extracellular may be then associated with the regulation of anion-selective channels seemingly responsible for the onset and maintenance of the secretory response (13). The rescue of outwardly rectifying Cl- channel activity (ORCC) in CF cells (16), for example, can be triggered by expression of wild-type CFTR (13). More recently, extracellular was shown to activate CFTR-mediated Cl- channel activity in cells
AJP - Cell Physiology – The American Physiological Society
Published: Feb 1, 1996
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