Download e-book for kindle: Aquaporins by Baoxue Yang (eds.)

By Baoxue Yang (eds.)

ISBN-10: 9402410554

ISBN-13: 9789402410556

ISBN-10: 9402410570

ISBN-13: 9789402410570

This ebook presents a cutting-edge document on our present figuring out of aquaporins and the longer term course of the sphere. Aquaporins (AQPs) are a bunch of water-channel proteins which are in particular permeable to water and different small molecules, comparable to glycerol and urea. thus far 13 water-channel proteins (AQP0 – AQP12) were cloned and the mechanisms and physiological capabilities of water shipping throughout organic membranes have lengthy been the topic of curiosity. contemporary advances within the molecular biology and body structure of water shipping have yielded new insights into how and why water strikes throughout telephone membranes, and reports on aquaporin knockout mouse types recommend that aquaporins are focused on the advance of a few ailments and so they will be precious goals of study into selective-inhibitor medicinal drugs. via targeting the advances remodeled the final two decades within the biophysics, genetics, protein constitution, molecular biology, body structure, pathophysiology and pharmacology of aquaporins in mammalian telephone membranes, this booklet offers novel insights into additional mechanisms and the physiological value of water and a few small molecule delivery in mammals in an effort to stimulate extra examine in new directions.

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This induces a signaling cascade, involving Gs protein mediated activation of adenylate cyclase (AC), a rise in intracellular cAMP, activation of protein kinase A (PKA) and subsequent phosphorylation of AQP2. This results in the redistribution of AQP2 from intracellular vesicles to the apical membrane. AVP ­stimulation also results in increased intracellular Ca2+ levels via Ca2+ release from calmodulin-dependent ryanodine-sensitive intracellular stores, which induces apical membrane expression of AQP2.

CRE present in the AQP2 gene regulates decreased rate of endocytosis [138, 156], thus, transcription of the gene [79, 151]. Hypertonicity phosphorylation of AQP2 may alter the efficiency affects transcription of many genes through the of pit maturation and clathrin-coated vesicle and interaction between the tonicity-responsive modulate quantity of AQP2 in clathrin-coated enhancer (TonE) and its transcription factor pits and internalization [56].  TonEBP knockout mice show downLately, AQP2 was shown to interact with regulated protein expression of AQP2, confirmcaveolin-1, a principal component of caveolae ing the role of TonE/ToneEBP in AQP2 membranes that are involved in receptor-­ transcription [79] (Fig.

There are several potential AQP5 membrane trafficking has been shown to phosphorylation sites of AQP4 for PKA, PKC, be affected by cAMP in a PKA-dependent manPKG, casein kinase (CK) and calcium/calmodu- ner [121, 254]. Elevated intracellular cAMP lin dependent protein kinases (CaMK). appears to have distinct acute and chronic effects, The Ser111 residue of AQP4 is a potential site which cause a decrease in AQP5 membrane for both PKA phosphorylation and calcium-­ abundance in short-term (minutes) and increased dependent CaMKII phosphorylation.

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Aquaporins by Baoxue Yang (eds.)

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