By Stefan Hohmann
Aquaporins summarizes the current wisdom during this increasing box of study, beginning with the structural research of water channel proteins. next chapters start with mammalian aquaporins, reading body structure and pathophysiology, research of knock-out version animals, and the rules of aquaporin functionality. additionally lined is the distribution and rules of aquaporins in vegetation and the functionality of water and glycerol channels in microbial structures. Key beneficial properties* entire remedy of a topical examine box* Authored via global leaders within the box* Covers structural biology and body structure* Covers varied experimental and organic structures* Chapters on plant and microbial structures* vast remedy of mammalian body structure and pathophysiology* Structural research excellently illustrated
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Extra resources for Aquaporins
As noted previously, phylogenetic analysis of mammalian aquaporins splits the superfamily into two subfamilies—orthodox aquaporins and aquaglyceroporins (Fig. 8A). , 1995). , 1994). Structural explanations for these functional differences are being sought. The primary amino acid sequences are highly homologous, yet a few sequence differences are present (Fig. 8B). Of note, AqpZ and orthodox aquaporins have a Ser following the second NPA motif in loop E (NPARS), whereas GlpF and aquaglyceroporins have an Asp at this site (NPARD) as well as a motif (GLYY) at the extracellular end of the third transmembrane domain.
Acad. Sci. USA 90, 7275–7279. , Chou, C. , Christensen, E. , Kishore, B. , and Knepper, M. A. (1995a). Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. Proc. Natl. Acad. Sci. USA 92, 1013–1017. , Smith, B. , Christensen, E. , and Maunsbach, A. (1995b). Aquaporin-1 water channels in short and long loop descending thin limbs and in descending vasa recta in rat kidney. Am. J. Physiol. Renal 37, F1023–1037.
8). A. Orthodox Aquaporins The ﬁrst characterized member of the family, AQP1, is freely permeated by water but not by other solutes. Several other members of the family were also found to be highly water selective. 1. , 1993). A series of reports deﬁned this protein in various physiologic and clinical states (see Chapters 3, 4, and 6). Although it was predicted to be the vasopressin-regulated water channel, formal demonstration was achieved by an elegant report in which collecting ducts were isolated from rat kidney and examined for water permeability and the distribution of AQP2 was established by immunogold electron microscopy (Fig.
Aquaporins by Stefan Hohmann