Internal Medicine

Get Aquaporins PDF

By Stefan Hohmann

ISBN-10: 0080494390

ISBN-13: 9780080494395

ISBN-10: 0121533514

ISBN-13: 9780121533519

ISBN-10: 0123520959

ISBN-13: 9780123520951

Aquaporins summarizes the current wisdom during this increasing box of analysis, beginning with the structural research of water channel proteins. next chapters commence with mammalian aquaporins, interpreting body structure and pathophysiology, research of knock-out version animals, and the law of aquaporin functionality. additionally lined is the distribution and rules of aquaporins in vegetation and the functionality of water and glycerol channels in microbial platforms. Key good points* entire remedy of a topical examine box* Authored by way of global leaders within the box* Covers structural biology and body structure* Covers diverse experimental and organic structures* Chapters on plant and microbial platforms* vast therapy of mammalian body structure and pathophysiology* Structural research excellently illustrated

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Extra info for Aquaporins

Example text

Knepper, M. , and Nielsen, S. (1996). Hypokalemia-induced downregulation of aquaporin-2 water channel expression in rat kidney medulla and cortex. J. Clin. Invest. 97, 1960–1968. Mathai, J. , Smith, B. , Preston, G. , van Zijl, P. C. , Zeidel, M. , and Agre, P. (1996). Functional analysis of aquaporin-1 deficient red cells: the Colton-null phenotype. J. Biol. Chem. 271, 1309–1313. Maunsbach, A. , and Nielsen, S. (1997). Aquaporin-1 water channel expression in human kidney. J. Am. Soc. Nephrol.

NY. Acad. Sci. 372, 106–117. , Smith, B. , Zeidel, M. , and Agre, P. (1994). Biologically active two-dimensional crystals of Aquaporin CHIP. J. Biol. Chem. 269, 1583–1586. , Heymann, J. , Smith, B. , and Engel, A. (1997). Three-dimensional structure of aquaporin-1. Nature 387, 624–627. Wistow, G. , Pisano, M. , and Chepelinsky, A. B. (1991). Tandem sequence repeats in transmembrane channel proteins. Trends Biochem. Sci. 165, 170–171. Xu, D. , Martin, P. , et al. (1997).

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.

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Aquaporins by Stefan Hohmann


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