Cl- absorption and HCO3- secretion are intimately associated
processes vital to epithelial function, itself a key physiological
activity. Until recently the transporters responsible remained
obscure, but a breakthrough occurred with the discovery of the
SLC26 transporters family. It is now clear that the SLC26
transporters have broad physiological functions since mutations in
several members are linked to a variety of diseases. This book
describes the properties of this family in detail, with
contributions from the leading global researchers in the field.
Complementary views from experts on other ion channels are offered
in the discussions, which make fascinating reading.
This family consists of at least 10 genes, each of which has
several splice variants. Most members of the family are expressed
in the luminal membrane of epithelial cells. Characterization of
anion transport by three members has revealed that all function as
Cl-/HCO3- exchangers, suggesting that SLC26 transporters are
responsible for the luminal Cl-/HCO3- exchange activity. The SLC26
transporters are activated by the CF transmembrane conductance
regulator and activate it in turn, leading to a model in which
these molecules act together to mediate epithelial Cl- absorption
and HCO3- secretion.
The book includes chapters on the transport of other molecules by
the SLC26 family, including oxalate in the kidney and sugars in
cochlear hair cells amongst others. It also describes recent
discoveries that most SLC26 transporters bind to scaffold proteins
and that they all contain a conserved domain predicted to
participate in protein-protein interactions. These suggest the
SLC26 transporters exist in complexes with other Cl- and HCO3-
transporters, and possibly other regulatory proteins. This book
explores the functional role of these interactions, leading to
better understanding of transepithelial fluid and electrolyte
secretion and the diseases associated with it.
قائمة المحتويات
Chair’s introduction (Michael
Welsh).
Overview of the SLC26 family and associated diseases
(Juha Kere) .
Discussion.
Individual characteristics of members of the SLC26 family in
Vertebrates and their homologues in insects (Marlies
Knipper, Thomas Weber, Harald Winter, Claudia Braig, Jelka
Cimerman, Juergen T. Fraenzer and Ulrike
Zimmermann).
Discussion.
Sulfate transport by SLC26 transporters (Daniel
Markovich).
Sugar transport by members of the SLC26 superfamily
(Jonathan Ashmore and Jean-Marie
Chambard).
Discussion.
Discussion.
SLC26A3 and congenital chloride diarrhoea (Pia
Höglund).
Discussion.
Expression, regulation and the role of SLC26 Cl-/HCO3-
exchangers in kidney and gastrointestinal tract (Manoocher
Soleimani).
Discussion.
Anion exchangers in flux: functional differences between
human and mouse SLC26A6 polypeptides (Seth L. Alper, Andrew
K. Stewart, Marina N. Chernova, Alexander S. Zolotarev, Jeffrey S.
Clark and David H. Vandorpe).
Discussion.
Physiology of electrogenic SLC26 paralogues (Michael
F. Romero, Min-Hwang Chang, Consuelo Plata, Kambiz Zandi-Nejad,
Vadjista Broumand, Caroline R. Sussman and David B.
Mount).
Discussion.
Role of SLC26-mediated Cl-/base exchange in proximal tubule
na Cl transport (Peter S. Aronson).
Discussion.
SLC26 transporters and the inhibitory control of pancreatic
ductal bicarbonate secretion (Péter Hegyi, Zoltán
Rakonczay Jr., László Tiszlavica, András
Varró, András Tóth, Gábor Rácz, Gábor
Varga, Michael A. Gray and Barry E. Argent).
Discussion.
Regulatory interaction between CFt R and the SLC26
transporters (Nikolay Shcheynikov, Shigeru B. H. Ko,
Weizhong Zeng, Joo Young Choi, Michael R. Dorwart, Philip J. Thomas
and Shmuel Muallem).
Discussion.
Insights from a transgenic mouse model on the role of SLC26A2
in health and disease.
Discussion.
Lorraine A. Everett new insights into the role of pendrin
(SLC26A4) in inner ear fluid homeostasis (Antonella Forlino,
Benedetta Gualeni, Fabio Pecora, Sara Della Torre, Rocco Piazza,
Cecilia Tiveron, Laura Tatangelo, Andrea Superti-Furga, Giuseppe
Cetta and Antonio Rossi).
Discussion.
the renal physiology of pendrin (SLC26A4) and its role in
hypertension (Susan M. Wall).
Discussion.
Interaction of prestin (SLC26A5) with monovalent
intracellular anions (Dominik Oliver, Thorsten
Schächinger and Bernd Fakler).
Discussion.
Final Discussion.
Index of contributors.
Subject index.
عن المؤلف
The Novartis Foundation is an international scientific and educational charity which promotes the study and general knowledge of science and in particular encourages international co-operation in scientific research.
المزيد من الكتب الإلكترونية من نفس المؤلف (المؤلفين) / محرر
2٬671 كتب إلكترونية في هذه الفئة
