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Characteristics of mammalian Rh glycoproteins (SLC42 transporters) and their role in acid-base transport.
- Source :
-
Molecular aspects of medicine [Mol Aspects Med] 2013 Apr-Jun; Vol. 34 (2-3), pp. 629-37. - Publication Year :
- 2013
-
Abstract
- The mammalian Rh glycoproteins belong to the solute transporter family SLC42 and include RhAG, present in red blood cells, and two non-erythroid members RhBG and RhCG that are expressed in various tissues, including kidney, liver, skin and the GI tract. The Rh proteins in the red blood cell form an "Rh complex" made up of one D-subunit, one CE-subunit and two RhAG subunits. The Rh complex has a well-known antigenic effect but also contributes to the stability of the red cell membrane. RhBG and RhCG are related to the NH4(+) transporters of the yeast and bacteria but their exact function is yet to be determined. This review describes the expression and molecular properties of these membrane proteins and their potential role as NH3/NH4(+) and CO2 transporters. The likelihood that these proteins transport gases such as CO2 or NH3 is novel and significant. The review also describes the physiological importance of these proteins and their relevance to human disease.<br /> (Copyright © 2012 Elsevier Ltd. All rights reserved.)
- Subjects :
- Blood Proteins metabolism
Carbon Dioxide metabolism
Cation Transport Proteins metabolism
Glycoproteins metabolism
Humans
Membrane Glycoproteins metabolism
Membrane Transport Proteins metabolism
Models, Genetic
Protein Conformation
Quaternary Ammonium Compounds metabolism
Skin metabolism
Substrate Specificity
Viscera metabolism
Blood Proteins genetics
Blood Proteins physiology
Cation Transport Proteins genetics
Cation Transport Proteins physiology
Glycoproteins genetics
Glycoproteins physiology
Membrane Glycoproteins genetics
Membrane Glycoproteins physiology
Membrane Transport Proteins genetics
Membrane Transport Proteins physiology
Models, Molecular
Multigene Family genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1872-9452
- Volume :
- 34
- Issue :
- 2-3
- Database :
- MEDLINE
- Journal :
- Molecular aspects of medicine
- Publication Type :
- Academic Journal
- Accession number :
- 23506896
- Full Text :
- https://doi.org/10.1016/j.mam.2012.05.013