title: A role for taurine in mitochondrial function.
abstract: The mitochondrial pH gradient across the inner-membrane is stabilised by buffering of the matrix. A low-molecular mass buffer compound has to be localised in the matrix to maintain its alkaline pH value. Taurine is found ubiquitously in animal cells with concentrations in the millimolar range and its pKa value is determined to 9.0 (25 degrees C) and 8.6 (37 degrees C), respectively. Localisation of such a low-molecular buffer in the mitochondrial matrix, transforms the matrix into a biochemical reaction chamber for the important matrix-localised enzyme systems. Three acyl-CoA dehydrogenase enzymes, which are pivotal for beta-oxidation of fatty acids, are demonstrated to have optimal activity in a taurine buffer. By application of the model presented, taurine depletion caused by hyperglycemia could provide a link between mitochondrial dysfunction and diabetes.
authors.affiliation: Department of Clinical Biochemistry, 3-01-1, Rigshospitalet, Copenhagen University Hospital, Blegdamsvej 9, DK-2100 Copenhagen, Denmark. shhansen@rh.dk
authors.forename: Svend Høime
authors.initials: SH
authors.lastname: Hansen
authors.forename: Mogens Larsen
authors.initials: ML
authors.lastname: Andersen
authors.forename: Claus
authors.initials: C
authors.lastname: Cornett
authors.forename: Robert
authors.initials: R
authors.lastname: Gradinaru
authors.forename: Niels
authors.initials: N
authors.lastname: Grunnet
mesh_terms: D044944:Acyl-CoA Dehydrogenases / Q000378:metabolism; D000818:Animals; D002021:Buffers; D019069:Cell Respiration; D006863:Hydrogen-Ion Concentration; D008564:Membrane Potentials / Q000502:physiology; D008928:Mitochondria / Q000378:metabolism*; D015394:Molecular Structure; D010084:Oxidation-Reduction; D013654:Taurine / Q000737:chemistry / Q000378:metabolism*
chemical_list: D002021:Buffers; D013654:Taurine; D044944:Acyl-CoA Dehydrogenases
references.citation: Am J Physiol. 1985 Oct;249(4 Pt 2):R449-54
references.pmid: 4051030
references.citation: Diabetes Metab Res Rev. 2001 Sep-Oct;17(5):330-46
references.pmid: 11747139
references.citation: Eur J Biochem. 2004 Feb;271(3):494-508
references.pmid: 14728676
references.citation: Histochem J. 2000 Jan;32(1):53-61
references.pmid: 10805385
references.citation: Biochemistry. 1966 Feb;5(2):467-77
references.pmid: 5942950
references.citation: FEBS Lett. 2003 Oct 9;553(1-2):73-8
references.pmid: 14550549
references.citation: Can J Physiol Pharmacol. 2009 Feb;87(2):91-9
references.pmid: 19234572
references.citation: J Physiol. 1938 Apr 14;92(3):336-43
references.pmid: 16994977
references.citation: J Biomed Sci. 2010 Aug 24;17 Suppl 1:S25
references.pmid: 20804600
references.citation: Biol Rev Camb Philos Soc. 1966 Aug;41(3):445-502
references.pmid: 5329743
references.citation: Biochem J. 1938 Feb;32(2):209-11
references.pmid: 16746608
references.citation: EMBO J. 2002 Dec 2;21(23):6581-9
references.pmid: 12456664
references.citation: Adv Exp Med Biol. 2006;583:129-35
references.pmid: 17153596
references.citation: Cardiovasc Res. 2002 Jan;53(1):48-58
references.pmid: 11744012
references.citation: Anal Biochem. 1990 May 1;186(2):280-4
references.pmid: 2363500
references.citation: Anat Embryol (Berl). 1988;178(5):407-21
references.pmid: 3177894
references.citation: Nature. 1961 Jul 8;191:144-8
references.pmid: 13771349
references.citation: Biochem J. 1967 Aug;104(2):588-600
references.pmid: 6048801
references.citation: Neurochem Res. 2004 Jan;29(1):27-63
references.pmid: 14992263
references.citation: Amino Acids. 2000;19(3-4):527-46
references.pmid: 11140357
references.citation: Eur J Biochem. 1997 May 1;245(3):600-7
references.pmid: 9182995
references.citation: Am Heart J. 1992 Feb;123(2):339-45
references.pmid: 1736568
references.citation: Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6803-8
references.pmid: 9618493
references.citation: Science. 2005 Jan 21;307(5708):384-7
references.pmid: 15662004
references.citation: Am J Physiol Endocrinol Metab. 2006 Oct;291(4):E807-16
references.pmid: 16720625
references.citation: J Endocrinol. 1998 Nov;159(2):341-8
references.pmid: 9795376
references.citation: FASEB J. 2004 Mar;18(3):577-9
references.pmid: 14734644
references.citation: Meat Sci. 1998 Nov;50(3):327-32
references.pmid: 22061151
references.citation: Eur J Biochem. 1997 Jun 1;246(2):548-56
references.pmid: 9208949
references.citation: Methods Enzymol. 1979;55:547-69
references.pmid: 37402
references.citation: Biochim Biophys Acta. 1994 Dec 30;1188(3):405-16
references.pmid: 7803454
references.citation: Mol Cell Biochem. 1997 Sep;174(1-2):61-6
references.pmid: 9309666
references.citation: Diabetes. 2005 Jun;54(6):1615-25
references.pmid: 15919781
references.citation: Meat Sci. 1999 Mar;51(3):215-9
references.pmid: 22061854
references.citation: J Biol Chem. 2004 Mar 19;279(12):11521-9
references.pmid: 14701849
references.citation: Brain Res. 1990 Feb 12;509(1):153-5
references.pmid: 2306631