Artikel: Control of oxalate formation from L-hydroxyproline in liver mitochondria.
Journal of the American Society of Nephrology : JASN
2003 Band 14, Heft 4, Seite(n) 939–946
Abstract: Serine:pyruvate/alanine:glyoxylate aminotransferase (SPT/AGT) is largely located in mitochondria in carnivores, whereas it is entirely found within peroxisomes in herbivores and humans. In rat liver, SPT/AGT is found in both of these organelles, and only ...
Abstract | Serine:pyruvate/alanine:glyoxylate aminotransferase (SPT/AGT) is largely located in mitochondria in carnivores, whereas it is entirely found within peroxisomes in herbivores and humans. In rat liver, SPT/AGT is found in both of these organelles, and only the mitochondrial enzyme is markedly induced by glucagon. Although SPT/AGT is a bifunctional enzyme involved in the metabolism of both L-serine and glyoxylate, its contribution to L-serine metabolism is independent of mitochondrial or peroxisomal localization (Xue HH et al., J Biol Chem 274: 16028-16033, 1999). Therefore, the species-specific and food habit-dependent organelle distribution might be required for proper metabolism of glyoxylate at the subcellular site of its formation. Glyoxylate formation from glycolate and that from L-hydroxyproline have been shown to occur in peroxisomes and mitochondria, respectively. The present study found that urinary excretion of oxalate was markedly increased when a large dose of L-hydroxyproline or glycolate was administered to rats. Oxalate formation from L-hydroxyproline but not that from glycolate was significantly reduced when mitochondrial SPT/AGT had been induced by glucagon. The hydroxyproline content of collagen is 10 to 13%, and collagen accounts for about 30% of total animal protein; therefore, these results suggest that an important role of mitochondrial SPT/AGT in carnivores is to convert L-hydroxyproline-derived glyoxylate into glycine in situ, preventing undesirable overflow into the production of oxalate. |
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Mesh-Begriff(e) | Animals ; Glucagon/metabolism ; Glyoxylates/metabolism ; Glyoxylates/urine ; Hydroxyproline/metabolism ; Liver/enzymology ; Male ; Mitochondria, Liver/metabolism ; Oxalates/metabolism ; Rats ; Rats, Wistar ; Transaminases/metabolism | |||||
Chemische Substanzen | Glyoxylates ; Oxalates ; Glucagon (9007-92-5) ; Transaminases (EC 2.6.1.-) ; Alanine-glyoxylate transaminase (EC 2.6.1.44) ; serine-pyruvate aminotransferase (EC 2.6.1.51) ; glyoxylic acid (JQ39C92HH6) ; Hydroxyproline (RMB44WO89X) | |||||
Sprache | Englisch | |||||
Erscheinungsdatum | 2003-02-17 | |||||
Erscheinungsland | United States | |||||
Dokumenttyp | Journal Article ; Research Support, Non-U.S. Gov't | |||||
ZDB-ID | 1085942-1 | |||||
ISSN | 1533-3450 ; 1046-6673 | |||||
ISSN (online) | 1533-3450 | |||||
ISSN | 1046-6673 | |||||
DOI | 10.1097/01.asn.0000059310.67812.4f | |||||
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Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
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