A cancer-associated lactate dehydrogenase is expressed in normal retina.
An unusual isozyme of lactate dehydrogenase, lactate dehydrogenase k, is found in high concentrations in cultured cells transformed by the Kirsten murine sarcoma virus and in many human cancer tissues. In experiments described here high levels of a lactate dehydrogenase k activity were detected in extracts of normal rodent retina. This activity had the same key properties as the human tumor isozyme, namely, a highly cathodic electrophoretic mobility and inhibition of enzymatic activity by oxygen and 5',5'-dipurinenucleoside tetraphosphates. Expression of this activity in the retina may be related to the high aerobic glycolysis characteristic of the retina, a metabolic feature shared with many tumors.
D000818:Animals; D002471:Cell Transformation, Neoplastic / Q000378:metabolism; D002645:Chickens; D004586:Electrophoresis; D006019:Glycolysis; D006168:Guinea Pigs; D006801:Humans; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D051379:Mice; D008815:Mice, Inbred Strains; D009369:Neoplasms / Q000201:enzymology*; D010100:Oxygen / Q000494:pharmacology; D051381:Rats; D012160:Retina / Q000201:enzymology*
D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase; D010100:Oxygen