Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte

Publisher:
National Academy of Sciences
Publication Type:
Journal Article
Citation:
Proceedings of the National Academy of Sciences, 1993, 90 (NA), pp. 11419 - 11423
Issue Date:
1993-01
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Incubation of buman articular cbondrocytes with interleukin III results in the time-dependent expression of nitric oxide (NO) synthase. We report bere the isolatIon of a cDNA clone which encodes a protein of 1153 amino acids with a molecular mass of 131,213 Da and a calculated isoelectric point of 7.9. CHO ceUs transfected with a plasmid harboring Ibis eDNA clone expressed NO syntbase activity that was inhibited by some L-arginine analogues. Tbe deduced amino acid sequence of the human chondrocyte inducible NO synthase sbows 51 % identity and 68% simUarity witb the endotheUaI NO synthase and 54% identity and 70% sbnllarity with tbe neuronal NO synthase. The simUarity (88%) between tbe buman cbondrocyte NO synthase eDNA sequence and that reported for the murine macropbage suggests tbat tbe inducible class of enzyme -is conserved between different cell types and across species.
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