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

Charles, IG; Palmer, RM; Hickery, MS; Bayliss, MT; Chubb, A; Hall, VS; Moss, DW; Moncada, S

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

Charles, IG Palmer, RM Hickery, MS Bayliss, MT Chubb, A Hall, VS Moss, DW Moncada, S

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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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Field	Value	Language
dc.contributor.author	Charles, IG	en_US
dc.contributor.author	Palmer, RM	en_US
dc.contributor.author	Hickery, MS	en_US
dc.contributor.author	Bayliss, MT	en_US
dc.contributor.author	Chubb, A	en_US
dc.contributor.author	Hall, VS	en_US
dc.contributor.author	Moss, DW	en_US
dc.contributor.author	Moncada, S	en_US
dc.date.issued	1993-01	en_US
dc.identifier.citation	Proceedings of the National Academy of Sciences, 1993, 90 (NA), pp. 11419 - 11423	en_US
dc.identifier.issn	1091-6490	en_US
dc.identifier.uri	http://hdl.handle.net/10453/13312
dc.description.abstract	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.	en_US
dc.publisher	National Academy of Sciences	en_US
dc.relation.ispartof	Proceedings of the National Academy of Sciences	en_US
dc.title	Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte	en_US
dc.type	Journal Article
utslib.citation.volume	NA	en_US
utslib.citation.volume	90	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	closed_access
pubs.consider-herdc	false	en_US
pubs.issue	NA	en_US
pubs.volume	90	en_US

Abstract:

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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http://hdl.handle.net/10453/13312