Reddy, Madhava C and Bhat, Vadiraja B and Kiranmai, G and Reddy, Narsa M and Reddanna, P and Madyastha, KM (2000) Selective inhibition of cyclooxygenase-2 by C-phycocyanin, a biliprotein from Spirulina platensis. In: Biochemical and Biophysical Research Communications, 277 (2). pp. 599-603.
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Abstract
We report data from two related assay systems (isolated enzyme assays and whole blood assays) that C-phycocyanin a biliprotein from Spirulina platensis is a selective inhibitor of cyclooxygenase-a (COX-2) with a very low IC50 COX-2/IC50 COX-1 ratio (0.04). The extent of inhibition depends on the period of preincubation of phycocyanin with COX-2, but without any effect on the period of preincubation with COX-1. The IC50 value obtained for the inhibition of COX-2 by phycocyanin is much lower (180 nM) as compared to those of celecoxib (255 nM) and rofecoxib (401 nM), the well-known selective COX-2 inhibitors. In the human whole blood assay, phycocyanin very efficiently inhibited COX-2 with an IC50 value of 80 nM. Reduced phycocyanin and phycocyanobilin, the chromophore of phycocyanin are poor inhibitors of COX-2 without COX-2 selectivity. This suggests that apoprotein in phycocyanin plays a key role in the selective inhibition of COX-2. The present study points out that the hepatoprotective, anti-inflammatory, and anti-arthritic properties of phycocyanin reported in the literature may be due, in part, to its selective COX-2 inhibitory property, although its ability to efficiently scavenge free radicals and effectively inhibit lipid peroxidation may also be involved. (C) 2000 Academic Press.
Item Type: | Journal Article |
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Publication: | Biochemical and Biophysical Research Communications |
Publisher: | Elsevier Science |
Additional Information: | Copyright of this article belongs to Elsevier Science. |
Department/Centre: | Division of Chemical Sciences > Organic Chemistry |
Date Deposited: | 04 Aug 2010 07:03 |
Last Modified: | 19 Sep 2010 06:13 |
URI: | http://eprints.iisc.ac.in/id/eprint/31066 |
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