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Nitric oxide and its decomposed derivatives decrease the binding of extracellular‐superoxide dismutase to the endothelial cell surface
Author(s) -
Yamamoto Masayuki,
Hara Hirokazu,
Adachi Tetsuo
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02839-3
Subject(s) - chemistry , superoxide dismutase , nitric oxide , endothelial stem cell , biochemistry , superoxide , umbilical vein , nitric oxide synthase , extracellular , endothelium , microbiology and biotechnology , oxidative stress , endocrinology , enzyme , biology , organic chemistry , in vitro
Extracellular‐superoxide dismutase (EC‐SOD) is bound to the vascular endothelial cell surface with an affinity for heparan sulfate proteoglycan. The binding of EC‐SOD to the human umbilical vein endothelial cell (HUVEC) and bovine aortic endothelial cell surface proteoglycans was significantly decreased by the incubation with S ‐nitroso‐ N ‐acetyl‐ DL ‐penicillamine (SNAP) and (±)‐ N ‐[( E )‐4‐ethyl‐2‐[( Z )‐hydroxyimino]‐5‐nitro‐3‐hexene‐1‐yl]‐3‐pyridine carboxamide (NOR4), potent nitric oxide (NO) donors. NO derived from lipopolysaccharide‐stimulated J774 A‐1 cells also decreased the binding of EC‐SOD to HUVEC, and this decrease was blocked by N G ‐nitro‐ L ‐arginine, a nitric oxide synthase inhibitor. SNAP and NOR4 also decreased the binding of EC‐SOD to immobilized heparin. Furthermore, the decomposed derivatives of NO donors and sodium nitrite decreased the binding of EC‐SOD. These observations suggest that excess NO produced in the inflammatory conditions decreases the binding of EC‐SOD to the vascular endothelial cell surface, which results in a loss of the ability to protect the endothelial cell surface from oxidative stress.