Nitric oxide and its decomposed derivatives decrease the binding of extracellular‐superoxide dismutase to the endothelial cell surface

FEBS Letters

Yamamoto, Masayuki¹  Adachi, Tetsuo¹  Hara, Hirokazu¹ 

[1] Laboratory of Clinical Pharmaceutics, Gifu Pharmaceutical University, 5-6-1 Mitahora-higashi, Gifu 502-8585, Japan

关键词: Extracellular-superoxide dismutase;    Nitric oxide;    Nitrite;    Endothelial cell;    Heparan sulfate proteoglycan;    Oxidative stress;    BAEC;    bovine aortic endothelial cell(s);    BSA;    bovine serum albumin;    DMEM;    Dulbecco's modified Eagle's medium;    EC-SOD;    extracellular-superoxide dismutase;    FCS;    fetal calf serum;    HUVEC;    human umbilical vein endothelial cell(s);    iNOS;    inducible nitric oxide synthase;    L-NNA;    N G-nitro-L-arginine;    LPS;    lipopolysaccharide;    NO;    nitric oxide;    NOS;    nitric oxide synthase;    NOR4;    (±)-N-[(E)-4-ethyl-2-[(Z)-hydroxyimino]-5-nitro-3-hexene-1-yl]-3-pyridine carboxamide;    PBS;    phosphate-buffered saline;    SIN-1;    3-(4-morpholinyl) sydnonimine hydrochloride;    SNAP;    S-nitroso-N-acetyl-DL-penicillamine;   

DOI  :  10.1016/S0014-5793(01)02839-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown