Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 28, Issue 11, Pages 1671-1678Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/S0891-5849(00)00281-1
Keywords
creatine kinase; S-nitrosothiols; S-thiolation; nitric oxide; free radicals
Funding
- NCI NIH HHS [CA77822] Funding Source: Medline
- NCRR NIH HHS [RR010008] Funding Source: Medline
- NIGMS NIH HHS [GM55792] Funding Source: Medline
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Creatine kinase is reversibly inhibited by incubation with S-nitrosothiols. Loss of enzyme activity is associated with the depletion of 5,5'-dithiobis (2-nitrobenzoic acid)-accessible thiol groups, and is not due to nitric oxide release from RSNO. Full enzymatic activity and protein thiol content are restored by incubation of the S-nitrosothiol-modified protein with glutathione. S-niuoso-N-acetylpenicillamine, which contains a more sterically hindered S-nitroso group than S-nitrosoglutathione, predominantly modifies the protein thiol to an S-nitrosothiol via a transnitrosation reaction. In contrast, S-nitrosoglutathione modifies creatine kinase predominantly by S-thiolation. Both S-nitroso-N-acetylpenicillamine and S-nitrosoglutathione modify bovine serum albumin to an S-nitroso derivative. This indicates that S-thiolation and S-nitrosation are both relevant reactions for S-nitrosothiols, and the relative importance of these reactions in biological systems depends on both the environment of the protein thiol and on the chemical nature of the S-nitrosothiol. (C) 2000 Elsevier Science Inc.
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