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Inhibition of creatine kinase by S ‐nitrosoglutathione
Author(s) -
Wolosker Herman,
Panizzutti Rogério,
Engelender Simone
Publication year - 1996
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 - 10.1016/0014-5793(96)00829-0
Subject(s) - s nitrosoglutathione , chemistry , creatine kinase , pharmacology , biochemistry , medicine , enzyme , glutathione
The sarcoplasmic reticulum‐bound creatine kinase from rabbit skeletal muscle was inhibited by the nitric oxide donor S ‐nitrosoglutathione (GSNO). This led to a decrease in Ca 2+ uptake in sarcoplasmic reticulum vesicles when the transport was driven by ATP generated from phosphocreatine and ADP. In contrast, the Ca 2+ transport measured using 2 mM ATP as substrate was unaffected by GSNO up to 200 μM. GSNO (5–20 μM) inhibited the activity of both soluble and membrane‐bound creatine kinase. Oxyhemoglobin (15–40 μM) protected creatine kinase against inactivation by GSNO. The inhibition by 10 μM GSNO was reversed by the addition of dithiothreitol (2 mM). The results indicate that nitric oxide (NO, including NO + , NO and NO − ) inactivates creatine kinase in vitro by promoting nitrosylation of critical sulphydryl groups of the enzyme.