FEBS Letters | |
The protein inhibitor of neuronal nitric oxide synthase (PIN): characterization of its action on pure nitric oxide synthases | |
Schmidt, Kurt1  Hemmens, Benjamin1  Völker, Christof1  Woschitz, Silvia1  Mayer, Bernd1  Klösch, Burkhardt1  Pitters, Eva1  | |
[1] Institut für Pharmakologie und Toxikologie, Karl-Franzens Universität Graz, Universitätsplatz 2, A-8010 Graz, Austria | |
关键词: Nitric oxide; Nitric oxide synthase; Dimerization; Isoenzyme; Inhibitor protein; NOS; nitric oxide synthase; nNOS; neuronal nitric oxide synthase (type I); iNOS; inducible nitric oxide synthase (type II); eNOS; endothelial nitric-oxide synthase (type III); H4biopterin; (6R)-5; 6; 7; 8-tetrahydro-l-biopterin=(6R)-5; 6; 7; 8-tetrahydro-6-(l-erythro-1; 2-dihydroxypropyl)pteridine; PIN; protein inhibitor of nNOS; GST-PIN; fusion protein of PIN with glutathione S-transferase; | |
DOI : 10.1016/S0014-5793(98)00704-2 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Neuronal NO synthase (nNOS) was discovered recently to interact specifically with the protein PIN (protein inhibitor of nNOS) [Jaffrey, S.R. and Snyder, S.H. (1996) Science 274, 774–777]. We have studied the effects on pure NOS enzymes of the same GST-tagged PIN used in the original paper. Unexpectedly, all NOS isoenzymes were inhibited. The IC50 for nNOS was 18±6 μM GST-PIN with 63 nM nNOS after 30 min at 37°C. Uncoupled NADPH oxidation was inhibited similarly, whereas cytochrome c reductase activity, the K M for l-arginine, and dimerization were unaffected. We reconsider the physiological role of PIN in the light of these results.
【 授权许可】
Unknown
【 预 览 】
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