Human blood platelets lack nitric oxide synthase activity
Human blood platelets lack nitric oxide synthase activity
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DOI：
10.3109/09537104.2014.974024
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发表时间：
2015-01-01
期刊：
影响因子：
3.3
通讯作者：
Tsikas, Dimitrios
中科院分区：
文献类型：
--
作者：
Boehmer, Anke;Gambaryan, Stepan;Tsikas, Dimitrios
关于一氧化氮合酶(NOS)在人血、血小板和红细胞中的表达和功能的报道相互矛盾。采用气相色谱-质谱法(GC-MS)检测人血小板中一氧化氮合酶活性。本方法同时测定氧化的N-15标记的一氧化氮((NO)-N-15)在一氧化氮合酶的催化下从底物L-[N-15(2)]-精氨酸生成的[N-15]亚硝酸盐和[N-15]硝酸盐。使用这种GC-MS分析方法，我们没有在未刺激的血小板和由各种激动剂(二磷酸腺苷、胶原、凝血酶或von Willebrand因子)或溶解的血小板激活的完整血小板中检测到功能性的NOS。将重组人内皮型一氧化氮合酶加入溶解的血小板中，测定L-精氨酸抑制型一氧化氮合酶的活性。我们小组以前和最近的研究挑战了人血小板和红细胞中一氧化氮合酶的表达和功能。
Reports on expression and functionality of nitric oxide synthase (NOS) activity in human blood platelets and erythrocytes are contradictory. We used a specific gas chromatography-mass spectrometry (GC-MS) method to detect NOS activity in human platelets. The method measures simultaneously [N-15] nitrite and [N-15] nitrate formed from oxidized N-15-labeled nitric oxide ((NO)-N-15) upon its NOS-catalyzed formation from the substrate L-[guanidino-N-15(2)]-arginine. Using this GC-MS assay, we did not detect functional NOS in non-stimulated platelets and in intact platelets activated by various agonists (adenosine diphosphate, collagen, thrombin, or von Willebrand factor) or lysed platelets. L-[guanidino-nitro]-Arginine-inhibitable NOS activity was measured after addition of recombinant human endothelial NOS to lysed platelets. Previous and recent studies from our group challenge expression and functionality of NOS in human platelets and erythrocytes.