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Molecular cloning and characterization of human endothelial nitric oxide synthase

机译:人内皮型一氧化氮合酶的分子克隆与表征

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>The constitutive calcium/calmodulin-dependent nitric oxide (NO) synthase expressed in vascular endothelium shares common biochemical and pharmacologic properties with neuronal NO synthase. However, recent cloning and molecular characterization of NO synthase from bovine endothelial cells indicated the existence of a family of constitutive NO synthases. Accordingly, we undertook molecular cloning and sequence analysis of human endothelial NO synthase. Complementary DNA clones predict a protein of 1,203 amino acids sharing 94% identity with the bovine endothelial protein, but only 60% identity with the rat brain NO synthase isoform. Northern blot analysis with an endothelial-derived cDNA identified a 4.6–4.8 kb mRNA transcript in HUVEC and in situ hybridization localized transcripts to vascular endothelium but not neuronal tissue.
机译:>在血管内皮中表达的组成型钙/钙调蛋白依赖性一氧化氮(NO)合酶与神经元NO合酶具有共同的生化和药理特性。然而,最近从牛内皮细胞中克隆和合成NO合酶的分子特征表明存在一类组成型NO合酶。因此,我们进行了人内皮一氧化氮合酶的分子克隆和序列分析。互补的DNA克隆预测一种1,203个氨基酸的蛋白质与牛内皮蛋白具有94%的同一性,但与大鼠脑NO合酶同种型只有60%的同一性。用内皮衍生的cDNA进行Northern印迹分析时,在HUVEC中发现了一个4.6–4.8 kb的mRNA转录本,并且原位杂交将转录本定位到了血管内皮,但未检测到神经元组织。

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