Larsson B, Phillips S C
Department of Clinical Pharmacology, Lund University Hospital, Lund, Sweden.
Biochem Biophys Res Commun. 1998 Oct 29;251(3):898-902. doi: 10.1006/bbrc.1998.9578.
A splice variant of nNOS has recently been identified in both rat and mouse which contains an in-frame insertion of 34 conserved amino acids between the N-terminal oxygenase and the C-terminal reductase domains. In the present study we report the isolation and characterization of a similar, but not identical (76% amino acid identity), human variant (nNOSmu) which arises from the splicing in of an additional exon between exons 16 and 17 of the human nNOS gene. Furthermore, we describe two additional splice variants which, if translated, would give rise to truncated forms of nNOS lacking the C-terminal reductase domain. These additional variants and nNOSmu; have a distinct and more restricted expression pattern compared to nNOS. Further studies are required to elucidate the possible physiological roles of these novel human nNOS splice variants in NO signaling.
最近在大鼠和小鼠中均鉴定出一种nNOS剪接变体，该变体在N端加氧酶和C端还原酶结构域之间含有34个保守氨基酸的框内插入。在本研究中，我们报告了一种相似但不完全相同（氨基酸同一性为76%）的人类变体（nNOSmu）的分离和特征，该变体是由于人类nNOS基因第16和17外显子之间额外一个外显子的剪接插入而产生的。此外，我们描述了另外两种剪接变体，如果进行翻译，将产生缺乏C端还原酶结构域的nNOS截短形式。与nNOS相比，这些额外的变体和nNOSmu具有独特且更受限的表达模式。需要进一步研究以阐明这些新型人类nNOS剪接变体在NO信号传导中可能的生理作用。
