Miller Allison L, Verma Deepti, Grinninger Carola, Huang Mei-Chuan, Goetzl Edward J
Department of Medicine, University of California Medical Center, Room UB8B, UC Box 0711, 533 Parnassus at 4th, San Francisco, CA 94143-0711, USA.
Ann N Y Acad Sci. 2006 Jul;1070:422-6. doi: 10.1196/annals.1317.055.
A PCR-based search for splice variants of the VPAC2 G protein-coupled receptor for vasoactive intestinal peptide (VIP) revealed: (a) a short-deletion variant in mouse lymphocytes termed VPAC2de367-380, that lacks 14 amino acids in the seventh transmembrane domain, and (b) a long-deletion variant in human lymphocytes termed VPAC2de325-438(i325-334), that lacks 114 amino acids beginning with the carboxyl-terminal end of the third cytoplasmic loop and has 10 new carboxy-terminal amino acids. VPAC2de367-380 binds VIP normally, but shows reduced VIP-evoked signaling and effects on immune functions, whereas VPAC2de325-438(i325-334) shows reduced binding affinity for VIP and a complex pattern of functional differences. These splice variants may modify the immunoregulatory contributions of the VIP-VPAC2 axis.
一项基于聚合酶链反应（PCR）的对血管活性肠肽（VIP）的VPAC2 G蛋白偶联受体剪接变体的研究发现：（a）在小鼠淋巴细胞中存在一种短缺失变体，称为VPAC2de367 - 380，它在第七跨膜结构域中缺少14个氨基酸；（b）在人淋巴细胞中存在一种长缺失变体，称为VPAC2de325 - 438（i325 - 334），它从第三个细胞质环的羧基末端开始缺少114个氨基酸，并具有10个新的羧基末端氨基酸。VPAC2de367 - 380能正常结合VIP，但显示出VIP诱导的信号传导减少以及对免疫功能的影响减弱，而VPAC2de325 - 438（i325 - 334）对VIP的结合亲和力降低，并且具有复杂的功能差异模式。这些剪接变体可能会改变VIP - VPAC2轴的免疫调节作用。
