Smit A B, Geraerts P M, Meester I, van Heerikhuizen H, Joosse J
Department of Biology, Vrije Universiteit, Amsterdam, The Netherlands.
Eur J Biochem. 1991 Aug 1;199(3):699-703. doi: 10.1111/j.1432-1033.1991.tb16173.x.
A cDNA clone encoding molluscan insulin-related peptide (MIP) II was isolated from a cDNA library of the central nervous system (CNS) of the freshwater snail, Lymnaea stagnalis, using a heterologous screening with a previously identified MIP cDNA (renamed MIP-I cDNA). The MIP-II cDNA encodes a preprohormone resembling the organization of preproinsulin, with a putative signal sequence, and A and B chains; however, in this case connected by two distinct C peptides, C alpha and C beta, instead of a single C peptide, a phenomenon which represents a new development in the prohormone organization of peptides belonging to the insulin superfamily. The A and B chains of MIP II and I differ remarkably in primary structure; in contrast, the C alpha peptide domains are fully identical. MIP II has only limited sequence similarity with insulins and related peptides. Both MIP II and I exhibit structural features, which make them a unique class of the insulin superfamily. The MIP I and II genes are expressed in a single type of neuron: the growth-controlling neuroendocrine light green cells of the Lymnaea CNS.
利用先前鉴定的MIP cDNA(重新命名为MIP-I cDNA)进行异源筛选,从淡水螺椎实螺(Lymnaea stagnalis)中枢神经系统(CNS)的cDNA文库中分离出一个编码软体动物胰岛素相关肽(MIP)II的cDNA克隆。MIP-II cDNA编码一种前激素原,其结构类似于胰岛素原,具有一个假定的信号序列以及A链和B链;然而,在这种情况下,A链和B链由两个不同的C肽(Cα和Cβ)连接,而不是单个C肽,这种现象代表了胰岛素超家族肽类前激素结构的新发展。MIP II和I的A链和B链在一级结构上有显著差异;相比之下,Cα肽结构域完全相同。MIP II与胰岛素及相关肽的序列相似性有限。MIP II和I都具有一些结构特征,这使它们成为胰岛素超家族中独特的一类。MIP I和II基因在一种单一类型的神经元中表达:椎实螺CNS中控制生长的神经内分泌浅绿细胞。