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大鼠肠神经系统中血管活性肠肽原的替代加工途径

Alternative processing pathways for preprovasoactive intestinal peptide in the enteric nervous system of the rat.

作者信息

Dimaline R, Vowles L

机构信息

MRC Secretory Control Group, University of Liverpool, U.K.

出版信息

Regul Pept. 1988 Mar;20(3):199-210. doi: 10.1016/0167-0115(88)90076-6.

Abstract

In order to study biosynthetic processing of preprovasoactive intestinal peptide (prepro VIP) we have raised antisera to sequences that flank the biologically active peptides VIP and PHI (peptide with N-terminal His and C-terminal Ile). We have used these antisera in radioimmunoassays to identify the N-terminal flanking peptide (NFP) and C-terminal flanking peptide (CFP)-like immunoreactivities in rat brain and gastrointestinal tract. Concentrations of NFP-LI were similar to those of VIP in brain and throughout the gut. Concentrations of CFP-LI were 10-20% those of VIP-LI but could be increased 5-fold by digestion with carboxypeptidase B, suggesting that the C-terminal lysine residue of prepro VIP is not normally removed during processing. In rat stomach the NFP-LI was of higher molecular weight and greater hydrophobicity than the intestinal component. The data are consistent with alternative processing pathways for prepro VIP in enteric nerves of rat stomach and intestine.

摘要

为了研究血管活性肠肽原(prepro VIP)的生物合成过程,我们制备了针对生物活性肽VIP和PHI(N端为组氨酸、C端为异亮氨酸的肽)两侧序列的抗血清。我们利用这些抗血清进行放射免疫分析,以鉴定大鼠脑和胃肠道中N端侧翼肽(NFP)和C端侧翼肽(CFP)样免疫反应性。NFP-LI在脑和整个肠道中的浓度与VIP相似。CFP-LI的浓度为VIP-LI的10%-20%,但用羧肽酶B消化后可增加5倍,这表明prepro VIP的C端赖氨酸残基在加工过程中通常不会被去除。在大鼠胃中,NFP-LI的分子量比肠道成分更高,疏水性更强。这些数据与大鼠胃和肠的肠神经中prepro VIP的不同加工途径一致。

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