Deliconstantinos Georgia, Barton Stephen, Soloviev Mikhail, Page Nigel
School of Life Sciences, Kingston University, London, U.K.
School of Pharmacy & Chemistry, Kingston University, London, U.K.
In Vivo. 2017 Sep-Oct;31(5):991-998. doi: 10.21873/invivo.11159.
BACKGROUND/AIM: The tachykinin mouse hemokinin-1, expressed by the mouse Tac4 gene, produces either analgesia or nociception, interacting with the neurokinin 1 receptor. TAC4 precursor processing is not identical to the processing of the TAC1 precursor, for the release of substance P (amidated undecapeptide). The characterization of the mouse hemokinin-1 sequence was required.
We developed anti-tachykinin-specific antibodies for the immunoaffinity purification of tachykinins.
Using MALDI-ToF, we identified mouse hemokinin-1 as an amidated decapeptide expressed in murine brain and periphery. Furthermore, we interestingly observed an additional mass peak corresponding to acetylated mouse hemokinin-1 and this post-translational modification is brain-specific, not detected in the periphery.
We suggest that the N-terminal acetylation of the peptide provides greater potency for ligand-receptor interactions during neural cell signaling.
背景/目的:由小鼠Tac4基因表达的速激肽小鼠血激肽-1,与神经激肽1受体相互作用,可产生镇痛或伤害感受作用。TAC4前体的加工过程与TAC1前体不同,后者可释放P物质(酰胺化十一肽)。需要对小鼠血激肽-1序列进行表征。
我们开发了抗速激肽特异性抗体,用于速激肽的免疫亲和纯化。
使用基质辅助激光解吸电离飞行时间质谱(MALDI-ToF),我们鉴定出小鼠血激肽-1为一种在小鼠脑和外周表达的酰胺化十肽。此外,我们有趣地观察到一个对应于乙酰化小鼠血激肽-1的额外质量峰,这种翻译后修饰具有脑特异性,在外周未检测到。
我们认为该肽的N端乙酰化在神经细胞信号传导过程中为配体-受体相互作用提供了更高的效力。