摘要

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. Materials and Methods: We developed antitachykinin- specific antibodies for the immunoaffinity purification of tachykinins. Results: 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. Conclusion: We suggest that the N-terminal acetylation of the peptide provides greater potency for ligand-receptor interactions during neural cell signaling.

  • 出版日期2017-10

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