Georgia Deliconstantinos1, Stephen Barton2, Mikhail Soloviev3, Nigel Page4. 1. School of Life Sciences, Kingston University, London, U.K. ginadeli@hotmail.com. 2. School of Pharmacy & Chemistry, Kingston University, London, U.K. 3. School of Biological Sciences, Royal Holloway University of London, London, U.K. 4. School of Life Sciences, Kingston University, London, U.K.
Abstract
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 anti-tachykinin-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. Copyright
BACKGROUND/AIM: The tachykinin mouse hemokinin-1, expressed by the mouseTac4 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 anti-tachykinin-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. Copyright
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