Abstract
Although it is known that neutrophils infiltrate damaged sites immediately after tissue injury, the endogenous factors that induce their acute transmigration and activation have not been thoroughly investigated. For the candidates of those factors, we recently discovered two novel neutrophil-activating cryptides, mitocryptide-1 (MCT-1) and mitocryptide-2 (MCT-2), hidden in mitochondrial proteins. In addition, many unknown neutrophil-activating peptides other than MCT-1 and MCT-2 were also observed during their purification. Here, we isolated and purified a novel neutrophil-activating peptide from porcine hearts, which we showed by structural analyses to have an identical primary structure to porcine mitochondrial cytochrome c (68-85). We named this novel functional octadecapeptide as mitocryptide-CYC (MCT-CYC). Structure-activity relationships of cytochrome c on β-hexosaminidase (β-HA) release from neutrophilic-differentiated HL- 60 cells demonstrated that peptides derived from the C-terminal part of cytochrome c induced β-HA release and that cytochrome c (70-85) was the most potent cryptide among them. Since cytochrome c is known to be involved in the apoptotic process, our results suggest that cryptides, including MCT-CYC, derived from mitochondrial cytochrome c are possible factors that induce scavenging of toxic debris produced from apoptotic cells by neutrophils.
Keywords: Cryptide, cytochrome c, mitochondria, mitocryptide-1, mitocryptide-2, mitocryptide-CYC, neutrophil, arboxypeptidases, neutrophil-activating peptide, Peptidergic neurotransmitters
Protein & Peptide Letters
Title:Isolation and Identification of Novel Neutrophil-Activating Cryptides Hidden in Mitochondrial Cytochrome c
Volume: 19 Issue: 6
Author(s): Yoshinori Hokari, Tetsuo Seki, Hiroko Nakano, Yuko Matsuo, Akiyoshi Fukamizu, Eisuke Munekata, Yoshiaki Kiso and Hidehito Mukai
Affiliation:
Keywords: Cryptide, cytochrome c, mitochondria, mitocryptide-1, mitocryptide-2, mitocryptide-CYC, neutrophil, arboxypeptidases, neutrophil-activating peptide, Peptidergic neurotransmitters
Abstract: Although it is known that neutrophils infiltrate damaged sites immediately after tissue injury, the endogenous factors that induce their acute transmigration and activation have not been thoroughly investigated. For the candidates of those factors, we recently discovered two novel neutrophil-activating cryptides, mitocryptide-1 (MCT-1) and mitocryptide-2 (MCT-2), hidden in mitochondrial proteins. In addition, many unknown neutrophil-activating peptides other than MCT-1 and MCT-2 were also observed during their purification. Here, we isolated and purified a novel neutrophil-activating peptide from porcine hearts, which we showed by structural analyses to have an identical primary structure to porcine mitochondrial cytochrome c (68-85). We named this novel functional octadecapeptide as mitocryptide-CYC (MCT-CYC). Structure-activity relationships of cytochrome c on β-hexosaminidase (β-HA) release from neutrophilic-differentiated HL- 60 cells demonstrated that peptides derived from the C-terminal part of cytochrome c induced β-HA release and that cytochrome c (70-85) was the most potent cryptide among them. Since cytochrome c is known to be involved in the apoptotic process, our results suggest that cryptides, including MCT-CYC, derived from mitochondrial cytochrome c are possible factors that induce scavenging of toxic debris produced from apoptotic cells by neutrophils.
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Hokari Yoshinori, Seki Tetsuo, Nakano Hiroko, Matsuo Yuko, Fukamizu Akiyoshi, Munekata Eisuke, Kiso Yoshiaki and Mukai Hidehito, Isolation and Identification of Novel Neutrophil-Activating Cryptides Hidden in Mitochondrial Cytochrome c, Protein & Peptide Letters 2012; 19 (6) . https://dx.doi.org/10.2174/092986612800494048
DOI https://dx.doi.org/10.2174/092986612800494048 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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