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Mitocryptides from Human Mitochondrial DNA-Encoded Proteins Activate Neutrophil Formyl Peptide Receptors: Receptor Preference and Signaling Properties.

Artikel i vetenskaplig tidskrift
Författare Michael Gabl
Martina Sundqvist
André Holdfeldt
Simon Lind
Jonas Mårtensson
Karin Christenson
Takayuki Marutani
Claes Dahlgren
Hidehito Mukai
Huamei Forsman
Publicerad i Journal of immunology
Volym 200
Nummer/häfte 9
Sidor 3269-3282
ISSN 1550-6606
Publiceringsår 2018
Publicerad vid Institutionen för odontologi
Institutionen för medicin, avdelningen för reumatologi och inflammationsforskning
Sidor 3269-3282
Språk en
Länkar dx.doi.org/10.4049/jimmunol.1701719
www.ncbi.nlm.nih.gov/entrez/query.f...
Ämneskategorier Medicinsk cellbiologi

Sammanfattning

Phagocytic neutrophils express formyl peptide receptors (FPRs; FPR1 and FPR2) that distinctly recognize peptides starting with an N-formylated methionine (fMet). This is a hallmark of bacterial metabolism; similar to prokaryotes, the starting amino acid in synthesis of mitochondrial DNA-encoded proteins is an fMet. Mitochondrial cryptic peptides (mitocryptides; MCTs) with an N-terminal fMet could be identified by our innate immune system; however, in contrast to our knowledge about bacterial metabolites, very little is known about the recognition profiles of MCTs. In this study, we determined the neutrophil-recognition profiles and functional output of putative MCTs originating from the N termini of the 13 human mitochondrial DNA-encoded proteins. Six of the thirteen MCTs potently activated neutrophils with distinct FPR-recognition profiles: MCTs from ND3 and ND6 have a receptor preference for FPR1; MCTs from the proteins ND4, ND5, and cytochromebprefer FPR2; and MCT-COX1 is a dual FPR1/FPR2 agonist. MCTs derived from ND2 and ND4L are very weak neutrophil activators, whereas MCTs from ND1, ATP6, ATP8, COX2, and COX3, do not exert agonistic or antagonistic FPR effects. In addition, the activating MCTs heterologously desensitized IL-8R but primed the response to the platelet-activating factor receptor agonist. More importantly, our data suggest that MCTs have biased signaling properties in favor of activation of the superoxide-generating NADPH oxidase or recruitment of β-arrestin. In summary, we identify several novel FPR-activating peptides with sequences present in the N termini of mitochondrial DNA-encoded proteins, and our data elucidate the molecular basis of neutrophil activation by MCTs.

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