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Articles by Michael Gabl
Staphylococcus aureus-Derived PSMα Peptides Activate Neutrophil FPR2 but Lack the Ability to Mediate β-Arrestin Recruitment and Chemotaxis
Martina Sundqvist, Karin Christenson, Michael Gabl, André Holdfeldt, Karin Jennbacken, Thor C. Møller, Claes Dahlgren and Huamei Forsman J Immunol December 15, 2019, 203 (12) 3349-3360; DOI: https://doi.org/10.4049/jimmunol.1900871 Key Points FPR2-specific PSMα peptides are not chemotactic but activate the NADPH oxidase. PSMα peptides induce ERK1/2 phosphorylation but not β-arrestin recruitment.
Staphylococcus aureus-Derived PSMα Peptides Activate Neutrophil FPR2 but Lack the Ability to Mediate β-Arrestin Recruitment and Chemotaxis
Martina Sundqvist, Karin Christenson, Michael Gabl, André Holdfeldt, Karin Jennbacken, Thor C. Møller, Claes Dahlgren and Huamei Forsman J Immunol November 6, 2019, ji1900871; DOI: https://doi.org/10.4049/jimmunol.1900871 Key Points FPR2-specific PSMα peptides are not chemotactic but activate the NADPH oxidase. PSMα peptides induce ERK1/2 phosphorylation but not β-arrestin recruitment.
Identification of Residues Critical for FPR2 Activation by the Cryptic Peptide Mitocryptide-2 Originating from the Mitochondrial DNA-Encoded Cytochrome b | The Journal of Immunology
Simon Lind, Michael Gabl, André Holdfeldt, Jonas Mårtensson, Martina Sundqvist, Kodai Nishino, Claes Dahlgren, Hidehito Mukai and Huamei Forsman J Immunol May 1, 2019, 202 (9) 2710-2719; DOI: https://doi.org/10.4049/jimmunol.1900060 Key Points Critical structural elements are identified in MCT-2 that mediate FPR2 activation. MCT-2 polymorphic variants activate human neutrophils with different potency.
Identification of Residues Critical for FPR2 Activation by the Cryptic Peptide Mitocryptide-2 Originating from the Mitochondrial DNA-Encoded Cytochrome b | The Journal of Immunology
Simon Lind, Michael Gabl, André Holdfeldt, Jonas Mårtensson, Martina Sundqvist, Kodai Nishino, Claes Dahlgren, Hidehito Mukai and Huamei Forsman J Immunol March 22, 2019, ji1900060; DOI: https://doi.org/10.4049/jimmunol.1900060 Key Points Critical structural elements are identified in MCT-2 that mediate FPR2 activation. MCT-2 polymorphic variants activate human neutrophils with different potency.
Mitocryptides from Human Mitochondrial DNA-Encoded Proteins Activate Neutrophil Formyl Peptide Receptors: Receptor Preference and Signaling Properties | The Journal of Immunology
Mitocryptides from Human Mitochondrial DNA–Encoded Proteins Activate Neutrophil Formyl Peptide Receptors: Receptor Preference and Signaling Properties Michael Gabl, Martina Sundqvist, Andre Holdfeldt, Simon Lind, Jonas Mårtensson, Karin Christenson, Takayuki Marutani, Claes Dahlgren, Hidehito Mukai, Huamei Forsman The Journal of Immunology May 1, 2018, 200 (9) 3269-3282; DOI: 10.4049/jimmunol.1701719
Mitocryptides from Human Mitochondrial DNA-Encoded Proteins Activate Neutrophil Formyl Peptide Receptors: Receptor Preference and Signaling Properties | The Journal of Immunology
Mitocryptides from Human Mitochondrial DNA–Encoded Proteins Activate Neutrophil Formyl Peptide Receptors: Receptor Preference and Signaling Properties Michael Gabl, Martina Sundqvist, Andre Holdfeldt, Simon Lind, Jonas Mårtensson, Karin Christenson, Takayuki Marutani, Claes Dahlgren, Hidehito Mukai, Huamei Forsman The Journal of Immunology March 30, 2018, ji1701719; DOI: 10.4049/jimmunol.1701719
The Lipidated Peptidomimetic Lau-((S)-Aoc)-(Lys-βNphe)6-NH2 Is a Novel Formyl Peptide Receptor 2 Agonist That Activates Both Human and Mouse Neutrophil NADPH Oxidase
Neutrophils expressing formyl peptide receptor 2 (FPR2) play key roles in host defense, immune regulation, and resolution of inflammation. Consequently, the search for FPR2-specific modulators has attracted much attention due to its therapeutic potential. Earlier described agonists for this receptor display potent activity for the human receptor (FPR2) but low activity for the mouse receptor orthologue (Fpr2), rendering them inapplicable in murine models of human disease.
The lipidated peptidomimetic Lau-[(S)-Aoc]-(Lys-βNphe)6-NH2 is a novel formyl peptide receptor 2 agonist that activates both human and mouse neutrophil NADPH-oxidase
Neutrophils expressing formyl peptide receptor 2 (FPR2) play key roles in host defense, immune regulation, and in resolution of inflammation. Consequently, the search for FPR2-specific modulators has attracted much attention due to its therapeutic potential. Earlier described agonists for this receptor display potent activity for the human receptor (FPR2) but low activity for the mouse receptor orthologue (Fpr2), rendering them inapplicable in murine models of human disease.
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