dc.contributor.author | Sarmiento, J. | |
dc.contributor.author | Shumate, C. | |
dc.contributor.author | Suetomi, K. | |
dc.contributor.author | Ravindran, A. | |
dc.contributor.author | Villegas, L. | |
dc.contributor.author | Rajarathnam, K. | |
dc.contributor.author | Navarro, J. | |
dc.date.accessioned | 2022-01-18T19:34:39Z | |
dc.date.available | 2022-01-18T19:34:39Z | |
dc.date.issued | 2011 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12866/11096 | |
dc.description.abstract | CXCL8/interleukin-8 is a pro-inflammatory chemokine that triggers pleiotropic responses, including inflammation, angiogenesis, wound healing and tumorigenesis. We engineered the first selective CXCR1 agonists on the basis of residue substitutions in the conserved ELR triad and CXC motif of CXCL8. Our data reveal that the molecular mechanisms of activation of CXCR1 and CXCR2 are distinct: the N-loop of CXCL8 is the major determinant for CXCR1 activation, whereas the N-terminus of CXCL8 (ELR and CXC) is essential for CXCR2 activation. We also found that activation of CXCR1 cross-desensitized CXCR2 responses in human neutrophils co-expressing both receptors, indicating that these novel CXCR1 agonists represent a new class of anti-inflammatory agents. Further, these selective CXCR1 agonists will aid at elucidating the functional significance of CXCR1 in vivo under pathophysiological conditions. | en_US |
dc.language.iso | eng | |
dc.publisher | Public Library of Science | |
dc.relation.ispartofseries | PLoS ONE | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/deed.es | |
dc.subject | Humans | en_US |
dc.subject | controlled study | en_US |
dc.subject | animal cell | en_US |
dc.subject | metabolism | en_US |
dc.subject | non protein expression | en_US |
dc.subject | unclassified drug | en_US |
dc.subject | human cell | en_US |
dc.subject | cytology | en_US |
dc.subject | Protein Binding | en_US |
dc.subject | interleukin 8 | en_US |
dc.subject | Models, Molecular | en_US |
dc.subject | chemistry | en_US |
dc.subject | drug potentiation | en_US |
dc.subject | neutrophil | en_US |
dc.subject | calcium | en_US |
dc.subject | protein structure | en_US |
dc.subject | rabbit | en_US |
dc.subject | amino acid substitution | en_US |
dc.subject | protein motif | en_US |
dc.subject | Neutrophils | en_US |
dc.subject | antiinflammatory agent | en_US |
dc.subject | Chemokines | en_US |
dc.subject | chemical structure | en_US |
dc.subject | amino terminal sequence | en_US |
dc.subject | Calcium | en_US |
dc.subject | cell strain HL 60 | en_US |
dc.subject | chemokine receptor agonist | en_US |
dc.subject | chemokine receptor CXCR1 | en_US |
dc.subject | chemokine receptor CXCR1 agonist | en_US |
dc.subject | chemokine receptor CXCR2 | en_US |
dc.subject | chemokine receptor CXCR2 agonist | en_US |
dc.subject | Endocytosis | en_US |
dc.subject | HL-60 Cells | en_US |
dc.subject | Mutant Proteins | en_US |
dc.subject | Protein Engineering | en_US |
dc.subject | Receptors, Chemokine | en_US |
dc.subject | Receptors, Interleukin-8A | en_US |
dc.subject | skin inflammation | en_US |
dc.title | Diverging mechanisms of activation of chemokine receptors revealed by novel chemokine agonists | en_US |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | https://doi.org/10.1371/journal.pone.0027967 | |
dc.subject.ocde | https://purl.org/pe-repo/ocde/ford#3.01.00 | |
dc.relation.issn | 1932-6203 |
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