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CXC chemokines in angiogenesis

Journal of Leukocyte Biology · 2000 · Vol. 68(1) · pp. 1–8
John A. BelperioMichael P. KeaneDouglas A. ArenbergChristina AddisonJan E. EhlertMarie D. BurdickRobert M. Strieter

Abstract

A variety of factors have been identified that regulate angiogenesis, including the CXC chemokine family. The CXC chemokines are a unique family of cytokines for their ability to behave in a disparate manner in the regulation of angiogenesis. CXC chemokines have four highly conserved cysteine amino acid residues, with the first two cysteine amino acid residues separated by one non-conserved amino acid residue (i.e., CXC). A second structural domain within this family determines their angiogenic potential. The NH2 terminus of the majority of the CXC chemokines contains three amino acid residues (Glu-Leu-Arg: the ELR motif), which precedes the first cysteine amino acid residue of the primary structure of these cytokines. Members that contain the ELR motif (ELR+) are potent promoters of angiogenesis. In contrast, members that are inducible by interferons and lack the ELR motif (ELR-) are potent inhibitors of angiogenesis. This difference in angiogenic activity may impact on the pathogenesis of a variety of disorders.

Chemokine receptors and signalingCell Adhesion Molecules ResearchCytokine Signaling Pathways and InteractionsAngiogenesisChemokineBiologyCysteineBiochemistryAmino acidCXC chemokine receptorsPeptide sequenceGeneGenetics

MeSH terms

AnimalsArthritis, RheumatoidChronic DiseaseFibrosisHumansInflammationMice, NudeNeoplasm ProteinsNeoplasmsNeovascularization, PathologicPulmonary FibrosisStructure-Activity RelationshipInterleukin-8Neovascularization, PhysiologicReceptors, Chemokine

Funding

  • National Institutes of Health
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807
FWCI
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