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CXC chemokines in angiogenesis
Author(s) -
Belperio John A.,
Keane Michael P.,
Arenberg Douglas A.,
Addison Christina L.,
Ehlert Jan E.,
Burdick Marie D.,
Strieter Robert M.
Publication year - 2000
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.68.1.1
Subject(s) - angiogenesis , chemokine , biology , cysteine , biochemistry , amino acid , peptide sequence , cxc chemokine receptors , genetics , gene , enzyme , chemokine receptor , receptor
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 NH 2 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.