title: Isolation of ALP, a novel divergent murine CC chemokine with a unique carboxy terminal extension.
abstract: Chemokines are a family of related proteins that regulate leukocyte infiltration into inflamed tissue and play important roles in many disease processes. Chemokines are divided into two major groups, CC or CXC, based on their sequence around the amino terminal cysteines. We report here, the isolation of a novel murine CC chemokine termed ALP for its amino terminal peptide sequence. This novel chemokine is distantly related to other CC chemokines (37% identity with murine Exodus-1/LARC/Mip-3alpha), but has a unique carboxy terminal extension. It is expressed preferentially in testis, heart, and liver, which is atypical for CC chemokines.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D054425:Chemokine CCL27; D019742:Chemokines, CC / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D002633:Chemotaxis; D006801:Humans; D008099:Liver / Q000378:metabolism; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D009206:Myocardium / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013737:Testis / Q000378:metabolism