Molecular cloning and characterization of a novel human CC chemokine, SCYA26

By searching the Expressed Sequence Tag database, a full-length cDNA for a novel human CC chemokine was cloned. This cDNA encoded a 94-amino-acid prot ein with a putative signal peptide of 26 amino acids. The deduced mature pr otein had the four conserved cysteine residues characteristic of CC chemoki nes and showed 44% identity with MIP-1 beta and 40% identity with MIP-1 alp ha, RANTES, and MCP-4. mRNA for this chemokine was expressed constitutively in human heart and liver and with lesser but detectable levels in skeletal muscle, kidney, and small intestine. To investigate its biological activit y, the protein was expressed in mammalian cells and purified by affinity ch romatography. The recombinant protein demonstrated chemotactic activity in vit ro for T cells and monocytes but not for neutrophils. The gene was mapp ed to chromosome 7q11.2 by fluorescence in situ hybridization. Based on its structural identity with other CC chemokines and the chemotactic activity and chromosomal location of this chemokine, we designate this chemokine sma ll inducible cytokine subfamily A, member 26 (SCYA26). This gene symbol has been approved by the HUGO Gene Nomenclature Committee. (C) 1999 Academic P ress.