Molecular Cloning and Functional Characterization of Human MIP-1δ, a New C–C Chemokine Related to Mouse CCF-18 and C10
- Cite this article as:
- Wang, W., Bacon, K.B., Oldham, E.R. et al. J Clin Immunol (1998) 18: 214. doi:10.1023/A:1020535106684
- 35 Downloads
We have isolated a novel human C–C chemokine, MIP-1δ, from a human fetal spleen cDNA library. The human MIP-1δ cDNA has an unusually long 400-bp 5-prime untranslated region and a predicted 113-amino acid protein of 10 kDa. The coding sequence contains a signal peptide of 21 amino acids, indicating that the mature protein has 92 amino acids (8 kDa). Recombinant human MIP-1δ produced by transfected human embryonic kidney 293 cells produced an 8-kDa protein, which confirmed the presence of a signal peptide. Compared with other human C–C chemokines, human MIP-1δ shows the highest homology with human HCC-1, CKβ-8, murine C10, and CCF18 (MIP-1γ). The human MIP-1δ gene is localized on chromosome 17 where most of the C–C chemokine superfamily is located. Human MIP-1δ is expressed in T and B lymphocytes, NK cells, monocytes, and monocyte-derived dendritic cells, but not in bone marrow-derived dendritic cells. Its expression can be induced by other proinflammatory cytokines in monocytes and dendritic cells. Human MIP-1δ is chemotactic for T cells and monocytes, but not for neutrophils, eosinophils, or B cells. Human MIP-1δ induced calcium flux in human CCR1-transfected cells.