Abstract
Two forms of monocyte chemoattractant protein-1 (MCP-1), MCP-lα and β have been purified from culture supernatants of either human malignant glioma cell line cells or PHA-stimulated peripheral blood mononuclear leukocytes. MCP-1 is chemotactic for monocytes but not for neutrophils, and appears to be identical to lymphocyte-derived chemotactic factor reported previously by others in an early era of lymphokine research. Amino acid sequence analysis and cDNA cloning have revealed that MCP-1 belongs to a family of proteins characterized by the location of 4 cysteins. Among those, mouse JE which was defined as a clone expressed by PDGF-stimulated fibroblasts has the highest similarity to MCP-1, suggesting that MCP-1 is a human homologue of mouse JE.Recently human JE has been cloned and found to be identical to MCP-1. Furthermore, human fibroblasts are capable to produce MCP-1 and the production is regulated by PDGF. From these results, it is highly possible that MCP-1 is identical to JE and this protein may play an important role in macrophage infiltration in vivo.
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