文摘
We report the identification, structural characterization, and mapping of the humanFIGFgene.FIGFis the human homologue of mousefigf(c-fos-induced growth factor), a new member of the platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family. It codes for a secreted factor with mitogenic and morphogenic activity on fibroblast cells. The predicted amino acid sequence ofFIGFis 84 % identical to that of the mouse protein, and it is highly conserved (up to 40 % ) in the dimerization domain with respect to the VEGF members of the family. The 2.5-kb mRNA ofFIGFwas detected in adult lung and heart tissues. The gene spans about 50 kb and is organized into seven exons and six introns. TheFIGFpromoter contains an optimal AP-1-binding site and lacks a canonical TATA box. Fluorescencein situhybridization mappedFIGFto chromosomal region Xp22.1. The subsequent identification of YAC positive clones from this region allowed us to refine the map and localizeFIGFcentromeric to the phosphatidylinositol glycan complementation class A (PIGA) gene and telomeric to the gastrin-releasing peptide receptor (GRPR) gene.FIGFandPIGAgenes lie next to each other in a head-to-tail orientation, with theFIGFpolyadenylation signal about 12 kb from thePIGAtranscriptional start site.