cDNA and protein sequence, genomic organization, and analysis of cis regulatory elements of mouse and human PLVAP genes

PV-1 is a novel protein component of the endothelial fenestral and stomatal diaphragms. PV-1 cDNA and protein sequences are highly conserved across sp ecies. The conserved extracellular domain features found in rat, mouse, and human PV-1 protein are four N-glycosylation sites, two coiled-coil domains , a proline-rich region, and even cysteine spacing. No consensus site in th e intracellular domain was found. Northern blotting of mouse and human tiss ues is in agreement with and expands those performed in rat and correlated well with the postulated presence of PV-1 in the endothelial diaphragms. Th e genomic organization of the human and mouse genes (HGMW-approved symbol P LVAP) has been determined, and the analysis of their 5' flanking regions ha s found a highly conserved classical TATA-driven promoter that shows severa l transcription factor consensus binding sites. Radiation hybrid panel mapp ing has localized the human and mouse PLVAP genes to chromosomes 19p13.2 an d 8B3-C1, respectively, (C) 2001 Academic Press.