Bovine urokinase-type plasminogen activator and its receptor: cloning and induction by retinoic acid

Abstract

Full-length cDNAs encoding bovine urokinase-type plasminogen activator (u-PA) and urokinase receptor (u-PAR) were cloned from an aortic endothelial cell cDNA library using PCR-amplified cDNA fragments as probes. Bovine u-PA amino acid identity ranges from 79.5 to 70.9% when compared to its pig, human, baboon and mouse analogues, while bovine u-PAR is 61.8 and 59.6% identical to its human and mouse counterparts, respectively. All Cys residues previously found in mature u-PA and u-PAR from these different species are also conserved in the bovine molecules. Bovine u-PA and its cell-surface receptor display one and six potential sites of N-linked glycosylation, respectively. Northern blot hybridization demonstrated a moderate induction of u-PA and u-PAR mRNA in bovine aortic endothelial cells after treatment with 10 nM and 1 microM retinoic acid for 8 hours.