| First Author | Altieri DC | Year | 1994 |
| Journal | J Biol Chem | Volume | 269 |
| Issue | 5 | Pages | 3139-42 |
| PubMed ID | 8106347 | Mgi Jnum | J:16702 |
| Mgi Id | MGI:64766 | Doi | 10.1016/s0021-9258(17)41838-2 |
| Citation | Altieri DC (1994) Molecular cloning of effector cell protease receptor-1, a novel cell surface receptor for the protease factor Xa. J Biol Chem 269(5):3139-42 |
| abstractText | Cellular receptors for blood proteases regulate chemotaxis, extracellular proteolysis, and growth behavior of normal and malignant cells. Binding of the coagulation protease factor Xa to leukocytes is contributed by a recently identified molecule, denominated Effector cell Protease Receptor-1 (EPR-1). Monoclonal antibodies were generated against EPR-1+ MOLT13 lymphocytes and selected for reactivity with lymphocyte surface proteins by flow cytometry and with affinity-purified EPR-1 in Western blots. Antibody-based functional cloning of the cDNA for EPR-1 reveals the sequence of a novel molecule encoded by a prominent 1.9-kilobase mRNA. The cDNA predicts a glycoprotein of 337 amino acids, characterized by a unique cysteine-rich extracellular module, a single membrane-spanning domain, and a serine-rich (26%) cytoplasmic tail featuring at least 15 potential phosphorylation sites. Genetically engineered EPR-1 transfectants were recognized by monoclonal antibodies to EPR-1 and bound 125I-factor Xa in a specific and saturable manner (Kd approximately 10-15 nM). In the absence of factor V/Va, EPR-1 transfectants promoted prothrombin activation in a factor Xa concentration-dependent reaction, inhibited by a monoclonal antibody to EPR-1. These findings define EPR-1 as a novel cell surface receptor for factor Xa potentially implicated in protease-dependent cellular effector functions. |
