| Fondo | Prolyl endopeptidase FAP is a ~87 kDa protein. Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein. Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). 3. Edosada, CY. et al. (2006) The Journal of biological chemistry 281, 7437-44. PMID: 164102484. Edosada, CY. et al. (2006) FEBS letters 580, 1581-6. PMID: 164807185. Meadows, SA. et al. (2007) Biochemistry 46, 4598-605. PMID: 173810736. Aggarwal, S. et al. (2008) Biochemistry 47, 1076-86. PMID: 180957117. Huang, CH. et al. (2011) Journal of biochemistry 149, 685-92. PMID: 212888889. Levy, MT. et al. (1999) Hepatology (Baltimore, Md.) 29, 1768-78. PMID: 1034712010. Mueller, SC. et al. (1999) The Journal of biological chemistry 274, 24947-52. PMID: 10455171 |
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