TAILIEUCHUNG - Báo cáo khoa học: Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-a

Fibroblast activation protein-a(FAP) is a cell surface-expressed and solu-ble enzyme of the prolyl oligopeptidase family, which includes dipeptidyl peptidase 4 (DPP4). FAP is not generally expressed in normal adult tissues, but is found at high levels in activated myofibroblasts and hepatic stellate cells in fibrosis and in stromal fibroblasts of epithelial tumours. | IFEBS Journal Neuropeptide Y B-type natriuretic peptide substance P and peptide YY are novel substrates of fibroblast activation protein-a Fiona M. Keane1 Naveed A. Nadvi1 2 Tsun-Wen Yao1 and Mark D. Gorrell1 1 Centenary Institute Sydney MedicalSchool University of Sydney NSW Australia 2 PharmaceuticalChemistry Faculty of Pharmacy University of Sydney NSW Australia Keywords antiplasmin-cleaving enzyme chemokine dipeptidyl peptidase incretin MALDI-TOF MS Correspondence M. D. Gorrell Molecular Hepatology Centenary Institute Locked Bag No. 6 Newtown NSW 2042 Australia Fax 61 2 95656101 Tel 61 2 95656156 E-mail Received 24 November 2010 revised 4 February 2011 accepted 9 February 2011 doi Fibroblast activation protein-a FAP is a cell surface-expressed and soluble enzyme of the prolyl oligopeptidase family which includes dipeptidyl peptidase 4 DPP4 . FAP is not generally expressed in normal adult tissues but is found at high levels in activated myofibroblasts and hepatic stellate cells in fibrosis and in stromal fibroblasts of epithelial tumours. FAP possesses a rare catalytic activity hydrolysis of the post-proline bond two or more residues from the N-terminus of target substrates. a2-antiplasmin is an important physiological substrate of FAP endopeptidase activity. This study reports the first natural substrates of FAP dipeptidyl peptidase activity. Neuropeptide Y B-type natriuretic peptide substance P and peptide YY were the most efficiently hydrolysed substrates and the first hormone substrates of FAP to be identified. In addition FAP slowly hydrolysed other hormone peptides such as the incretins glucagon-like peptide-1 and glucose-dependent insulinotropic peptide which are efficient DPP4 substrates. FAP showed negligible or no hydrolysis of eight chemo-kines that are readily hydrolysed by DPP4. This novel identification of FAP substrates furthers our understanding of this unique protease by indicating

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