TAILIEUCHUNG - Báo cáo khoa học: Degradation of tropoelastin by matrix metalloproteinases – cleavage site specificities and release of matrikines

To provide a basis for the development of approaches to treat elastin-degrading diseases, the aim of this study was to investigate the degradation of the natural substrate tropoelastin by the elastinolytic matrix metallopro-teinases MMP-7, MMP-9, and MMP-12 and to compare the cleavage site specificities of the enzymes using complementary MS techniques and molec-ular modeling. | Degradation of tropoelastin by matrix metalloproteinases -cleavage site specificities and release of matrikines Andrea Heinz1 Michael C. Jung1 Laurent Duca2 Wolfgang Sippl1 Samuel Taddese1 Christian Ihling1 Anthony Rusciani2 Gunther Jahreis3 Anthony S. Weiss4 Reinhard H. H. Neubert1 and Christian E. H. Schmelzer1 1 Institute of Pharmacy Martin Luther University Halle-Wittenberg Halle Saale Germany 2 Faculte des Sciences Laboratoire de Biochimie Reims France 3 Max Planck Research Unit for Enzymology of Protein Folding Halle Saale Germany 4 Schoolof Molecular and MicrobialBiosciences University of Sydney Australia Keywords gelatinase B GxxPG macrophage elastase matrilysin mass spectrometry Correspondence Christian E. H. Schmelzer Martin Luther University Halle-Wittenberg Institute of Pharmacy Wolfgang-Langenbeck-Str. 4 06120 Halle Saale Germany Fax 49 345 5527292 Tel 49 345 5525215 E-mail schmelzer@ Received 7 January 2010 revised 3 February 2010 accepted 12 February 2010 doi To provide a basis for the development of approaches to treat elastindegrading diseases the aim of this study was to investigate the degradation of the natural substrate tropoelastin by the elastinolytic matrix metalloproteinases MMP-7 MMP-9 and MMP-12 and to compare the cleavage site specificities of the enzymes using complementary MS techniques and molecular modeling. Furthermore the ability of the three proteases to release bioactive peptides was studied. Tropoelastin was readily degraded by all three MMPs. Eighty-nine cleavage sites in tropoelastin were identified for MMP-12 whereas MMP-7 and MMP-9 were found to cleave at only 58 and 63 sites respectively. Cleavages occurred predominantly in the N-terminal and C-terminal regions of tropoelastin. With respect to the cleavage site specificities the study revealed that all three MMPs similarly tolerate hydrophobic and or aliphatic amino acids including Pro Gly Ile and Val at P . MMP-7 shows

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