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Matrix Metalloproteinases: Pro- and Anti-Angiogenic Activities

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Presentation on theme: "Matrix Metalloproteinases: Pro- and Anti-Angiogenic Activities"— Presentation transcript:

1 Matrix Metalloproteinases: Pro- and Anti-Angiogenic Activities
Saadia L. Raza, Lynn A. Cornelius  Journal of Investigative Dermatology Symposium Proceedings  Volume 5, Issue 1, Pages (December 2000) DOI: /j x Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

2 Figure 1 MMP family, structural domains, and substrates.
Journal of Investigative Dermatology Symposium Proceedings 2000 5, 47-54DOI: ( /j x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

3 Figure 2 Targets for inhibiting MMP expression and activity.
Reproduced with permission fromWestermerck & Veli-Matti 1999). Journal of Investigative Dermatology Symposium Proceedings 2000 5, 47-54DOI: ( /j x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

4 Figure 3 Cleavage of plasminogen by matrix metalloproteinases. (A) Pancreatic elastase (PE) [39 mM] and the MMP [final concentration 5 × 10-7 M] mouse and human macrophage elastase (MMP-12, MME and HME, respectively) were incubated with 4 μM plasminogen (HPg) [final concentration] for 1 or 18 h at 37°C. The reaction mixtures were stopped with SDS sample buffer containing DTT and subjected to electrophoresis on a 10% SDS-polyacrylamide gel. (B) The MMP [final concentration 5 × 10-7 M] stromelysin (MMP-3), 92 kDa gelatinase (MMP-9), collagenase-2 (MMP-8), matrilysin (MMP-7), collagenase-1 (MMP-1) and collagenase-3 (MMP-13) were incubated with 4 μM HPg [final concentration] for the indicated times. (C) MMP-12 was preincubated with either aprotinin (Apr) [100 KIU/ml], a hydroxymate MMP-inhibitor (SC 44463) [25 μM], or TIMP [25 μM] for 1 h prior to the addition of HPg. For all parts, the arrows denote 38 kDa, 35 kDa, and 14 kDa cleavage products. The 38 k Da product was subsequently sequenced and is consistent with angiostatin (kringle regions 1–4). Reproduced with permission fromCornelius et al. (1998), Copyright 1998, American Association of Immunologists. Journal of Investigative Dermatology Symposium Proceedings 2000 5, 47-54DOI: ( /j x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

5 Figure 4 Synthetic MMP inhibitors. Hydroxymate group (CONHOH) binds to active site Zn ion of the MMP. Asterisks denote molecule sites that affect recognition of specific MMP. Journal of Investigative Dermatology Symposium Proceedings 2000 5, 47-54DOI: ( /j x) Copyright © 2000 The Society for Investigative Dermatology, Inc Terms and Conditions

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