Cancer metastatis, molecular and cellular mechanisms and by Wen G Jiang; R E Mansel

April 3, 2017 | Cancer | By admin | 0 Comments

By Wen G Jiang; R E Mansel

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The plasminogen activator inhibitor PAI-1 controls in vivo tumor vascularization by interaction with proteases, not vitronectin: implications for antiangiogenic strategies. J Cell Biol 2001; 152: 777–784. Bajou K, Noël A, Gerard RD, Masson V, Brunner N, Holst-Hansen C, Skobe M, Fusenig NE, Carmeliet P, Collen D, Foidart JM. Absence of host plasminogen activator inhibitor 1 prevents cancer invasion and vascularization. Nat Med 1998; 4: 923–928. Bergers G, Brekken R, McMahon GA, Vu TH, Itoh T, Tamaki K, Tanzawa K, Thorpe P, Werb Z, Hanahan D.

Both are secreted proteins and both have a typical signal peptide at the N terminal end. The propeptide domain is responsible for inhibition of the active site and maintains both proteins in a latent state until cleavage of the propeptide at a conserved amino acid sequence PRCGVPPV. This sequence is conserved not only within the gelatinases, but also throughout the MMP family. The rest of the propeptide diverges between MMP-9 and 2. The catalytic domains of both enzymes contain a zinc binding domain including 3 histidines that can complex a zinc ion that is a critical component of the active site.

Relationship between secreted urokinase plasminogen activator activity and metastatic potential in murine B16 cells transfected with human urokinase sense and antisense genes. Cancer Res 1990; 50: 7623–7633. 38 Chapter 3 THE GELATINASES, MMP-2 AND MMP-9-IMPLICATIONS FOR INVASION AND METASTASIS Ruth J. , University of Pennsylvania, Philadelphia, PA 19104, USA 1. INTRODUCTION The gelatinase subgroup of matrix metalloproteinases consists of two highly homologous members, a larger 92 kDa enzyme MMP-9 and a smaller 72 kDa, MMP-2.

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