Oct 13, 2009

Effects of detergents on catalytic activity of human endometase/matrilysin 2, a putative cancer biomarker

Analytical Biochemistry
Hyun I ParkQing-Xiang Amy Sang


Matrix metalloproteinases (MMPs) are a family of hydrolytic enzymes that play significant roles in development, morphogenesis, inflammation, and cancer invasion. Endometase (matrilysin 2 or MMP-26) is a putative early biomarker for human carcinomas. The effects of the ionic and nonionic detergents on catalytic activity of endometase were investigated. The hydrolytic activity of endometase was detergent concentration dependent, exhibiting a bell-shaped curve with its maximum activity near the critical micelle concentration (CMC) of nonionic detergents tested. The effect of Brij-35 on human gelatinase B (MMP-9), matrilysin (MMP-7), and membrane-type 1 MMP (MT1-MMP) was further explored. Their maximum catalysis was observed near the CMC of Brij-35 ( approximately 90muM). Their IC(50) values were above the CMC. The inhibition mechanism of MMP-7, MMP-9, and MT1-MMP by Brij-35 was a mixed type as determined by Dixon's plot; however, the inhibition mechanism of endometase was noncompetitive with a K(i) value of 240muM. The catalytic activities of MMPs are influenced by detergents. Monomer of detergents may activate and stabilize MMPs to enhance catalysis, but micelle of detergents may sequester enzyme and block the substrate binding s...Continue Reading

  • References27
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Mentioned in this Paper

MMP14 gene
Dimethyl Sulfoxide
SLC25A29 gene
Enzymes, antithrombotic
Inclusion Bodies
Digestive Surfactants
GM 6001
Homology Modeling
Chudley-Mccullough Syndrome
Crystallography, X-Ray

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