Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease
Advances in Biochemistry
Volume 1, Issue 3, August 2013, Pages: 43-50
Received: Aug. 8, 2013; Published: Aug. 20, 2013
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Authors
Hayley A. Hanby, Department of Pathology and Laboratory Medicine, The Children's Hospital of Philadelphia and The University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104
X. Long Zheng, Department of Pathology and Laboratory Medicine, The Children's Hospital of Philadelphia and The University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104
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Abstract
Here, we provide a comprehensive review of current findings concerning the biochemistry and physiological functions of ADAMTS7, a metalloprotease that is known to interact with cartilage oligomeric matrix protein, progranulin, and alpha2-macroglobulin. Such broad substrate specificity and potentially diverse physiological functions make ADAMTS7 an interesting enzyme to study. ADAMTS7 has been shown to play a role in the pathogenesis of arthritis and disc disorders. More recently, the ADAMTS7 locus is identified to have a strong association with coronary atherosclerotic disease. However, the role of ADAMTS7 in the development of atherosclerosis is yet to be determined. The development of an easy and high throughput assay for ADAMTS7 activity and appropriate animal models will allow us to uncover the novel mechanisms of coronary arterial disease.
Keywords
ADAMTS7, Substrate Specificity, Structure-Function, Cardiovascular Disease, and Smooth Muscle Cell
To cite this article
Hayley A. Hanby, X. Long Zheng, Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease, Advances in Biochemistry. Vol. 1, No. 3, 2013, pp. 43-50. doi: 10.11648/j.ab.20130103.11
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