Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease

Hayley A. Hanby; X. Long Zheng

doi:doi:10.11648/j.ab.20130103.11

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Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease

Hayley A. Hanby, X. Long Zheng

Published in Advances in Biochemistry (Volume 1, Issue 3)

Received: 8 August 2013 Accepted: Published: 20 August 2013

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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.

Published in	Advances in Biochemistry (Volume 1, Issue 3)
DOI	10.11648/j.ab.20130103.11
Page(s)	43-50
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

ADAMTS7, Substrate Specificity, Structure-Function, Cardiovascular Disease, and Smooth Muscle Cell

References

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APA Style

Hayley A. Hanby, X. Long Zheng. (2013). Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease. Advances in Biochemistry, 1(3), 43-50. https://doi.org/10.11648/j.ab.20130103.11

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ACS Style

Hayley A. Hanby; X. Long Zheng. Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease. Adv. Biochem. 2013, 1(3), 43-50. doi: 10.11648/j.ab.20130103.11

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AMA Style

Hayley A. Hanby, X. Long Zheng. Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease. Adv Biochem. 2013;1(3):43-50. doi: 10.11648/j.ab.20130103.11

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@article{10.11648/j.ab.20130103.11,
  author = {Hayley A. Hanby and X. Long Zheng},
  title = {Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease},
  journal = {Advances in Biochemistry},
  volume = {1},
  number = {3},
  pages = {43-50},
  doi = {10.11648/j.ab.20130103.11},
  url = {https://doi.org/10.11648/j.ab.20130103.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20130103.11},
  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.},
 year = {2013}
}

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TY  - JOUR
T1  - Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease
AU  - Hayley A. Hanby
AU  - X. Long Zheng
Y1  - 2013/08/20
PY  - 2013
N1  - https://doi.org/10.11648/j.ab.20130103.11
DO  - 10.11648/j.ab.20130103.11
T2  - Advances in Biochemistry
JF  - Advances in Biochemistry
JO  - Advances in Biochemistry
SP  - 43
EP  - 50
PB  - Science Publishing Group
SN  - 2329-0862
UR  - https://doi.org/10.11648/j.ab.20130103.11
AB  - 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.
VL  - 1
IS  - 3
ER  -

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Author Information

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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Hayley A. Hanby, X. Long Zheng. (2013). Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease. Advances in Biochemistry, 1(3), 43-50. https://doi.org/10.11648/j.ab.20130103.11

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ACS Style

Hayley A. Hanby; X. Long Zheng. Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease. Adv. Biochem. 2013, 1(3), 43-50. doi: 10.11648/j.ab.20130103.11

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AMA Style

Hayley A. Hanby, X. Long Zheng. Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease. Adv Biochem. 2013;1(3):43-50. doi: 10.11648/j.ab.20130103.11

Copy | Download

@article{10.11648/j.ab.20130103.11,
  author = {Hayley A. Hanby and X. Long Zheng},
  title = {Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease},
  journal = {Advances in Biochemistry},
  volume = {1},
  number = {3},
  pages = {43-50},
  doi = {10.11648/j.ab.20130103.11},
  url = {https://doi.org/10.11648/j.ab.20130103.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20130103.11},
  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.},
 year = {2013}
}

Copy | Download

TY  - JOUR
T1  - Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease
AU  - Hayley A. Hanby
AU  - X. Long Zheng
Y1  - 2013/08/20
PY  - 2013
N1  - https://doi.org/10.11648/j.ab.20130103.11
DO  - 10.11648/j.ab.20130103.11
T2  - Advances in Biochemistry
JF  - Advances in Biochemistry
JO  - Advances in Biochemistry
SP  - 43
EP  - 50
PB  - Science Publishing Group
SN  - 2329-0862
UR  - https://doi.org/10.11648/j.ab.20130103.11
AB  - 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.
VL  - 1
IS  - 3
ER  -

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