The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases

The a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) comprise a family of secreted zinc metalloproteinases with a precisely ordered modular organization. These enzymes play an important role in the turnover of extracellular matrix proteins in various tissues and their dysregul...

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Main Authors: Lin, Edward A, Liu, Chuan-ju
Format: Online
Language:English
Published: Dove Medical Press 2009
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5074720/
id pubmed-5074720
recordtype oai_dc
spelling pubmed-50747202016-10-27 The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases Lin, Edward A Liu, Chuan-ju Review The a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) comprise a family of secreted zinc metalloproteinases with a precisely ordered modular organization. These enzymes play an important role in the turnover of extracellular matrix proteins in various tissues and their dysregulation has been implicated in disease-related processes such as arthritis, atherosclerosis, cancer, and inflammation. ADAMTS-7 and ADAMTS-12 share a similar domain organization to each other and form a subgroup within the ADAMTS family. Emerging evidence suggests that ADAMTS-7 and ADAMTS-12 may play an important role in the development and pathogenesis of various kinds of diseases. In this review, we summarize what is currently known about the roles of these two metalloproteinases, with a special focus on their involvement in chondrogenesis, endochondral ossification, and the pathogenesis of arthritis, atherosclerosis, and cancer. The future study of ADAMTS-7 and ADAMTS-12, as well as the molecules with which they interact, will help us to better understand a variety of human diseases from both a biological and therapeutic standpoint. Dove Medical Press 2009-09-22 /pmc/articles/PMC5074720/ /pubmed/27789986 Text en © 2009 Lin and Liu, publisher and licensee Dove Medical Press Ltd This is an Open Access article which permits unrestricted noncommercial use, provided the original work is properly cited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Lin, Edward A
Liu, Chuan-ju
spellingShingle Lin, Edward A
Liu, Chuan-ju
The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases
author_facet Lin, Edward A
Liu, Chuan-ju
author_sort Lin, Edward A
title The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases
title_short The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases
title_full The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases
title_fullStr The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases
title_full_unstemmed The emerging roles of ADAMTS-7 and ADAMTS-12 matrix metalloproteinases
title_sort emerging roles of adamts-7 and adamts-12 matrix metalloproteinases
description The a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) comprise a family of secreted zinc metalloproteinases with a precisely ordered modular organization. These enzymes play an important role in the turnover of extracellular matrix proteins in various tissues and their dysregulation has been implicated in disease-related processes such as arthritis, atherosclerosis, cancer, and inflammation. ADAMTS-7 and ADAMTS-12 share a similar domain organization to each other and form a subgroup within the ADAMTS family. Emerging evidence suggests that ADAMTS-7 and ADAMTS-12 may play an important role in the development and pathogenesis of various kinds of diseases. In this review, we summarize what is currently known about the roles of these two metalloproteinases, with a special focus on their involvement in chondrogenesis, endochondral ossification, and the pathogenesis of arthritis, atherosclerosis, and cancer. The future study of ADAMTS-7 and ADAMTS-12, as well as the molecules with which they interact, will help us to better understand a variety of human diseases from both a biological and therapeutic standpoint.
publisher Dove Medical Press
publishDate 2009
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5074720/
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