The biology and pathophysiology of the proatherogenic metalloprotease ADAMTS7. Open Biol 2026 Apr 01;16(4)
Date
04/01/2026Pubmed ID
41920022DOI
10.1098/rsob.250111Scopus ID
2-s2.0-105034818167 (requires institutional sign-in at Scopus site)Abstract
The ADAMTS (a disintegrin and metalloproteinase with thrombospondin type-1 motifs) metalloprotease family comprises 19 members, and they play critical roles in development, angiogenesis and coagulation. These enzymes are also pivotal in the turnover of extracellular matrix proteins in various tissues, and their dysregulation has been linked to diseases such as arthritis, atherosclerosis, cancer and inflammation. These secreted zinc metalloproteases are composed of multiple domains and are localized to the extracellular matrix and present in circulation. The metalloprotease member 7 of this family or ADAMTS7 was cloned in 2004. However, in 2011, it gained significant attention when its gene locus was associated with an increased risk of atherosclerosis and coronary artery disease. Despite its strong association with human diseases, the biological functions, substrate targets and processing of ADAMTS7 remain poorly understood, limiting our comprehension of its roles in both health and disease. This review highlights the structural organization of ADAMTS7, its expression and regulation, known substrates, and its involvement in various pathophysiological processes. Additionally, perspectives on future research directions and priorities are presented. ADAMTS7 remains a compelling target for drug and biomarker discovery, though much about this metalloprotease remains to be uncovered.
Author List
Goyal S, Muniu J, Bhat MA, Oldham E, Pruitt DW, Frias Perez L, Miranda FZ, Muia JAuthor
Joshua Muia PhD Assistant Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ADAMTS7 ProteinAnimals
Atherosclerosis
Humans
