Work

A Disintegrin-like and Metalloprotease (Reprolysin-type) with Thrombospondin Type 1 Motif (ADAMTS) Superfamily: Functions and Mechanisms

Year: 2009

Type: review

Abstract: Together with seven ADAMTS-like proteins, the 19 mammalian ADAMTS proteases constitute a superfamily. ADAMTS proteases are secreted zinc metalloproteases whose hallmark is an ancillary domain containing one or more thrombospondin type 1 repeats. ADAMTS-like proteins resemble ADAMTS ancillary domains and lack proteolytic activity. Vertebrate expansion of the superfamily reflects emergence of new substrates, duplication of proteolytic activities in new contexts, and cooperative functions of the duplicated genes. ADAMTS proteases are involved in maturation of procollagen and von Willebrand factor, as well as in extracellular matrix proteolysis relating to morphogenesis, angiogenesis, ovulation, cancer, and arthritis. New insights into ADAMTS mechanisms indicate significant regulatory roles for ADAMTS ancillary domains, propeptide processing, and glycosylation. ADAMTS-like proteins appear to have regulatory roles in the extracellular matrix.

Source: Journal of Biological Chemistry

DOI: 10.1074/jbc.r109.052340

Author: Suneel S. Apte

Institution: Cleveland Clinic

Language: English

Topic: Protease and Inhibitor Mechanisms

Subfield: Cancer Research

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: Arthritis Foundation, National Marfan Foundation, National Institutes of Health, National Institute of Arthritis and Musculoskeletal and Skin Diseases