The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology.

By M. Bekhouche, A. Colige. 2015

133 citations recorded by the source corpus.

Collagen fibers are the main components of most of the extracellular matrices where they provide a structural support to cells, tissues and organs. Fibril-forming procollagens are synthetized as individual chains that associate to form homo- or hetero-trimers. They are characterized by the presence of a central triple helical domain flanked by amino and carboxy propeptides. Although there are some exceptions, these two propeptides have to be proteolytically removed to allow the almost spontaneous assembly of the trimers into collagen fibrils and fibers. While the carboxy-propeptide is mainly cleaved by proteinases from the tolloid family, the amino-propeptide is usually processed by procollagen N-proteinases: ADAMTS2, 3 and 14. This review summarizes the current knowledge concerning this subfamily of ADAMTS enzymes and discusses their potential involvement in physiopathological processes that are not directly linked to fibrillar procollagen processing.

Subfields: Cancer Research, Genetics, Immunology and Allergy

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In Cancer Research

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Citations in the corpus

• A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “Studies on ADAMTS-2 have shown that an autocatalytic cleavage occurring within the C-terminal end, possibly in the procollagen N-propetidase domain, increases its activity [35, 41].”
• ADAMTS proteins in human disorders (2018, background): “ADAMTS2 mutations lead to Ehlers-Danlos syndrome (dermatosparactic type or VIIc), whose major manifestation is severe skin fragility, although other anomalies, including abnormal dentition have been described [25, 26].”