ADAMTS2
ADAMTS2 (ADAM metallopeptidase with thrombospondin type 1 motif 2) is a secreted metalloproteinase of the ADAMTS family that removes the N-propeptide from fibrillar procollagens. It is also known as ADAMTS-3, ADAM-TS2, hPCPNI, PCINP and NPI. Browse Assay Genie's current range of ADAMTS2 research reagents below, or read on for the biology behind the target.
ADAMTS2 is a secreted metalloproteinase that acts in the extracellular matrix. It cleaves the propeptides of type I and type II collagen before fibril assembly, and it does not act on type III collagen. The NCBI Gene summary describes the mature enzyme as a procollagen N-proteinase that excises the N-propeptide of the fibrillar procollagens types I-III and type V. ADAMTS2 also cleaves lysyl oxidase (LOX) at a site downstream of its propeptide cleavage site. This produces a short LOX form with reduced collagen-binding activity.
The ADAMTS2 gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Family members share several modules: a propeptide region, a metalloproteinase domain, a disintegrin-like domain and a thrombospondin type 1 (TS) motif. They differ in the number of C-terminal TS motifs, and some carry unique C-terminal domains. The ADAMTS2 protein is made as a preproprotein and is proteolytically processed to give the mature enzyme. Alternative splicing produces multiple transcript variants, and at least one encodes an isoform that is proteolytically processed.
Mutations in the ADAMTS2 gene cause Ehlers-Danlos syndrome type VIIC, a recessively inherited connective-tissue disorder. This makes the enzyme a useful reference point for studies of collagen maturation and connective-tissue biology. The HGNC previous name, a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 2, reflects the domain architecture shared across the ADAMTS group. The mouse ortholog is Adamts2.
ADAMTS2 removes the N-propeptide from type I and II procollagens before fibril assembly, so it is central to studies of collagen processing.
Mutations in ADAMTS2 cause Ehlers-Danlos syndrome type VIIC, a recessive connective-tissue disorder, making it relevant to disease mechanism research.
As a secreted matrix protease that also cleaves lysyl oxidase, ADAMTS2 links propeptide processing to matrix maturation.
Comparing ADAMTS2 with other family members clarifies how differences in TS motif number and C-terminal domains relate to substrate handling.
ADAMTS2 is a procollagen N-proteinase. It cleaves the propeptides of type I and II collagen before fibril assembly, but does not act on type III collagen. It also cleaves lysyl oxidase (LOX) downstream of its propeptide site, giving a short LOX form with reduced collagen-binding activity.
ADAMTS2 is also called ADAMTS-3, ADAM-TS2, hPCPNI, PCINP and NPI. The full name is ADAM metallopeptidase with thrombospondin type 1 motif 2, and UniProt lists it as a disintegrin and metalloproteinase with thrombospondin motifs 2. The enzyme carries EC number 3.4.24.14.
Mutations in ADAMTS2 cause Ehlers-Danlos syndrome type VIIC, a recessively inherited connective-tissue disorder. The mouse ortholog is Adamts2. Check the datasheet of any product for its validated reactivity.
Other ADAMTS family metalloproteinases involved in extracellular matrix processing and connective-tissue biology.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O95450; product specifications from Assay Genie datasheets.