Adamts2

ADAMTS2 is the acronym for " A Disintegrin-like and metalloproteinase with thrombospondin type 1 motif 2". ADAMTS2 denotes a gene located on chromosome 5q35.3 (genomic coordinates (GRCh38): 5:179, 110,852-179, 345,460) which codes for a procollagen I N proteinase (NPI; EC 3.4.24.14) of the same name (Hurskainen et al. 1999).

The enzyme ADAM-TS2 is a metalloproteinase with thrombospondin motifs 2, which is responsible for the processing of various types of procollagen (Colige et al. 1999). In particular, this enzyme cuts off a short chain of amino acids at one end of the procollagen. This "clipping step" is essential for the collagen molecules to be processed normally and to be able to assemble into fibrils outside the cells. Mutations in the ADAMTS2 proteinase can only process procollagens incorrectly. The collagen fibrils appear band-shaped and unorganized under the microscope. Furthermore, cross-linking of the collagen fibrils or their chemical interactions with each other are affected.

The Dermato-sparaxis Ehlers-Danlos syndrome is caused by different mutations in the ADAMTS2 gene (Van Damme et al. 2016). Also in cows a Dermato-sparaxis phenotype similar to the human EDS type can occur, which is also caused by mutations in the ADAMTS gene.

1. Colige A et al (2004) Novel types of mutation responsible for the dermatosparactic type of Ehlers-Danlos syndrome (type VIIC) and common polymorphisms in the ADAMTS2 gene. J Invest Derm 123: 656-663.
2. Colige A et al (2005) Domain and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase clearing the aminopropeptide of fibrillar procollagens types I-III and VJ Biol Chem 280: 34397-34408
3. Hurskainen TL et al (1999) ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases: general features and genomic distribution of the ADAM-TS family. J Biol Chem 274: 25555-25563.
4. Van Damme et al (2016) Expanding the clinical and mutational spectrum of the Ehlers-Danlos syndrome, dermatosparaxis type. Genet. Med 18: 882-891