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ADAMTS2: More than a procollagen N-proteinase
Ruben Vanlerberghe1, Alain Colige2, Anne-Marie Malfait3
1Center for Medical Genetics, Ghent University Hospital, Department of Biomolecular Medicine, Ghent University, Ghent 9000, Belgium.
Genes & Diseases
|August 21, 2025
Summary
A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAMTS2) is crucial for collagen maturation, and its defects cause Ehlers-Danlos syndrome dermatosparaxis type. Emerging roles in other diseases highlight its therapeutic potential.
Area of Science:
- Biochemistry
- Genetics
- Cell Biology
Background:
- ADAMTS2 is a metalloproteinase essential for fibrillar collagen processing.
- Defects in ADAMTS2 cause dermatosparaxis (dEDS), a connective tissue disorder.
- Recent research indicates broader roles for ADAMTS2 beyond collagen maturation.
Purpose of the Study:
- To review the discovery, structure, regulation, and function of ADAMTS2.
- To explore its role in collagen maturation and dEDS pathogenesis.
- To discuss newly identified substrates and implications in complex diseases.
Main Methods:
- Literature review of ADAMTS2 research.
- Analysis of genetic defects leading to dEDS.
- Synthesis of findings on novel ADAMTS2 substrates and functions.
Main Results:
- ADAMTS2 deficiency leads to impaired collagen I processing and severe skin fragility.
- ADAMTS2 participates in angiogenesis, lymphangiogenesis, neurodevelopment, immunity, and spermatogenesis.
- Evidence suggests ADAMTS2 involvement in cancer, cardiovascular, and neurodegenerative diseases.
Conclusions:
- ADAMTS2 is a key enzyme in connective tissue integrity and has diverse biological functions.
- Understanding ADAMTS2's expanded roles may resolve dEDS questions and reveal therapeutic targets.
- ADAMTS2 holds potential as a biomarker and therapeutic agent for various complex disorders.
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