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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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ADAMTS3

Introduction

A disintegrin and metalloproteinase with thrombospondin motifs 3 is an enzyme that in humans is encoded by the ADAMTS3 gene.[1][2] The protein encoded by this gene is the major procollagen II N-propeptidase.[2]

Structure

Structure

This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The protein encoded by this gene is the major procollagen II N-propeptidase.[2]

Function

Function

Because of the high similarity to ADAMTS2, the major substrate of ADAMTS3 had been erroneously assumed to be procollagen II.[3] However, ADAMTS3 appears largely irrelevant for collagen maturation but instead is required for the activation of the lymphangiogenic growth factor VEGF-C.[4] Hence, ADAMTS3 is essential for the development and growth of lymphatic vessels. The proteolytic processing of VEGF-C by ADAMTS3 is regulated by the CCBE1 protein.

Clinical significance

Clinical significance

A deficiency of this protein may be responsible for dermatosparaxis, a genetic defect of connective tissues.[2]

Some hereditary forms of lymphedema are caused by mutations in ADAMTS3.[5][6]

References

References

  1. ↑ Tang BL, Hong W (February 1999). “ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats”. FEBS Letters. 445 (2–3): 223–5. doi:10.1016/S0014-5793(99)00119-2. PMID 10094461.
  2. ↑ 2.0 2.1 2.2 2.3 “Entrez Gene: ADAMTS3 ADAM metallopeptidase with thrombospondin type 1 motif, 3”.
  3. ↑ Fernandes RJ, Hirohata S, Engle JM, Colige A, Cohn DH, Eyre DR, Apte SS (August 2001). “Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis”. The Journal of Biological Chemistry. 276 (34): 31502–9. doi:10.1074/jbc.M103466200. PMID 11408482.
  4. ↑ Jeltsch M, Jha SK, Tvorogov D, Anisimov A, Leppänen VM, Holopainen T, Kivelä R, Ortega S, Kärpanen T, Alitalo K (May 2014). “CCBE1 enhances lymphangiogenesis via A disintegrin and metalloprotease with thrombospondin motifs-3-mediated vascular endothelial growth factor-C activation”. Circulation. 129 (19): 1962–71. doi:10.1161/CIRCULATIONAHA.113.002779. PMID 24552833.
  5. ↑ Jha SK, Rauniyar K, Karpanen T, Leppänen VM, Brouillard P, Vikkula M, Alitalo K, Jeltsch M (July 2017). “Efficient activation of the lymphangiogenic growth factor VEGF-C requires the C-terminal domain of VEGF-C and the N-terminal domain of CCBE1”. Scientific Reports. 7 (1): 4916. doi:10.1038/s41598-017-04982-1. PMC 5501841. PMID 28687807.
  6. ↑ Brouillard P, Dupont L, Helaers R, Coulie R, Tiller GE, Peeden J, Colige A, Vikkula M (November 2017). “Loss of ADAMTS3 activity causes Hennekam lymphangiectasia-lymphedema syndrome 3”. Human Molecular Genetics. 26 (21): 4095–4104. doi:10.1093/hmg/ddx297. PMID 28985353.
Further reading

Further reading

  • Tang BL (January 2001). “ADAMTS: a novel family of extracellular matrix proteases”. The International Journal of Biochemistry & Cell Biology. 33 (1): 33–44. doi:10.1016/S1357-2725(00)00061-3. PMID 11167130.
  • Martel-Pelletier J, Welsch DJ, Pelletier JP (December 2001). “Metalloproteases and inhibitors in arthritic diseases”. Best Practice & Research. Clinical Rheumatology. 15 (5): 805–29. doi:10.1053/berh.2001.0195. PMID 11812023.
  • Hirohata S (November 2001). “[ADAMTS family–new extracellular matrix degrading enzyme]”. Seikagaku. The Journal of Japanese Biochemical Society. 73 (11): 1333–7. PMID 11831030.
  • Hurskainen TL, Hirohata S, Seldin MF, Apte SS (September 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”. The Journal of Biological Chemistry. 274 (36): 25555–63. doi:10.1074/jbc.274.36.25555. PMID 10464288.
  • Colige A, Vandenberghe I, Thiry M, Lambert CA, Van Beeumen J, Li SW, Prockop DJ, Lapiere CM, Nusgens BV (February 2002). “Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3”. The Journal of Biological Chemistry. 277 (8): 5756–66. doi:10.1074/jbc.M105601200. PMID 11741898.
External links