ADAMTS2

ADAMTS2
Identifiers
Aliases	ADAMTS2 , ADAM-TS2, ADAMTS-2, ADAMTS-3, NPI, PC I-NP, PCI-NP, PCINP, PCPNI, PNPI, ADAM metallopeptidase with thrombospondin type 1 motif 2, EDSDERMS
External IDs	OMIM: 604539; MGI: 1347356; HomoloGene: 8597; GeneCards: ADAMTS2; OMA:ADAMTS2 - orthologs
Gene location (Mouse) Chr. Chromosome 11 (mouse) [1] Band 11|11 B1.3 Start 50,492,911 bp [1] End 50,698,400 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium subcutaneous adipose tissue right lung right coronary artery spleen left coronary artery upper lobe of left lung gastric mucosa myometrium left uterine tube Top expressed in ascending aorta aortic valve decidua gastrula umbilical cord stroma of bone marrow body of femur ankle cervix vas deferens More reference expression data BioGPS n/a
Gene ontology Molecular function zinc ion binding peptidase activity metalloendopeptidase activity hydrolase activity metallopeptidase activity metal ion binding Cellular component extracellular region collagen-containing extracellular matrix extracellular matrix Biological process collagen catabolic process protein processing spermatogenesis skin development collagen fibril organization lung development proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9509 216725 Ensembl n/a ENSMUSG00000036545 UniProt O95450 Q8C9W3 RefSeq (mRNA) NM_021599 NM_014244 NM_001277305 NM_175643 RefSeq (protein) NP_055059 NP_067610 NP_783574 Location (UCSC) n/a Chr 11: 50.49 – 50.7 Mb PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS2) also known as procollagen I N-proteinase (PC I-NP) is an enzyme ^[4] that in humans is encoded by the ADAMTS2 gene. ^{[5] [6]}

Gene

The ADAMTS2 gene is located on the long (q) arm of chromosome 5 at the end (terminus) of the arm, from base pair 178,473,473 to base pair 178,704,934.

Function

ADAMTS2 is responsible for processing several types of procollagen proteins. Procollagens are the precursors of collagens, the proteins that add strength and support to many body tissues. Specifically, this enzyme clips a short chain of amino acids off one end of the procollagen. This clipping step is necessary for collagen molecules to function normally and assemble into fibrils outside cells.

Clinical significance

Ehlers-Danlos syndrome, dermatosparaxis type is caused by mutations in the ADAMTS2 gene. ^[6] Several mutations in the ADAMTS2 gene have been identified in people with this syndrome. These mutations greatly reduce the production of the enzyme made by the ADAMTS2 gene. Procollagen cannot be processed correctly without this enzyme. As a result, collagen fibrils are not assembled properly; they appear ribbon-like and disorganized under the microscope. Cross-links, or chemical interactions, between collagen fibrils are also affected. These defects weaken connective tissue (the tissue that binds and supports the body's muscles, ligaments, organs, and skin), which causes the signs and symptoms of the disorder.

See also

• ADAMTS5
• ADAMTS13

References

1. GRCm38: Ensembl release 89: ENSMUSG00000036545 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Tang BL, Hong W (February 1999). "ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats". FEBS Lett. 445 (2–3): 223–5. Bibcode:1999FEBSL.445..223T. doi: 10.1016/S0014-5793(99)00119-2 . PMID   10094461. S2CID   37955930.
5. "Entrez Gene: ADAM metallopeptidase with thrombospondin type 1 motif".
6. Colige A, Nuytinck L, Hausser I, van Essen AJ, Thiry M, Herens C, Adès LC, Malfait F, Paepe AD, Franck P, Wolff G, Oosterwijk JC, Smitt JH, Lapière CM, Nusgens BV (October 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. Dermatol. 123 (4): 656–63. doi: 10.1111/j.0022-202X.2004.23406.x . PMID   15373769.^{[ permanent dead link ]}

Further reading

• Wang WM, Lee S, Steiglitz BM, Scott IC, Lebares CC, Allen ML, Brenner MC, Takahara K, Greenspan DS (May 2003). "Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase". J. Biol. Chem. 278 (21): 19549–57. doi: 10.1074/jbc.M300767200 . PMID   12646579.
• Reardon W, Winter RM, Smith LT, et al. (1995). "The natural history of human dermatosparaxis (Ehlers-Danlos syndrome type VIIC)". Clin. Dysmorphol. 4 (1): 1–11. doi:10.1097/00019605-199501000-00001. PMID   7735500. S2CID   2412884.
• Colige A, Vandenberghe I, Thiry M, et al. (2002). "Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3". J. Biol. Chem. 277 (8): 5756–66. doi: 10.1074/jbc.M105601200 . PMID   11741898.
• Kevorkian L, Young DA, Darrah C, et al. (2004). "Expression profiling of metalloproteinases and their inhibitors in cartilage". Arthritis Rheum. 50 (1): 131–41. doi: 10.1002/art.11433 . PMID   14730609.
• Hurskainen TL, Hirohata S, Seldin MF, Apte SS (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 (36): 25555–63. doi: 10.1074/jbc.274.36.25555 . PMID   10464288.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC   1356129 . PMID   16344560.
• Dubail J, Kesteloot F, Deroanne C, et al. (2010). "ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity" (PDF). Cellular and Molecular Life Sciences. 67 (24): 4213–32. doi:10.1007/s00018-010-0431-6. hdl:2268/73235. PMC   11115784 . PMID   20574651. S2CID   20047628. Archived from the original (PDF) on 2022-02-26. Retrieved 2019-09-26.
• Colige A, Sieron AL, Li SW, et al. (1999). "Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene". Am. J. Hum. Genet. 65 (2): 308–17. doi:10.1086/302504. PMC   1377929 . PMID   10417273.
• Hartley JL, Temple GF, Brasch MA (2000). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC   310948 . PMID   11076863.
• Tang BL (2001). "ADAMTS: a novel family of extracellular matrix proteases". Int. J. Biochem. Cell Biol. 33 (1): 33–44. doi:10.1016/S1357-2725(00)00061-3. PMID   11167130.
• Lasky-Su J, Anney RJ, Neale BM, et al. (2008). "Genome-wide association scan of the time to onset of Attention Deficit Hyperactivity Disorder". Am. J. Med. Genet. B Neuropsychiatr. Genet. 147B (8): 1355–8. doi:10.1002/ajmg.b.30869. PMC   2605611 . PMID   18937294.
• Colige A, Ruggiero F, Vandenberghe I, et al. (2005). "Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase cleaving the aminopropeptide of fibrillar procollagens types I-III and V". J. Biol. Chem. 280 (41): 34397–408. doi: 10.1074/jbc.M506458200 . PMID   16046392.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Brandenberger R, Wei H, Zhang S, et al. (2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID   15146197. S2CID   27764390.
• Tomii Y, Kamochi J, Yamazaki H, et al. (2002). "Human thrombospondin 2 inhibits proliferation of microvascular endothelial cells". Int. J. Oncol. 20 (2): 339–42. doi:10.3892/ijo.20.2.339. PMID   11788898.

External links

• GeneCard
• The MEROPS online database for peptidases and their inhibitors: M12.301
• Human ADAMTS2 genome location and ADAMTS2 gene details page in the UCSC Genome Browser .