ADAMTS3: Difference between revisions

Jump to navigation Jump to search
Newer edit →
VisualWikitext
 
reorganize
Line 1: Line 1:
{{Infobox_gene}}
{{Infobox_gene}}
'''A disintegrin and metalloproteinase with thrombospondin motifs 3''' is an [[enzyme]] that in humans is encoded by the ''ADAMTS3'' [[gene]].<ref name="pmid10094461">{{cite journal | vauthors = Tang BL, Hong W | title = ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats | journal = FEBS Lett | volume = 445 | issue = 2–3 | pages = 223–5 |date=Apr 1999| pmid = 10094461 | pmc =  | doi =10.1016/S0014-5793(99)00119-2 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ADAMTS3 ADAM metallopeptidase with thrombospondin type 1 motif, 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9508| accessdate = }}</ref>
'''A disintegrin and metalloproteinase with thrombospondin motifs 3''' is an [[enzyme]] that in humans is encoded by the ''ADAMTS3'' [[gene]].<ref name="pmid10094461">{{cite journal | vauthors = Tang BL, Hong W | title = ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats | journal = FEBS Letters | volume = 445 | issue = 2-3 | pages = 223–5 | date = February 1999 | pmid = 10094461 | pmc =  | doi = 10.1016/S0014-5793(99)00119-2 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ADAMTS3 ADAM metallopeptidase with thrombospondin type 1 motif, 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9508| access-date = }}</ref> The protein encoded by this gene is the major procollagen II N-propeptidase.<ref name="entrez" />


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Structure ==
{{PBB Summary
| section_title =  
| summary_text = 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. A deficiency of this protein may be responsible for dermatosparaxis, a genetic defect of connective tissues.<ref name="entrez" />
}}


==References==
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.<ref name="entrez" />
 
== Function ==
 
Because of the high similarity to [[ADAMTS2]], the major substrate of ADAMTS3 had been erroneously assumed to be procollagen II.<ref name="pmid11408482">{{cite journal | vauthors = Fernandes RJ, Hirohata S, Engle JM, Colige A, Cohn DH, Eyre DR, Apte SS | title = Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis | journal = The Journal of Biological Chemistry | volume = 276 | issue = 34 | pages = 31502–9 | date = August 2001 | pmid = 11408482 | doi = 10.1074/jbc.M103466200 }}</ref> However, ADAMTS3 appears largely irrelevant for collagen maturation but instead is required for the activation of the lymphangiogenic growth factor [[VEGF-C]].<ref name="pmid24552833">{{cite journal | vauthors = Jeltsch M, Jha SK, Tvorogov D, Anisimov A, Leppänen VM, Holopainen T, Kivelä R, Ortega S, Kärpanen T, Alitalo K | title = CCBE1 enhances lymphangiogenesis via A disintegrin and metalloprotease with thrombospondin motifs-3-mediated vascular endothelial growth factor-C activation | journal = Circulation | volume = 129 | issue = 19 | pages = 1962–71 | date = May 2014 | pmid = 24552833 | doi = 10.1161/CIRCULATIONAHA.113.002779 }}</ref> Hence, ADAMTS3 is essential for the development and growth of [[lymphatic vessel]]s. The proteolytic processing of VEGF-C by ADAMTS3 is regulated by the [[CCBE1]] protein.
 
== Clinical significance ==
 
A deficiency of this protein may be responsible for [[dermatosparaxis]], a genetic defect of connective tissues.<ref name="entrez" />
 
Some hereditary forms of [[lymphedema]] are caused by mutations in ADAMTS3.<ref name="pmid28687807">{{cite journal | vauthors = Jha SK, Rauniyar K, Karpanen T, Leppänen VM, Brouillard P, Vikkula M, Alitalo K, Jeltsch M | title = Efficient activation of the lymphangiogenic growth factor VEGF-C requires the C-terminal domain of VEGF-C and the N-terminal domain of CCBE1 | journal = Scientific Reports | volume = 7 | issue = 1 | pages = 4916 | date = July 2017 | pmid = 28687807 | pmc = 5501841 | doi = 10.1038/s41598-017-04982-1 }}</ref><ref name="pmid28985353">{{cite journal | vauthors = Brouillard P, Dupont L, Helaers R, Coulie R, Tiller GE, Peeden J, Colige A, Vikkula M | title = Loss of ADAMTS3 activity causes Hennekam lymphangiectasia-lymphedema syndrome 3 | journal = Human Molecular Genetics | volume = 26 | issue = 21 | pages = 4095–4104 | date = November 2017 | pmid = 28985353 | doi = 10.1093/hmg/ddx297 }}</ref>
 
== References ==
{{reflist}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Tang BL | title = ADAMTS: a novel family of extracellular matrix proteases | journal = The International Journal of Biochemistry & Cell Biology | volume = 33 | issue = 1 | pages = 33–44 | date = January 2001 | pmid = 11167130 | doi = 10.1016/S1357-2725(00)00061-3 }}
| citations =
* {{cite journal | vauthors = Martel-Pelletier J, Welsch DJ, Pelletier JP | title = Metalloproteases and inhibitors in arthritic diseases | journal = Best Practice & Research. Clinical Rheumatology | volume = 15 | issue = 5 | pages = 805–29 | date = December 2001 | pmid = 11812023 | doi = 10.1053/berh.2001.0195 }}
*{{cite journal | author=Tang BL |title=ADAMTS: a novel family of extracellular matrix proteases |journal=Int. J. Biochem. Cell Biol. |volume=33 |issue= 1 |pages= 33–44 |year= 2001 |pmid= 11167130 |doi=10.1016/S1357-2725(00)00061-3 }}
* {{cite journal | vauthors = Hirohata S | title = [ADAMTS family--new extracellular matrix degrading enzyme] | journal = Seikagaku. The Journal of Japanese Biochemical Society | volume = 73 | issue = 11 | pages = 1333–7 | date = November 2001 | pmid = 11831030 | doi =  }}
*{{cite journal | vauthors=Martel-Pelletier J, Welsch DJ, Pelletier JP |title=Metalloproteases and inhibitors in arthritic diseases |journal=Best practice & research. Clinical rheumatology |volume=15 |issue= 5 |pages= 805–29 |year= 2002 |pmid= 11812023 |doi= 10.1053/berh.2001.0195 }}
* {{cite journal | vauthors = Hurskainen TL, Hirohata S, Seldin MF, Apte SS | title = 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 | journal = The Journal of Biological Chemistry | volume = 274 | issue = 36 | pages = 25555–63 | date = September 1999 | pmid = 10464288 | doi = 10.1074/jbc.274.36.25555 }}
*{{cite journal | author=Hirohata S |title=[ADAMTS family--new extracellular matrix degrading enzyme] |journal=Seikagaku |volume=73 |issue= 11 |pages= 1333–7 |year= 2002 |pmid= 11831030 |doi=  }}
* {{cite journal | vauthors = Colige A, Vandenberghe I, Thiry M, Lambert CA, Van Beeumen J, Li SW, Prockop DJ, Lapiere CM, Nusgens BV | title = Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3 | journal = The Journal of Biological Chemistry | volume = 277 | issue = 8 | pages = 5756–66 | date = February 2002 | pmid = 11741898 | doi = 10.1074/jbc.M105601200 }}
*{{cite journal | vauthors=Nagase T, Ishikawa K, Nakajima D |title=Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro |journal=DNA Res. |volume=4 |issue= 2 |pages= 141–50 |year= 1997 |pmid= 9205841 |doi=10.1093/dnares/4.2.141  |display-authors=etal}}
*{{cite journal  | vauthors=Hurskainen TL, Hirohata S, Seldin MF, Apte SS |title=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 |journal=J. Biol. Chem. |volume=274 |issue= 36 |pages= 25555–63 |year= 1999 |pmid= 10464288 |doi=10.1074/jbc.274.36.25555 }}
*{{cite journal  | vauthors=Fernandes RJ, Hirohata S, Engle JM |title=Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis |journal=J. Biol. Chem. |volume=276 |issue= 34 |pages= 31502–9 |year= 2001 |pmid= 11408482 |doi= 10.1074/jbc.M103466200 |display-authors=etal}}
*{{cite journal | vauthors=Colige A, Vandenberghe I, Thiry M |title=Cloning and characterization of ADAMTS-14, a novel ADAMTS displaying high homology with ADAMTS-2 and ADAMTS-3 |journal=J. Biol. Chem. |volume=277 |issue= 8 |pages= 5756–66 |year= 2002 |pmid= 11741898 |doi= 10.1074/jbc.M105601200 |display-authors=etal}}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M12.220 M12.220]
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M12.220 M12.220]
* {{UCSC gene info|ADAMTS3}}
* {{UCSC gene info|ADAMTS3}}
Line 32: Line 34:
{{Metalloproteinases}}
{{Metalloproteinases}}


<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


[[Category:ADAMTS]]
[[Category:ADAMTS]]


{{gene-4-stub}}
{{gene-4-stub}}

Revision as of 12:36, 28 December 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

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

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

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

  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

  • 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

Retrieved from "https://www.wikidoc.org/index.php?title=ADAMTS3&oldid=1526384"