ADAMTS10: Difference between revisions
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{{ | {{Infobox_gene}} | ||
'''A disintegrin and metalloproteinase with thrombospondin motifs 10''' is an [[enzyme]] that in humans is encoded by the ''ADAMTS10'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADAMTS10 ADAM metallopeptidase with thrombospondin type 1 motif, 10| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81794| accessdate = }}</ref> | |||
''' | |||
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| summary_text = This gene belongs to the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 motifs) family of zinc-dependent proteases. ADAMTS proteases are complex secreted enzymes containing a prometalloprotease domain of the reprolysin type attached to an ancillary domain with a highly conserved structure that includes at least one thrombospondin type 1 repeat. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. The product of this gene plays a major role in growth and in skin, lens, and heart development. It is also a candidate gene for autosomal recessive [[Weill-Marchesani syndrome]].<ref name="entrez" | | summary_text = This gene belongs to the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 motifs) family of zinc-dependent proteases. ADAMTS proteases are complex secreted enzymes containing a prometalloprotease domain of the reprolysin type attached to an ancillary domain with a highly conserved structure that includes at least one thrombospondin type 1 repeat. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. The product of this gene plays a major role in growth and in skin, lens, and heart development. It is also a candidate gene for autosomal recessive [[Weill-Marchesani syndrome]].<ref name="entrez" /> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist}} | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{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= }} | *{{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 | | *{{cite journal | vauthors=Faivre L, Dollfus H, Lyonnet S |title=Clinical homogeneity and genetic heterogeneity in Weill-Marchesani syndrome. |journal=Am. J. Med. Genet. A |volume=123 |issue= 2 |pages= 204–7 |year= 2004 |pmid= 14598350 |doi= 10.1002/ajmg.a.20289 |display-authors=etal}} | ||
*{{cite journal | author=Apte SS |title=A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 6 |pages= 981–5 |year= 2004 |pmid= 15094112 |doi= 10.1016/j.biocel.2004.01.014 }} | *{{cite journal | author=Apte SS |title=A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 6 |pages= 981–5 |year= 2004 |pmid= 15094112 |doi= 10.1016/j.biocel.2004.01.014 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Faivre L, Mégarbané A, Alswaid A |title=Homozygosity mapping of a Weill-Marchesani syndrome locus to chromosome 19p13.3-p13.2. |journal=Hum. Genet. |volume=110 |issue= 4 |pages= 366–70 |year= 2002 |pmid= 11941487 |doi= 10.1007/s00439-002-0689-3 |display-authors=etal}} | ||
*{{cite journal | | *{{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}} | ||
*{{cite journal | | *{{cite journal | vauthors=Brandenberger R, Wei H, Zhang S |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Fu GK, Wang JT, Yang J |title=Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes. |journal=Genomics |volume=84 |issue= 1 |pages= 205–10 |year= 2005 |pmid= 15203218 |doi= 10.1016/j.ygeno.2004.01.011 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Somerville RP, Jungers KA, Apte SS |title=Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation. |journal=J. Biol. Chem. |volume=279 |issue= 49 |pages= 51208–17 |year= 2005 |pmid= 15355968 |doi= 10.1074/jbc.M409036200 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Charrier L, Yan Y, Driss A |title=ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers. |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=288 |issue= 2 |pages= G346–53 |year= 2005 |pmid= 15358598 |doi= 10.1152/ajpgi.00262.2004 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Dagoneau N, Benoist-Lasselin C, Huber C |title=ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome. |journal=Am. J. Hum. Genet. |volume=75 |issue= 5 |pages= 801–6 |year= 2005 |pmid= 15368195 |doi= 10.1086/425231 | pmc=1182109 |display-authors=etal}} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{ | ==External links== | ||
* [https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=gene&part=weill-ms GeneReviews/NIH/NCBI/UW entry on Weill-Marchesani Syndrome] | |||
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M12.235 M12.235] | |||
* {{UCSC gene info|ADAMTS10}} | |||
{{Metalloproteinases}} | {{Metalloproteinases}} | ||
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[[Category:ADAMTS]] | |||
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Latest revision as of 17:48, 29 August 2017
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| Location (UCSC) | n/a | n/a | |||||
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A disintegrin and metalloproteinase with thrombospondin motifs 10 is an enzyme that in humans is encoded by the ADAMTS10 gene.[1]
This gene belongs to the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 motifs) family of zinc-dependent proteases. ADAMTS proteases are complex secreted enzymes containing a prometalloprotease domain of the reprolysin type attached to an ancillary domain with a highly conserved structure that includes at least one thrombospondin type 1 repeat. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. The product of this gene plays a major role in growth and in skin, lens, and heart development. It is also a candidate gene for autosomal recessive Weill-Marchesani syndrome.[1]
References
Further reading
- 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.
- Faivre L, Dollfus H, Lyonnet S, et al. (2004). "Clinical homogeneity and genetic heterogeneity in Weill-Marchesani syndrome". Am. J. Med. Genet. A. 123 (2): 204–7. doi:10.1002/ajmg.a.20289. PMID 14598350.
- Apte SS (2004). "A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family". Int. J. Biochem. Cell Biol. 36 (6): 981–5. doi:10.1016/j.biocel.2004.01.014. PMID 15094112.
- Faivre L, Mégarbané A, Alswaid A, et al. (2002). "Homozygosity mapping of a Weill-Marchesani syndrome locus to chromosome 19p13.3-p13.2". Hum. Genet. 110 (4): 366–70. doi:10.1007/s00439-002-0689-3. PMID 11941487.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Brandenberger R, Wei H, Zhang S, et al. (2005). "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.
- Fu GK, Wang JT, Yang J, et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics. 84 (1): 205–10. doi:10.1016/j.ygeno.2004.01.011. PMID 15203218.
- Somerville RP, Jungers KA, Apte SS (2005). "Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation". J. Biol. Chem. 279 (49): 51208–17. doi:10.1074/jbc.M409036200. PMID 15355968.
- Charrier L, Yan Y, Driss A, et al. (2005). "ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers". Am. J. Physiol. Gastrointest. Liver Physiol. 288 (2): G346–53. doi:10.1152/ajpgi.00262.2004. PMID 15358598.
- Dagoneau N, Benoist-Lasselin C, Huber C, et al. (2005). "ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome". Am. J. Hum. Genet. 75 (5): 801–6. doi:10.1086/425231. PMC 1182109. PMID 15368195.
External links
- GeneReviews/NIH/NCBI/UW entry on Weill-Marchesani Syndrome
- The MEROPS online database for peptidases and their inhibitors: M12.235
- Human ADAMTS10 genome location and ADAMTS10 gene details page in the UCSC Genome Browser.
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