File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: When MT1-MMP meets ADAMs

TitleWhen MT1-MMP meets ADAMs
Authors
KeywordsADAM15
ADAM9
Angiogenesis
FGF signaling
MT1-MMP
Osteogenesis
Issue Date2012
PublisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/cc
Citation
Cell Cycle, 2012, v. 11 n. 15, p. 2793-2798 How to Cite?
AbstractMT1-MMP is a membrane-tethered enzyme capable of remodeling extracellular matrix. MT1-MMP-deficient mice exhibit systematic defects during development, especially in craniofacial development characterized by retarded calvarial bone formation. Recently, we identified MT1-MMP as a critical positive modulator of FGF signaling during intramembranous ossification. MT1-MMP cleaves ADAM9 to protect FGFR2 from ectodomain shedding. Depletion of ADAM9 in MT1-MMP-deficient mice significantly rescued the calvarial defects via restoring FGF signaling. Interestingly, this regulatory mechanism seems to be highly tissue-specific, as defective FGF2-induced corneal angiogenesis in Mmp14-/- mice could not be rescued by removal of ADAM9. In addition, MT1-MMP also cleaves another ADAM family member, ADAM15. Our current findings not only present a novel regulatory mechanism for FGF signaling but also reveal a functional crosstalk between MMP and ADAM families. Better understanding of the interplay between ADAMs and MT1-MMP and its consequences for signaling pathways will provide new insights into therapeutic approaches for the management of developmental disorders and various diseases, such as cancer. © 2012 Landes Bioscience.
Persistent Identifierhttp://hdl.handle.net/10722/163620
ISSN
2015 Impact Factor: 3.952
2015 SCImago Journal Rankings: 2.244
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWong, HLXen_HK
dc.contributor.authorCao, Ren_HK
dc.contributor.authorJin, Gen_HK
dc.contributor.authorChan, KMen_HK
dc.contributor.authorCao, Yen_HK
dc.contributor.authorZhou, Zen_HK
dc.date.accessioned2012-09-12T03:16:56Z-
dc.date.available2012-09-12T03:16:56Z-
dc.date.issued2012en_HK
dc.identifier.citationCell Cycle, 2012, v. 11 n. 15, p. 2793-2798en_HK
dc.identifier.issn1538-4101en_HK
dc.identifier.urihttp://hdl.handle.net/10722/163620-
dc.description.abstractMT1-MMP is a membrane-tethered enzyme capable of remodeling extracellular matrix. MT1-MMP-deficient mice exhibit systematic defects during development, especially in craniofacial development characterized by retarded calvarial bone formation. Recently, we identified MT1-MMP as a critical positive modulator of FGF signaling during intramembranous ossification. MT1-MMP cleaves ADAM9 to protect FGFR2 from ectodomain shedding. Depletion of ADAM9 in MT1-MMP-deficient mice significantly rescued the calvarial defects via restoring FGF signaling. Interestingly, this regulatory mechanism seems to be highly tissue-specific, as defective FGF2-induced corneal angiogenesis in Mmp14-/- mice could not be rescued by removal of ADAM9. In addition, MT1-MMP also cleaves another ADAM family member, ADAM15. Our current findings not only present a novel regulatory mechanism for FGF signaling but also reveal a functional crosstalk between MMP and ADAM families. Better understanding of the interplay between ADAMs and MT1-MMP and its consequences for signaling pathways will provide new insights into therapeutic approaches for the management of developmental disorders and various diseases, such as cancer. © 2012 Landes Bioscience.en_HK
dc.languageeng-
dc.publisherLandes Bioscience. The Journal's web site is located at http://www.landesbioscience.com/journals/ccen_HK
dc.relation.ispartofCell Cycleen_HK
dc.subjectADAM15en_HK
dc.subjectADAM9en_HK
dc.subjectAngiogenesisen_HK
dc.subjectFGF signalingen_HK
dc.subjectMT1-MMPen_HK
dc.subjectOsteogenesisen_HK
dc.titleWhen MT1-MMP meets ADAMsen_HK
dc.typeArticleen_HK
dc.identifier.emailChan, KM: ming616@graduate.hku.hken_HK
dc.identifier.emailZhou, Z: zhongjun@hkucc.hku.hken_HK
dc.identifier.authorityChan, KM=rp01757en_HK
dc.identifier.authorityZhou, Z=rp00503en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.4161/cc.20949en_HK
dc.identifier.pmid22801544-
dc.identifier.scopuseid_2-s2.0-84864538245en_HK
dc.identifier.hkuros206818-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84864538245&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume11en_HK
dc.identifier.issue15en_HK
dc.identifier.spage2793en_HK
dc.identifier.epage2798en_HK
dc.identifier.eissn1551-4005-
dc.identifier.isiWOS:000307118000013-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWong, HLX=55248144900en_HK
dc.identifier.scopusauthoridCao, R=7103341338en_HK
dc.identifier.scopusauthoridJin, G=55224723000en_HK
dc.identifier.scopusauthoridChan, KM=8631854500en_HK
dc.identifier.scopusauthoridCao, Y=7404524342en_HK
dc.identifier.scopusauthoridZhou, Z=8631856300en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats