File Download
 
Links for fulltext
(May Require Subscription)
 
Supplementary

Article: Tumor suppressor Alpha B-crystallin (CRYAB) associates with the cadherin/catenin adherens junction and impairs NPC progression-associated properties
  • Basic View
  • Metadata View
  • XML View
TitleTumor suppressor Alpha B-crystallin (CRYAB) associates with the cadherin/catenin adherens junction and impairs NPC progression-associated properties
 
AuthorsHuang, Z1
Cheng, Y1
Chiu, PM1
Cheung, FMF2
Nicholls, JM1
Kwong, DLW1
Lee, AWM2
Zabarovsky, ER5 4
Stanbridge, EJ3
Lung, HL1
Lung, ML1
 
Issue Date2012
 
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/onc
 
CitationOncogene, 2012, v. 31 n. 32, p. 3709-3720 [How to Cite?]
DOI: http://dx.doi.org/10.1038/onc.2011.529
 
AbstractAlpha B-crystallin (CRYAB) maps within the nasopharyngeal carcinoma (NPC) tumor-suppressive critical region 11q22-23 and its downregulation is significantly associated with the progression of NPC. However, little is known about the functional impact of CRYAB on NPC progression. In this study we evaluated the NPC tumor-suppressive and progression-associated functions of CRYAB. Activation of CRYAB suppressed NPC tumor formation in nude mice. Overexpression of CRYAB affected NPC progression-associated phenotypes such as loss of cell adhesion, invasion, interaction with the tumor microenvironment, invasive protrusion formation in three dimensional Matrigel culture, as well as expression of epithelial-mesenchymal transition-associated markers. CRYAB mediates this ability to suppress cancer progression by inhibition of E-cadherin cytoplasmic internalization and maintenance of beta-catenin in the membrane that subsequently reduces the levels of expression of critical downstream targets such as cyclin-D1 and c-myc. Both ectopically expressed and recombinant CRYAB proteins were associated with endogenous E-cadherin and beta-catenin, and, thus, the cadherin/catenin adherens junction. The CRYAB alpha-crystallin core domain is responsible for the interaction of CRYAB with both E-cadherin and beta-catenin. Taken together, these results indicate that CRYAB functions to suppress NPC progression by associating with the cadherin/catenin adherens junction and modulating the beta-catenin function.
 
ISSN0950-9232
2013 Impact Factor: 8.559
2013 SCImago Journal Rankings: 4.764
 
DOIhttp://dx.doi.org/10.1038/onc.2011.529
 
DC FieldValue
dc.contributor.authorHuang, Z
 
dc.contributor.authorCheng, Y
 
dc.contributor.authorChiu, PM
 
dc.contributor.authorCheung, FMF
 
dc.contributor.authorNicholls, JM
 
dc.contributor.authorKwong, DLW
 
dc.contributor.authorLee, AWM
 
dc.contributor.authorZabarovsky, ER
 
dc.contributor.authorStanbridge, EJ
 
dc.contributor.authorLung, HL
 
dc.contributor.authorLung, ML
 
dc.date.accessioned2012-05-29T06:14:33Z
 
dc.date.available2012-05-29T06:14:33Z
 
dc.date.issued2012
 
dc.description.abstractAlpha B-crystallin (CRYAB) maps within the nasopharyngeal carcinoma (NPC) tumor-suppressive critical region 11q22-23 and its downregulation is significantly associated with the progression of NPC. However, little is known about the functional impact of CRYAB on NPC progression. In this study we evaluated the NPC tumor-suppressive and progression-associated functions of CRYAB. Activation of CRYAB suppressed NPC tumor formation in nude mice. Overexpression of CRYAB affected NPC progression-associated phenotypes such as loss of cell adhesion, invasion, interaction with the tumor microenvironment, invasive protrusion formation in three dimensional Matrigel culture, as well as expression of epithelial-mesenchymal transition-associated markers. CRYAB mediates this ability to suppress cancer progression by inhibition of E-cadherin cytoplasmic internalization and maintenance of beta-catenin in the membrane that subsequently reduces the levels of expression of critical downstream targets such as cyclin-D1 and c-myc. Both ectopically expressed and recombinant CRYAB proteins were associated with endogenous E-cadherin and beta-catenin, and, thus, the cadherin/catenin adherens junction. The CRYAB alpha-crystallin core domain is responsible for the interaction of CRYAB with both E-cadherin and beta-catenin. Taken together, these results indicate that CRYAB functions to suppress NPC progression by associating with the cadherin/catenin adherens junction and modulating the beta-catenin function.
 
dc.description.naturelink_to_subscribed_fulltext
 
dc.identifier.citationOncogene, 2012, v. 31 n. 32, p. 3709-3720 [How to Cite?]
DOI: http://dx.doi.org/10.1038/onc.2011.529
 
dc.identifier.doihttp://dx.doi.org/10.1038/onc.2011.529
 
dc.identifier.eissn1476-5594
 
dc.identifier.epage3720
 
dc.identifier.hkuros199894
 
dc.identifier.hkuros210082
 
dc.identifier.issn0950-9232
2013 Impact Factor: 8.559
2013 SCImago Journal Rankings: 4.764
 
dc.identifier.issue32
 
dc.identifier.pmid22158051
 
dc.identifier.scopuseid_2-s2.0-84864946374
 
dc.identifier.spage3709
 
dc.identifier.urihttp://hdl.handle.net/10722/148670
 
dc.identifier.volume31
 
dc.languageeng
 
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/onc
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofOncogene
 
dc.subject.meshAdherens Junctions - metabolism
 
dc.subject.meshCadherins - metabolism
 
dc.subject.meshCarcinoma - metabolism - pathology
 
dc.subject.meshNasopharyngeal Neoplasms - metabolism - pathology
 
dc.subject.meshTumor Suppressor Proteins - metabolism
 
dc.titleTumor suppressor Alpha B-crystallin (CRYAB) associates with the cadherin/catenin adherens junction and impairs NPC progression-associated properties
 
dc.typeArticle
 
<?xml encoding="utf-8" version="1.0"?>
<item><contributor.author>Huang, Z</contributor.author>
<contributor.author>Cheng, Y</contributor.author>
<contributor.author>Chiu, PM</contributor.author>
<contributor.author>Cheung, FMF</contributor.author>
<contributor.author>Nicholls, JM</contributor.author>
<contributor.author>Kwong, DLW</contributor.author>
<contributor.author>Lee, AWM</contributor.author>
<contributor.author>Zabarovsky, ER</contributor.author>
<contributor.author>Stanbridge, EJ</contributor.author>
<contributor.author>Lung, HL</contributor.author>
<contributor.author>Lung, ML</contributor.author>
<date.accessioned>2012-05-29T06:14:33Z</date.accessioned>
<date.available>2012-05-29T06:14:33Z</date.available>
<date.issued>2012</date.issued>
<identifier.citation>Oncogene, 2012, v. 31 n. 32, p. 3709-3720</identifier.citation>
<identifier.issn>0950-9232</identifier.issn>
<identifier.uri>http://hdl.handle.net/10722/148670</identifier.uri>
<description.abstract>Alpha B-crystallin (CRYAB) maps within the nasopharyngeal carcinoma (NPC) tumor-suppressive critical region 11q22-23 and its downregulation is significantly associated with the progression of NPC. However, little is known about the functional impact of CRYAB on NPC progression. In this study we evaluated the NPC tumor-suppressive and progression-associated functions of CRYAB. Activation of CRYAB suppressed NPC tumor formation in nude mice. Overexpression of CRYAB affected NPC progression-associated phenotypes such as loss of cell adhesion, invasion, interaction with the tumor microenvironment, invasive protrusion formation in three dimensional Matrigel culture, as well as expression of epithelial-mesenchymal transition-associated markers. CRYAB mediates this ability to suppress cancer progression by inhibition of E-cadherin cytoplasmic internalization and maintenance of beta-catenin in the membrane that subsequently reduces the levels of expression of critical downstream targets such as cyclin-D1 and c-myc. Both ectopically expressed and recombinant CRYAB proteins were associated with endogenous E-cadherin and beta-catenin, and, thus, the cadherin/catenin adherens junction. The CRYAB alpha-crystallin core domain is responsible for the interaction of CRYAB with both E-cadherin and beta-catenin. Taken together, these results indicate that CRYAB functions to suppress NPC progression by associating with the cadherin/catenin adherens junction and modulating the beta-catenin function.</description.abstract>
<language>eng</language>
<publisher>Nature Publishing Group. The Journal&apos;s web site is located at http://www.nature.com/onc</publisher>
<relation.ispartof>Oncogene</relation.ispartof>
<subject.mesh>Adherens Junctions - metabolism</subject.mesh>
<subject.mesh>Cadherins - metabolism</subject.mesh>
<subject.mesh>Carcinoma - metabolism - pathology</subject.mesh>
<subject.mesh>Nasopharyngeal Neoplasms - metabolism - pathology</subject.mesh>
<subject.mesh>Tumor Suppressor Proteins - metabolism</subject.mesh>
<title>Tumor suppressor Alpha B-crystallin (CRYAB) associates with the cadherin/catenin adherens junction and impairs NPC progression-associated properties</title>
<type>Article</type>
<description.nature>link_to_subscribed_fulltext</description.nature>
<identifier.doi>10.1038/onc.2011.529</identifier.doi>
<identifier.pmid>22158051</identifier.pmid>
<identifier.scopus>eid_2-s2.0-84864946374</identifier.scopus>
<identifier.hkuros>199894</identifier.hkuros>
<identifier.hkuros>210082</identifier.hkuros>
<identifier.volume>31</identifier.volume>
<identifier.issue>32</identifier.issue>
<identifier.spage>3709</identifier.spage>
<identifier.epage>3720</identifier.epage>
<identifier.eissn>1476-5594</identifier.eissn>
<publisher.place>United Kingdom</publisher.place>
</item>
Author Affiliations
  1. The University of Hong Kong
  2. Pamela Youde Nethersole Eastern Hospital
  3. UC Irvine
  4. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences
  5. Södersjukhuset