Tumor suppressor Alpha B-crystallin (CRYAB) associates with the cadherin/catenin adherens junction and impairs NPC progression-associated properties

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 ev...

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Published inOncogene Vol. 31; no. 32; pp. 3709 - 3720
Main Authors Huang, Z, Cheng, Y, Chiu, P M, Cheung, F M F, Nicholls, J M, Kwong, D L-W, Lee, A W M, Zabarovsky, E R, Stanbridge, E J, Lung, H L, Lung, M L
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 09.08.2012
Nature Publishing Group
Subjects
631/67/581
631/80/79/2028
692/699/67/1536
adherens junctions
Adherens Junctions - metabolism
alpha -Crystallin
alpha-Crystallin B Chain - metabolism
Animals
Apoptosis
beta Catenin - metabolism
c-Myc protein
Cadherin
Cadherins - metabolism
Carcinoma - metabolism
Carcinoma - pathology
catenin
Cell Adhesion
Cell adhesion & migration
Cell Biology
Cell culture
Cell Line, Tumor
Cell Movement
Crystallin
Disease Progression
E-Cadherin
Female
Gene expression
Genetic code
Head & neck cancer
Human Genetics
Humans
Internal Medicine
Internalization
Invasiveness
Medicin och hälsovetenskap
Medicine
Medicine & Public Health
Mesenchyme
Mice
Mice, Inbred BALB C
Mice, Nude
Microenvironments
Myc protein
Nasopharyngeal cancer
Nasopharyngeal Carcinoma
Nasopharyngeal Neoplasms - metabolism
Nasopharyngeal Neoplasms - pathology
Neoplasm Invasiveness
Neoplasm Transplantation
Oncology
original-article
Phenotypes
Protein Transport
Proteins
Throat cancer
Tumor Burden
Tumor microenvironment
Tumor suppressor genes
Tumor Suppressor Proteins - metabolism
Tumors
β-Catenin
United States
β-catenin
E-cadherin
nasopharyngeal carcinoma
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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 β-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 β-catenin, and, thus, the cadherin/catenin adherens junction. The CRYAB α-crystallin core domain is responsible for the interaction of CRYAB with both E-cadherin and β-catenin. Taken together, these results indicate that CRYAB functions to suppress NPC progression by associating with the cadherin/catenin adherens junction and modulating the β-catenin function.
AbstractList 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.
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 β-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 β-catenin, and, thus, the cadherin/catenin adherens junction. The CRYAB α-crystallin core domain is responsible for the interaction of CRYAB with both E-cadherin and β-catenin. Taken together, these results indicate that CRYAB functions to suppress NPC progression by associating with the cadherin/catenin adherens junction and modulating the β-catenin function. [PUBLICATION 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 β-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 β-catenin, and, thus, the cadherin/catenin adherens junction. The CRYAB α-crystallin core domain is responsible for the interaction of CRYAB with both E-cadherin and β-catenin. Taken together, these results indicate that CRYAB functions to suppress NPC progression by associating with the cadherin/catenin adherens junction and modulating the β-catenin function.
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 β-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 β-catenin, and, thus, the cadherin/catenin adherens junction. The CRYAB α-crystallin core domain is responsible for the interaction of CRYAB with both E-cadherin and β-catenin. Taken together, these results indicate that CRYAB functions to suppress NPC progression by associating with the cadherin/catenin adherens junction and modulating the β-catenin function.
Alpha B-crystallin (CRYAB) maps within the nasopharyngeal carcinoma (NPC) tumor-suppressive critical region llq22-23 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 β-catenin in the membrane that subsequently reduces the levels of expression of critical downstream targets such as cyclin-Dl and c-myc. Both ectopically expressed and recombinant CRYAB proteins were associated with endogenous E-cadherin and b-catenin, and, thus, the cadherin/catenin adherens junction. The CRYAB α-crystallin core domain is responsible for the interaction of CRYAB with both E-cadherin and β-catenin. Taken together, these results indicate that CRYAB functions to suppress NPC progression by associating with the cadherin/catenin adherens junction and modulating the β-catenin function.
Alpha B-crystallin (CRYAB) maps within the nasopharyngeal carcinoma (NPC) tumor-suppressive critical region llq22-23 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 β-catenin in the membrane that subsequently reduces the levels of expression of critical downstream targets such as cyclin-Dl and c-myc. Both ectopically expressed and recombinant CRYAB proteins were associated with endogenous E-cadherin and b-catenin, and, thus, the cadherin/catenin adherens junction. The CRYAB α-crystallin core domain is responsible for the interaction of CRYAB with both E-cadherin and β-catenin. Taken together, these results indicate that CRYAB functions to suppress NPC progression by associating with the cadherin/catenin adherens junction and modulating the β-catenin function. Keywords: Alpha B-crystallin; nasopharyngealcarcinoma; E-cadherin; β-catenin
Audience Academic
Author Lee, A W M
Cheng, Y
Zabarovsky, E R
Kwong, D L-W
Lung, M L
Huang, Z
Stanbridge, E J
Lung, H L
Nicholls, J M
Chiu, P M
Cheung, F M F
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  fullname: Cheng, Y
  organization: Department of Clinical Oncology and Center for Cancer Research, University of Hong Kong
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  surname: Chiu
  fullname: Chiu, P M
  organization: Department of Clinical Oncology and Center for Cancer Research, University of Hong Kong
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  surname: Cheung
  fullname: Cheung, F M F
  organization: Department of Clinical Pathology, Pamela Youde Nethersole Eastern Hospital
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  surname: Nicholls
  fullname: Nicholls, J M
  organization: Department of Pathology, University of Hong Kong
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  organization: Department of Clinical Oncology, Pamela Youde Nethersole Eastern Hospital
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  surname: Zabarovsky
  fullname: Zabarovsky, E R
  organization: Department of Microbiology, Department of Clinical Science and Education, Tumor and Cell Biology, Sodersjukhuset, Karolinska Institute, Laboratory of Structural and Functional Genomics, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences
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  fullname: Stanbridge, E J
  organization: Department of Microbiology and Molecular Genetics, University of California
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  surname: Lung
  fullname: Lung, H L
  email: hllung2@hku.hk
  organization: Department of Clinical Oncology and Center for Cancer Research, University of Hong Kong
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Issue 32
Keywords β-catenin
E-cadherin
nasopharyngeal carcinoma
Language English
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PublicationTitle Oncogene
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Snippet Alpha B-crystallin ( CRYAB ) maps within the nasopharyngeal carcinoma (NPC) tumor-suppressive critical region 11q22-23 and its downregulation is significantly...
Alpha B-crystallin (CRYAB) maps within the nasopharyngeal carcinoma (NPC) tumor-suppressive critical region 11q22-23 and its downregulation is significantly...
Alpha B-crystallin (CRYAB) maps within the nasopharyngeal carcinoma (NPC) tumor-suppressive critical region llq22-23 and its downregulation is significantly...
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crossref
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SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 3709
SubjectTerms 631/67/581
631/80/79/2028
692/699/67/1536
adherens junctions
Adherens Junctions - metabolism
alpha -Crystallin
alpha-Crystallin B Chain - metabolism
Animals
Apoptosis
beta Catenin - metabolism
c-Myc protein
Cadherin
Cadherins - metabolism
Carcinoma - metabolism
Carcinoma - pathology
catenin
Cell Adhesion
Cell adhesion & migration
Cell Biology
Cell culture
Cell Line, Tumor
Cell Movement
Crystallin
Disease Progression
E-Cadherin
Female
Gene expression
Genetic code
Head & neck cancer
Human Genetics
Humans
Internal Medicine
Internalization
Invasiveness
Medicin och hälsovetenskap
Medicine
Medicine & Public Health
Mesenchyme
Mice
Mice, Inbred BALB C
Mice, Nude
Microenvironments
Myc protein
Nasopharyngeal cancer
Nasopharyngeal Carcinoma
Nasopharyngeal Neoplasms - metabolism
Nasopharyngeal Neoplasms - pathology
Neoplasm Invasiveness
Neoplasm Transplantation
Oncology
original-article
Phenotypes
Protein Transport
Proteins
Throat cancer
Tumor Burden
Tumor microenvironment
Tumor suppressor genes
Tumor Suppressor Proteins - metabolism
Tumors
β-Catenin
Title Tumor suppressor Alpha B-crystallin (CRYAB) associates with the cadherin/catenin adherens junction and impairs NPC progression-associated properties
URI https://link.springer.com/article/10.1038/onc.2011.529
https://www.ncbi.nlm.nih.gov/pubmed/22158051
https://www.proquest.com/docview/1032758438
https://www.proquest.com/docview/2641505328
https://search.proquest.com/docview/1033154408
https://search.proquest.com/docview/1034814942
http://kipublications.ki.se/Default.aspx?queryparsed=id:125064991
Volume 31
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