αA- and αB-crystallins interact with caspase-3 and bax to guard mouse lens development

W. F. Hu, L. Gong, Z. Cao, H. Ma, W. Ji, M. Deng, M. Liu, X. H. Hu, P. Chen, Q. Yan, H. G. Chen, J. Liu, S. Sun, L. Zhang, J. P. Liu, E. Wawrousek, D. W.C. Li

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

he small heat shock protein, α-crystallin, exists in two isoforms, αA and αB, and displays strong ability against stress-induced apoptosis. Regarding their functional mechanisms, we and others have demonstrated that they are able to regulate members in both caspase and Bcl-2 families. In addition, we have also shown that αA and αB may display differential anti-apoptotic mechanisms under certain stress conditions. While αA-crystallin regulates activation of the AKT signaling pathway, αB negatively regulates the MAPK pathway to suppress apoptosis induced by UV and oxidative stress. Although previous studies revealed that αA and αB could regulate members in both caspase and Bcl-2 families, the molecular mechanism, especially the in vivo regulation still waits to be elucidated. In the present communication, we present both in vitro and in vivo evidence to further demonstrate the regulation of caspase-3 and Bax by αA and αB. First, Surface Plasmon Resonance (SPR) and yeast two-hybrid selection analysis demonstrate that αA and αB directly bind to caspase-3 and Bax with differential affinities. Second, immunohistochemistry reveals that αA and αB regulate caspase-3 and Bax at different developmental stages of mouse embryo. Third, coimmunoprecipitation shows that αA and αB form in vivo interacting complexes with caspase-3 and Bax. Together, our results further confirm that αA and αB regulate caspase-3 and Bax in vitro and in vivo to regulate lens differentiation.

Original languageEnglish (US)
Pages (from-to)177-187
Number of pages11
JournalCurrent Molecular Medicine
Volume12
Issue number2
DOIs
StatePublished - Feb 1 2012

Fingerprint

Crystallins
Caspase 3
Lenses
Caspase 2
Caspases
Apoptosis
Small Heat-Shock Proteins
Oxidative stress
Surface Plasmon Resonance
Surface plasmon resonance
Yeast
Protein Isoforms
Oxidative Stress
Embryonic Structures
Yeasts
Chemical activation
Immunohistochemistry
Communication

Keywords

  • Apoptosis
  • Bax
  • Caspase-3
  • Cataract
  • Lens differentition
  • Lens epithelial cells
  • αA-crystallin
  • αB-crystallin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology

Cite this

αA- and αB-crystallins interact with caspase-3 and bax to guard mouse lens development. / Hu, W. F.; Gong, L.; Cao, Z.; Ma, H.; Ji, W.; Deng, M.; Liu, M.; Hu, X. H.; Chen, P.; Yan, Q.; Chen, H. G.; Liu, J.; Sun, S.; Zhang, L.; Liu, J. P.; Wawrousek, E.; Li, D. W.C.

In: Current Molecular Medicine, Vol. 12, No. 2, 01.02.2012, p. 177-187.

Research output: Contribution to journalArticle

Hu, WF, Gong, L, Cao, Z, Ma, H, Ji, W, Deng, M, Liu, M, Hu, XH, Chen, P, Yan, Q, Chen, HG, Liu, J, Sun, S, Zhang, L, Liu, JP, Wawrousek, E & Li, DWC 2012, 'αA- and αB-crystallins interact with caspase-3 and bax to guard mouse lens development', Current Molecular Medicine, vol. 12, no. 2, pp. 177-187. https://doi.org/10.2174/156652412798889036
Hu, W. F. ; Gong, L. ; Cao, Z. ; Ma, H. ; Ji, W. ; Deng, M. ; Liu, M. ; Hu, X. H. ; Chen, P. ; Yan, Q. ; Chen, H. G. ; Liu, J. ; Sun, S. ; Zhang, L. ; Liu, J. P. ; Wawrousek, E. ; Li, D. W.C. / αA- and αB-crystallins interact with caspase-3 and bax to guard mouse lens development. In: Current Molecular Medicine. 2012 ; Vol. 12, No. 2. pp. 177-187.
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AU - Ma, H.

AU - Ji, W.

AU - Deng, M.

AU - Liu, M.

AU - Hu, X. H.

AU - Chen, P.

AU - Yan, Q.

AU - Chen, H. G.

AU - Liu, J.

AU - Sun, S.

AU - Zhang, L.

AU - Liu, J. P.

AU - Wawrousek, E.

AU - Li, D. W.C.

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AB - he small heat shock protein, α-crystallin, exists in two isoforms, αA and αB, and displays strong ability against stress-induced apoptosis. Regarding their functional mechanisms, we and others have demonstrated that they are able to regulate members in both caspase and Bcl-2 families. In addition, we have also shown that αA and αB may display differential anti-apoptotic mechanisms under certain stress conditions. While αA-crystallin regulates activation of the AKT signaling pathway, αB negatively regulates the MAPK pathway to suppress apoptosis induced by UV and oxidative stress. Although previous studies revealed that αA and αB could regulate members in both caspase and Bcl-2 families, the molecular mechanism, especially the in vivo regulation still waits to be elucidated. In the present communication, we present both in vitro and in vivo evidence to further demonstrate the regulation of caspase-3 and Bax by αA and αB. First, Surface Plasmon Resonance (SPR) and yeast two-hybrid selection analysis demonstrate that αA and αB directly bind to caspase-3 and Bax with differential affinities. Second, immunohistochemistry reveals that αA and αB regulate caspase-3 and Bax at different developmental stages of mouse embryo. Third, coimmunoprecipitation shows that αA and αB form in vivo interacting complexes with caspase-3 and Bax. Together, our results further confirm that αA and αB regulate caspase-3 and Bax in vitro and in vivo to regulate lens differentiation.

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