The E3 ubiquitin ligase Asb2β is downregulated in a mouse model of hypertrophic cardiomyopathy and targets desmin for proteasomal degradation
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- 作者：Tilo Thottakaraa ; b ; c ; 1 ; Felix W. Friedricha ; b ; 1 ; f.friedrich@uke.de" class="auth_mail" title="E-mail the corresponding author ; Silke Reischmanna ; b ; Simon Braumanna ; b ; Saskia Schlossareka ; b ; Elisabeth Krä ; mera ; b ; Denise Juhra ; Hartmut Schlü ; terd ; Jolanda van der Veldene ; f ; Julia Mü ; nchb ; c ; Monica Pattenb ; c ; Thomas Eschenhagena ; b ; Christel Moog-Lutzg ; h ; Lucie Carriera ; b ; l.carrier@uke.de" class="auth_mail" title="E-mail the corresponding author
- 关键词：Hypertrophic cardiomyopathy ; Asb2β ; Proteasome ; E3 ubiquitin ligase ; Desmin ; Filamin B
- 刊名：Journal of Molecular and Cellular Cardiology
- 出版年：2015
- 出版时间：October 2015
- 年：2015
- 卷：87
- 期：Complete
- 页码：214-224
- 全文大小：1931 K
文摘
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Asb2β was found to be the most downregulated muscle-specific E3 ligase in KI mice.
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The intermediate filament protein desmin was identified as a novel target of Asb2β.
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Mybpc3-KI HCM mice showed lower Asb2β and higher desmin protein levels
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Immunofluorescence analysis showed a co-localization of desmin and filamin B with Asb2β at the Z-disk of the sarcomere
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Septal myectomy samples of HCM patients also exhibited higher desmin levels and reduced proteasomal activity than non-failing hearts.
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