Chia Nan University of Pharmacy & Science Institutional Repository:Item 310902800/31037
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    Title: Cardiac fibrosis in mouse expressing DsRed tetramers involves chronic autophagy and proteasome degradation insufficiency
    Authors: Chen, Tsung-Hsien
    Chen, Mei-Ru
    Chen, Tzu-Yin
    Wu, Tzu-Chin
    Liu, Shan-Wen
    Hsu, Ching-Han
    Liou, Gan-Guang
    Kao, Yu-Ying
    Dong, Guo-Chung
    Chu, Pao-Hsien
    Liao, Jiunn-Wang
    Lin, Kurt Ming-Chao
    Contributors: Natl Hlth Res Inst, Inst Biomed Engn & Nanomed
    Natl Tsing Hua Univ, Inst Biomed Engn & Environm Sci
    Natl Hlth Res Inst, Inst Mol & Genom Med
    Chia Nan Univ Pharm & Sci, Dept Biotechnol
    Chang Gung Univ, Coll Med, Chang Gung Mem Hosp, Dept Cardiol
    Natl Chung Hsing Univ, Grad Inst Vet Pathobiol
    Keywords: protein aggregation
    cardiac hypertrophy
    heart failure
    Pathology Section
    Date: 2016-08
    Issue Date: 2018-01-18 11:40:20 (UTC+8)
    Publisher: Impact Journals Llc
    Abstract: Proteinopathy in the heart which often manifests excessive misfolded/aggregated proteins in cardiac myocytes can result in severe fibrosis and heart failure. Here we developed a mouse model, which transgenically express tetrameric DsRed, a red fluorescent protein (RFP), in an attempt to mimic the pathological mechanisms of cardiac fibrosis. Whilst DsRed is expressed and forms aggregation in most mouse organs, certain pathological defects are specifically recapitulated in cardiac muscle cells including mitochondria damages, aggresome-like residual bodies, excessive ubiquitinated proteins, and the induction of autophagy. The proteinopathy and cellular injuries caused by DsRed aggregates may be due to impaired or overburdened ubiquitin-proteasome system and autophagy-lysosome systems. We further identified that DsRed can be ubiquitinated and associated with MuRF1, a muscle-specific E3 ligase. Concomitantly, an activation of NF-kappa B signaling and a strong TIMP1 induction were noted, suggesting that RFP-induced fibrosis was augmented by a skewed balance between TIMP1 and MMPs. Taken together, our study highlights the molecular consequences of uncontrolled protein aggregation leading to congestive heart failure, and provides novel insights into fibrosis formation that can be exploited for improved therapy.
    Appears in Collections:[Dept. of Biotechnology (including master's program)] Periodical Articles

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