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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46488

Title: Developing a microbial time–temperature indicator to monitor total volatile basic nitrogen change in chilled vacuum-packed grouper fillets. Journal of Food Processing and Preservation
Authors: Chia-Chi,Hsu
Chun-Hui,Wang
Ling-Chia,Wu
Cheng-Yuan,Hsi
Chin-Wen,Chi
Pen-Hui,Yin
Chun-Ju,Chang
Ming-Ta,Sung
Yau-Huei,Wei
Shing-Hwa,Lu
Hsin-Chen,Lee
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: Protein synthesis
Hypoxia-inducible factor-1α
Mitochondrial dysfunction
Adenosine monophosphate-activated protein kinase
Date: 2013
Issue Date: 2018-05-21T06:00:41Z
Publisher: Biochimica et Biophysica Acta (BBA) - General Subjects
Abstract: Abstract: Background
Hypoxia-inducible factor-1α (HIF-1α) is an important transcription factor that modulates cellular responses to hypoxia and also plays critical roles in cancer progression. Recently, somatic mutations and decreased copy number of mitochondrial DNA (mtDNA) were detected in hepatocellular carcinoma (HCC). These mutations were shown to have the potential to cause mitochondrial dysfunction. However, the effects and mechanisms of mitochondrial dysfunction on HIF-1α function are not fully understood. This study aims to explore the underlying mechanism by which mitochondrial dysfunction regulates HIF-1α expression.

Methods
Human hepatoma HepG2 cells were treated with various mitochondrial respiration inhibitors and an uncoupler, respectively, and the mRNA and protein expressions as well as transactivation activity of HIF-1α were determined. The role of AMP-activated protein kinase (AMPK) was further analyzed by compound C and AMPK knock-down.

Results
Treatments of mitochondrial inhibitors and an uncoupler respectively reduced both the protein level and transactivation activity of HIF-1α in HepG2 cells under normoxia or hypoxia. The mitochondrial dysfunction-repressed HIF-1α protein synthesis was associated with decreased phosphorylations of p70S6K and 4E-BP-1. Moreover, mitochondrial dysfunction decreased intracellular ATP content and elevated the phosphorylation of AMPK. Treatments with compound C, an AMPK inhibitor, and knock-down of AMPK partially rescued the mitochondrial dysfunction-repressed HIF-1α expression.

Conclusions
Mitochondrial dysfunctions resulted in reduced HIF-1α protein synthesis through AMPK-dependent manner in HepG2 cells.

General significance
Our results provided a mechanism for communication from mitochondria to the nucleus through AMPK-HIF-1α. Mitochondrial function is important for HIF-1α expression in cancer progression.
Relation: 1830(10) pp.4743-4751
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/46488
Appears in Collections:[食品科學系] 期刊論文

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