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Fiber‐type specificity of cancer cachexia‐induced muscle wasting is phosphorylated p70S6K‐dependent
Author(s) -
Tanaka Minoru,
Matsumoto Tomohiro,
Sugimoto Ken,
Fujino Hidemi
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.lb487
Subject(s) - wasting , cachexia , medicine , endocrinology , phosphorylation , soleus muscle , cancer cachexia , chemistry , cancer , skeletal muscle , biochemistry
The purpose of the present study is to investigate the differences between slow‐ and fast‐twitch muscles in cancer cachexia‐induced muscle wasting. Twelve male Wistar rats were randomly divided into two groups; control and cancer cachexia‐induced group. The cancer cachexia‐induced rats received an intraperitoneal injection of AH‐130 ascites hepatoma cells. The serum, the soleus and plantaris muscles were collected nine days after injection. Then, the expression levels of TNF‐α, p70S6K, FoxO1, FoxO3a, IL‐6, Atrogin‐1, and MuRF‐1 were measured. The cachexia‐induced rats resulted in a loss in body weight and muscle mass, and an increase in the expression level of TNF‐α in serum. In addition, the mass in fast ‐twitch muscle decreased significantly higher than that in slow‐twitch muscle. The levels of Atrogin‐1 and MuRF‐1 expression, which are the indicators related to protein degradation, increased in the cachexia‐induced group compared with the control group. However, there were no significant differences in Atrogin‐1 and MuRF‐1expression between slow‐ and fast‐twitch muscles. The expression level of phosphorylated p70S6K, which is one of the indicators related to protein synthesis, decreased in the cachexia‐induced group. In addition, the expression level of phosphorylated p70S6K in the cachexia‐induced group was significantly lower in fast‐twitch than in slow‐twitch muscles. These results indicated that cancer cachexia‐induced both in slow‐ and fast‐twitch muscle wasting might be caused by increased protein degradation factors whereas preferential fast‐twitch muscle wasting depended on the suppression of phosphorylated p70S6K expression, which was different from slow muscle wasting. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .