Repetitive restriction of muscle blood flow enhances mTOR signaling pathways in a rat model View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2016-02-01

AUTHORS

Toshiaki Nakajima, Tomohiro Yasuda, Seiichiro Koide, Tatsuya Yamasoba, Syotaro Obi, Shigeru Toyoda, Yoshiaki Sato, Teruo Inoue, Yutaka Kano

ABSTRACT

Skeletal muscle is a plastic organ that adapts its mass to various stresses by affecting pathways that regulate protein synthesis and degradation. This study investigated the effects of repetitive restriction of muscle blood flow (RRMBF) on microvascular oxygen pressure (PmvO2), mammalian target of rapamycin (mTOR) signaling pathways, and transcripts associated with proteolysis in rat skeletal muscle. Eleven-week-old male Wistar rats under anesthesia underwent six RRMBF consisting of an external compressive force of 100 mmHg for 5 min applied to the proximal portion of the right thigh, each followed by 3 min rest. During RRMBF, PmvO2 was measured by phosphorescence quenching techniques. The total RNA and protein of the tibialis anterior muscle were obtained from control rats, and rats treated with RRMBF 0–6 h after the stimuli. The protein expression and phosphorylation of various signaling proteins were determined by western blotting. The mRNA expression level was measured by real-time RT-PCR analysis. The total muscle weight increased in rats 0 h after RRMBF, but not in rats 1–6 h. During RRMBF, PmvO2 significantly decreased (36.1 ± 5.7 to 5.9 ± 1.7 torr), and recovered at rest period. RRMBF significantly increased phosphorylation of p70 S6-kinase (p70S6k), a downstream target of mTOR, and ribosomal protein S6 1 h after the stimuli. The protein level of REDD1 and phosphorylation of AMPK and MAPKs did not change. The mRNA expression levels of FOXO3a, MuRF-1, and myostatin were not significantly altered. These results suggested that RRMBF significantly decreased PmvO2, and enhanced mTOR signaling pathways in skeletal muscle using a rat model, which may play a role in diminishing muscle atrophy under various conditions in human studies. More... »

PAGES

1685-1695

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00380-016-0801-6

DOI

http://dx.doi.org/10.1007/s00380-016-0801-6

DIMENSIONS

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PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26833042


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29 schema:description Skeletal muscle is a plastic organ that adapts its mass to various stresses by affecting pathways that regulate protein synthesis and degradation. This study investigated the effects of repetitive restriction of muscle blood flow (RRMBF) on microvascular oxygen pressure (PmvO2), mammalian target of rapamycin (mTOR) signaling pathways, and transcripts associated with proteolysis in rat skeletal muscle. Eleven-week-old male Wistar rats under anesthesia underwent six RRMBF consisting of an external compressive force of 100 mmHg for 5 min applied to the proximal portion of the right thigh, each followed by 3 min rest. During RRMBF, PmvO2 was measured by phosphorescence quenching techniques. The total RNA and protein of the tibialis anterior muscle were obtained from control rats, and rats treated with RRMBF 0–6 h after the stimuli. The protein expression and phosphorylation of various signaling proteins were determined by western blotting. The mRNA expression level was measured by real-time RT-PCR analysis. The total muscle weight increased in rats 0 h after RRMBF, but not in rats 1–6 h. During RRMBF, PmvO2 significantly decreased (36.1 ± 5.7 to 5.9 ± 1.7 torr), and recovered at rest period. RRMBF significantly increased phosphorylation of p70 S6-kinase (p70S6k), a downstream target of mTOR, and ribosomal protein S6 1 h after the stimuli. The protein level of REDD1 and phosphorylation of AMPK and MAPKs did not change. The mRNA expression levels of FOXO3a, MuRF-1, and myostatin were not significantly altered. These results suggested that RRMBF significantly decreased PmvO2, and enhanced mTOR signaling pathways in skeletal muscle using a rat model, which may play a role in diminishing muscle atrophy under various conditions in human studies.
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36 MAPKs
37 MuRF-1
38 PmvO2
39 REDD1
40 RNA
41 RT-PCR analysis
42 S6 kinase
43 S6-1
44 Western blotting
45 Wistar rats
46 analysis
47 anesthesia
48 anterior muscle
49 atrophy
50 blood flow
51 blotting
52 compressive force
53 conditions
54 control rats
55 degradation
56 downstream targets
57 effect
58 expression
59 expression levels
60 external compressive force
61 flow
62 force
63 human studies
64 levels
65 mRNA expression levels
66 mTOR
67 male Wistar rats
68 mammalian target
69 mass
70 microvascular oxygen pressure
71 min
72 min rest
73 mmHg
74 model
75 muscle
76 muscle atrophy
77 muscle blood flow
78 muscle weight
79 myostatin
80 organs
81 oxygen pressure
82 p70 S6 kinase
83 pathway
84 period
85 phosphorescence quenching techniques
86 phosphorylation
87 phosphorylation of AMPK
88 plastic organ
89 portion
90 pressure
91 protein
92 protein expression
93 protein levels
94 protein synthesis
95 proteolysis
96 proximal portion
97 quenching technique
98 rapamycin
99 rat model
100 rat skeletal muscle
101 rats
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104 real-time RT-PCR analysis
105 rest
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109 right thigh
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119 thigh
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