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Article ; Online: Decreased insulin-like growth factor-1 expression in response to mechanical loading is associated with skeletal muscle anabolic resistance in cancer cachexia.

Miyazaki, Mitsunori / Sawada, Atsushi / Sawamura, Daisuke / Yoshida, Susumu

Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society

2023 Volume 69-70, Page(s) 101536

Abstract: Objective: Cachexia is a systemic metabolic syndrome characterized by loss of body weight and skeletal muscle mass during chronic wasting diseases, such as cancer. Skeletal muscle in cancer cachexia is less responsive to anabolic factors including ... ...

Abstract	Objective: Cachexia is a systemic metabolic syndrome characterized by loss of body weight and skeletal muscle mass during chronic wasting diseases, such as cancer. Skeletal muscle in cancer cachexia is less responsive to anabolic factors including mechanical loading; however, the precise molecular mechanism is largely unknown. In this study, we examined the underlying mechanism of anabolic resistance in skeletal muscle in a cancer cachexia model. Methods: CD2F1 mice (male, 8 weeks old) were subcutaneously transplanted (1 × 10 Results: The hypertrophic response of skeletal muscle (increased skeletal muscle weight/protein synthesis efficiency and activation of mechanistic target of rapamycin complex 1 signaling) associated with mechanical overload was significantly suppressed during cancer cachexia. Screening of gene expression profile and pathway analysis using microarray revealed that blunted muscle protein synthesis was associated with cancer cachexia and was likely induced by downregulation of insulin-like growth factor-1 (IGF-1) and impaired activation of IGF-1-dependent signaling. Conclusions: These observations indicate that cancer cachexia induces resistance to muscle protein synthesis, which may be a factor for inhibiting the anabolic adaptation of skeletal muscle to physical exercise in cancer patients.
MeSH term(s)	Male ; Mice ; Animals ; Insulin-Like Growth Factor I/metabolism ; Cachexia/complications ; Cachexia/metabolism ; Muscle, Skeletal/metabolism ; Colonic Neoplasms/complications ; Colonic Neoplasms/metabolism ; Muscle Proteins/metabolism
Chemical Substances	Insulin-Like Growth Factor I (67763-96-6) ; Muscle Proteins
Language	English
Publishing date	2023-05-18
Publishing country	Scotland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1436781-6
ISSN	1532-2238 ; 1096-6374
ISSN (online)	1532-2238
ISSN	1096-6374
DOI	10.1016/j.ghir.2023.101536
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Article ; Online: Supplementing cultured human myotubes with hibernating bear serum results in increased protein content by modulating Akt/FOXO3a signaling.

Miyazaki, Mitsunori / Shimozuru, Michito / Tsubota, Toshio

PloS one

2022 Volume 17, Issue 1, Page(s) e0263085

Abstract: Hibernating bears remain in their dens for 5-7 months during winter and survive without eating or drinking while staying inactive. However, they maintain their physical functions with minimal skeletal muscle atrophy and metabolic dysfunction. In bears, ... ...

Abstract	Hibernating bears remain in their dens for 5-7 months during winter and survive without eating or drinking while staying inactive. However, they maintain their physical functions with minimal skeletal muscle atrophy and metabolic dysfunction. In bears, resistance to skeletal muscle atrophy during hibernation is likely mediated by seasonally altered systemic factors that are independent of neuromuscular activity. To determine whether there are components in bear serum that regulate protein and energy metabolism, differentiated human skeletal muscle cells were treated with bear serum (5% in DMEM/Ham's F-12, 24 h) collected during active summer (July) and hibernating winter (February) periods. The serum samples were collected from the same individual bears (Ursus thibetanus japonicus, n = 7 in each season). Total protein content in cultured skeletal muscle cells was significantly increased following a 24 h treatment with hibernating bear serum. Although the protein synthesis rate was not altered, the expression of MuRF1 protein, a muscle-specific E3 ubiquitin ligase was significantly decreased along with a concomitant activation of Akt/FOXO3a signaling. Increased levels of insulin-like growth factor-1 (IGF-1) were also observed in hibernating bear serum. These observations suggest that protein metabolism in cultured human myotubes may be altered when incubated with hibernating bear serum, with a significant increase in serum IGF-1 and diminished MuRF1 expression, a potential target of Akt/FOXO3a signaling. A protein sparing phenotype in cultured muscle cells by treatment with hibernating bear serum holds potential for the development of methods to prevent human muscle atrophy and related disorders.
MeSH term(s)	Animals ; Forkhead Box Protein O3/metabolism ; Hibernation ; Humans ; Muscle Fibers, Skeletal/metabolism ; Proto-Oncogene Proteins c-akt/metabolism ; Serum ; Signal Transduction ; Ursidae/blood
Chemical Substances	FOXO3 protein, human ; Forkhead Box Protein O3 ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2022-01-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0263085
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Article ; Online: Supplementing cultured human myotubes with hibernating bear serum results in increased protein content by modulating Akt/FOXO3a signaling.

Mitsunori Miyazaki / Michito Shimozuru / Toshio Tsubota

PLoS ONE, Vol 17, Iss 1, p e

2022 Volume 0263085

Abstract	Hibernating bears remain in their dens for 5-7 months during winter and survive without eating or drinking while staying inactive. However, they maintain their physical functions with minimal skeletal muscle atrophy and metabolic dysfunction. In bears, resistance to skeletal muscle atrophy during hibernation is likely mediated by seasonally altered systemic factors that are independent of neuromuscular activity. To determine whether there are components in bear serum that regulate protein and energy metabolism, differentiated human skeletal muscle cells were treated with bear serum (5% in DMEM/Ham's F-12, 24 h) collected during active summer (July) and hibernating winter (February) periods. The serum samples were collected from the same individual bears (Ursus thibetanus japonicus, n = 7 in each season). Total protein content in cultured skeletal muscle cells was significantly increased following a 24 h treatment with hibernating bear serum. Although the protein synthesis rate was not altered, the expression of MuRF1 protein, a muscle-specific E3 ubiquitin ligase was significantly decreased along with a concomitant activation of Akt/FOXO3a signaling. Increased levels of insulin-like growth factor-1 (IGF-1) were also observed in hibernating bear serum. These observations suggest that protein metabolism in cultured human myotubes may be altered when incubated with hibernating bear serum, with a significant increase in serum IGF-1 and diminished MuRF1 expression, a potential target of Akt/FOXO3a signaling. A protein sparing phenotype in cultured muscle cells by treatment with hibernating bear serum holds potential for the development of methods to prevent human muscle atrophy and related disorders.
Keywords	Medicine ; R ; Science ; Q
Subject code	571
Language	English
Publishing date	2022-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: Supplementing cultured human myotubes with hibernating bear serum results in increased protein content by modulating Akt/FOXO3a signaling

Mitsunori Miyazaki / Michito Shimozuru / Toshio Tsubota

PLoS ONE, Vol 17, Iss

2022 Volume 1

Abstract: Hibernating bears remain in their dens for 5–7 months during winter and survive without eating or drinking while staying inactive. However, they maintain their physical functions with minimal skeletal muscle atrophy and metabolic dysfunction. In bears, ... ...

Abstract	Hibernating bears remain in their dens for 5–7 months during winter and survive without eating or drinking while staying inactive. However, they maintain their physical functions with minimal skeletal muscle atrophy and metabolic dysfunction. In bears, resistance to skeletal muscle atrophy during hibernation is likely mediated by seasonally altered systemic factors that are independent of neuromuscular activity. To determine whether there are components in bear serum that regulate protein and energy metabolism, differentiated human skeletal muscle cells were treated with bear serum (5% in DMEM/Ham’s F-12, 24 h) collected during active summer (July) and hibernating winter (February) periods. The serum samples were collected from the same individual bears (Ursus thibetanus japonicus, n = 7 in each season). Total protein content in cultured skeletal muscle cells was significantly increased following a 24 h treatment with hibernating bear serum. Although the protein synthesis rate was not altered, the expression of MuRF1 protein, a muscle-specific E3 ubiquitin ligase was significantly decreased along with a concomitant activation of Akt/FOXO3a signaling. Increased levels of insulin-like growth factor-1 (IGF-1) were also observed in hibernating bear serum. These observations suggest that protein metabolism in cultured human myotubes may be altered when incubated with hibernating bear serum, with a significant increase in serum IGF-1 and diminished MuRF1 expression, a potential target of Akt/FOXO3a signaling. A protein sparing phenotype in cultured muscle cells by treatment with hibernating bear serum holds potential for the development of methods to prevent human muscle atrophy and related disorders.
Keywords	Medicine ; R ; Science ; Q
Subject code	571
Language	English
Publishing date	2022-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Regulation of protein and oxidative energy metabolism are down-regulated in the skeletal muscles of Asiatic black bears during hibernation.

Miyazaki, Mitsunori / Shimozuru, Michito / Kitaoka, Yu / Takahashi, Kenya / Tsubota, Toshio

Scientific reports

2022 Volume 12, Issue 1, Page(s) 19723

Abstract: Hibernating animals exhibit an unexplained physiological characteristic of skeletal muscles being atrophy resistance, in which case muscle mass and strength remain almost unchanged both before and after hibernation. In this study, we examined the ... ...

Abstract	Hibernating animals exhibit an unexplained physiological characteristic of skeletal muscles being atrophy resistance, in which case muscle mass and strength remain almost unchanged both before and after hibernation. In this study, we examined the alterations in the regulatory systems of protein and energy metabolism in the skeletal muscles of Asiatic black bears during hibernation. Skeletal muscle samples (vastus lateralis muscle) were collected from identical individuals (n = 8) during the active (July) and hibernating (February) periods, while histochemical and biochemical analyses were performed. We observed no significant alterations in body weight, muscle fiber size, and fiber type composition during the active and hibernating periods, indicating that the skeletal muscles of bears are very well preserved during hibernation. In hibernating bear skeletal muscles, both regulatory pathways of muscle protein synthesis (Akt/mechanistic target of rapamycin and mitogen-activated protein kinase systems) and proteolysis (ubiquitin-proteasome and autophagy systems) were down-regulated. Gene expression levels of factors regulating oxidative metabolism were also decreased in hibernating bear skeletal muscles. This is likely an adaptive strategy to minimize the energy wasting of amino acids and lipids during hibernation, which is accompanied by a prolonged period of disuse and starvation.
MeSH term(s)	Animals ; Hibernation/physiology ; Ursidae/physiology ; Muscular Atrophy/metabolism ; Muscle, Skeletal/metabolism ; Energy Metabolism ; Muscle Proteins/metabolism ; Oxidative Stress
Chemical Substances	Muscle Proteins
Language	English
Publishing date	2022-11-16
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-24251-0
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Article ; Online: Voluntary exercise prevents abnormal muscle mitochondrial morphology in cancer cachexia mice.

Kitaoka, Yu / Miyazaki, Mitsunori / Kikuchi, Shin

Physiological reports

2021 Volume 9, Issue 16, Page(s) e15016

Abstract: This study aimed to examine the effects of voluntary wheel running on cancer cachexia-induced mitochondrial alterations in mouse skeletal muscle. Mice bearing colon 26 adenocarcinoma (C26) were used as a model of cancer cachexia. C26 mice showed a lower ... ...

Abstract	This study aimed to examine the effects of voluntary wheel running on cancer cachexia-induced mitochondrial alterations in mouse skeletal muscle. Mice bearing colon 26 adenocarcinoma (C26) were used as a model of cancer cachexia. C26 mice showed a lower gastrocnemius and plantaris muscle weight, but 4 weeks of voluntary exercise rescued these changes. Further, voluntary exercise attenuated observed declines in the levels of oxidative phosphorylation proteins and activities of citrate synthase and cytochrome c oxidase in the skeletal muscle of C26 mice. Among mitochondrial morphology regulatory proteins, mitofusin 2 (Mfn2) and dynamin-related protein 1 (Drp1) were decreased in the skeletal muscle of C26 mice, but exercise resulted in similar improvements as seen in markers of mitochondrial content. In isolated mitochondria, 4-hydroxynonenal and protein carbonyls were elevated in C26 mice, but exercise blunted the increases in these markers of oxidative stress. In addition, electron microscopy revealed that exercise alleviated the observed increase in the percentage of damaged mitochondria in C26 mice. These results suggest that voluntary exercise effectively counteracts mitochondrial dysfunction to mitigate muscle loss in cachexia.
MeSH term(s)	Animals ; Cachexia/etiology ; Cachexia/prevention & control ; Citrate (si)-Synthase/metabolism ; Dynamins/metabolism ; Electron Transport Complex IV/metabolism ; GTP Phosphohydrolases/metabolism ; Male ; Mice ; Mitochondria, Muscle/metabolism ; Mitochondria, Muscle/ultrastructure ; Motor Activity ; Muscle, Skeletal/metabolism ; Muscle, Skeletal/ultrastructure ; Neoplasms/complications ; Oxidative Stress ; Physical Conditioning, Animal/methods ; Protein Carbonylation
Chemical Substances	Electron Transport Complex IV (EC 1.9.3.1) ; Citrate (si)-Synthase (EC 2.3.3.1) ; GTP Phosphohydrolases (EC 3.6.1.-) ; Mfn2 protein, mouse (EC 3.6.1.-) ; Dnm1l protein, mouse (EC 3.6.5.5) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2021-08-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2724325-4
ISSN	2051-817X ; 2051-817X
ISSN (online)	2051-817X
ISSN	2051-817X
DOI	10.14814/phy2.15016
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Article ; Online: Growth factor-dependent and independent regulation of skeletal muscle mass - Is IGF-1 necessary for skeletal muscle hypertrophy? -

Mitsunori Miyazaki

Journal of Physical Fitness and Sports Medicine, Vol 2, Iss 1, Pp 101-

2013 Volume 106

Abstract: Pituitary growth hormone (GH) and insulin-like growth factor-1 (IGF-1) play a critical role in the regulation of postnatal organ growth and overall body size. IGF-1 has been indicated as a very effective anabolic agent, and thus considered a critical ... ...

Abstract	Pituitary growth hormone (GH) and insulin-like growth factor-1 (IGF-1) play a critical role in the regulation of postnatal organ growth and overall body size. IGF-1 has been indicated as a very effective anabolic agent, and thus considered a critical regulator of skeletal muscle hypertrophy in response to increased workload such as resistance exercise. In contrast, recent studies using a genetic model of IGF-1/IGF-1 receptor have indicated that functional IGF-1-dependent mechanisms are not an absolute requirement for growth/hypertrophy in mature skeletal muscle. In this brief review, classic and recent aspects in hormonal/growth factor-dependent regulation of skeletal muscle mass are discussed. This review will particularly focus on 1) functional requirements of IGF-1 regulation in skeletal muscle hypertrophy and 2) cellular mechanisms in the regulation of protein synthesis in skeletal muscle.
Keywords	growth hormone ; insulin-like growth factor-1 ; protein synthesis ; mammalian target of rapamycin ; mechanical load ; Sports medicine ; RC1200-1245 ; Physiology ; QP1-981
Subject code	610
Language	English
Publishing date	2013-04-01T00:00:00Z
Publisher	Japanese Society of Physical Fitness and Sports Medicine
Document type	Article ; Online
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Article: Non-tuberculous mycobacterial disease associated with

Komine, Takeshi / Ihara, Hyogo / Inohana, Mari / Kwok, Jennifer Caroline / Shimizu, Akane / Terasawa, Tsumugi / Miyazaki, Ayaka / Srivorakul, Saralee / Iwao, Hajime / Harada, Sachiko / Yoshida, Mitsunori / Hoshino, Yoshihiko / Kurata, Osamu / Fukano, Hanako / Wada, Shinpei

Frontiers in veterinary science

2023 Volume 10, Page(s) 1248288

Abstract: Introduction: Mycobacterium montefiorense: Methods: Nine : Results: The microbiological and chemical characteristics of the : Conclusion: This study contributes to our understanding of the genetic diversity and phenotypic characteristics ... ...

Abstract	Introduction: Mycobacterium montefiorense Methods: Nine Results: The microbiological and chemical characteristics of the Conclusion: This study contributes to our understanding of the genetic diversity and phenotypic characteristics of
Language	English
Publishing date	2023-10-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2834243-4
ISSN	2297-1769
ISSN	2297-1769
DOI	10.3389/fvets.2023.1248288
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Article ; Online: Langerhans cell sarcoma arising after antecedent Langerhans cell histiocytosis in lymphoepithelial sialadenitis of Sjögren's syndrome.

Mihara, Yumi / Miura, Shiro / Mori, Ayaka / Miyazaki, Atsushi / Nagayama, Hiroki / Kitanosono, Hideaki / Soeda, Momoko / Sato, Shunsuke / Ito, Masahiro / Yamakawa, Mitsunori

Pathology international

2022 Volume 72, Issue 7, Page(s) 379–381

MeSH term(s)	Histiocytosis, Langerhans-Cell/complications ; Humans ; Langerhans Cell Sarcoma ; Sialadenitis/etiology ; Sjogren's Syndrome/complications
Language	English
Publishing date	2022-05-18
Publishing country	Australia
Document type	Letter
ZDB-ID	1194850-4
ISSN	1440-1827 ; 1320-5463
ISSN (online)	1440-1827
ISSN	1320-5463
DOI	10.1111/pin.13232
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Article ; Online: Transient activation of mTORC1 signaling in skeletal muscle is independent of Akt1 regulation.

Miyazaki, Mitsunori / Moriya, Nobuki / Takemasa, Tohru

Physiological reports

2020 Volume 8, Issue 19, Page(s) e14599

Abstract: The regulation of cellular protein synthesis is a critical determinant of skeletal muscle growth and hypertrophy in response to an increased workload such as resistance exercise. The mechanistic target of rapamycin complex 1 (mTORC1) and its upstream ... ...

Abstract	The regulation of cellular protein synthesis is a critical determinant of skeletal muscle growth and hypertrophy in response to an increased workload such as resistance exercise. The mechanistic target of rapamycin complex 1 (mTORC1) and its upstream protein kinase Akt1 have been implicated as a central signaling pathway that regulates protein synthesis in the skeletal muscle; however, the precise molecular regulation of mTORC1 activity is largely unknown. This study employed germline Akt1 knockout (KO) mice to examine whether upstream Akt1 regulation is necessary for the acute activation of mTORC1 signaling in the plantaris muscle following mechanical overload. The phosphorylation states of S6 kinase 1, ribosomal protein S6, and eukaryotic translation initiation factor 4E-binding protein 1 which show the functional activity of mTORC1 signaling, were significantly increased in the skeletal muscle of both wildtype and Akt1 KO mice following an acute bout (3 and 12 hr) of mechanical overload. Akt1 deficiency did not affect load-induced alteration of insulin-like growth factor-1 (IGF-1)/IGF receptor mRNA expression. Also, no effect of Akt1 deficiency was observed on the overload-induced increase in the gene expressions of pax7 and myogenic regulatory factor of myogenin. These observations show that the upstream IGF-1/Akt1 regulation is dispensable for the acute activation of mTORC1 signaling and regulation of satellite cells in response to mechanical overload.
MeSH term(s)	Animals ; Hypertrophy/metabolism ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Mice ; Multiprotein Complexes/metabolism ; Muscle Development/drug effects ; Muscle Development/physiology ; Muscle Proteins/metabolism ; Muscle, Skeletal/metabolism ; Protein Biosynthesis/physiology ; Signal Transduction/physiology
Chemical Substances	Multiprotein Complexes ; Muscle Proteins ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1)
Language	English
Publishing date	2020-10-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2724325-4
ISSN	2051-817X ; 2051-817X
ISSN (online)	2051-817X
ISSN	2051-817X
DOI	10.14814/phy2.14599
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