関: MRF

WordNet

be a contributing factor; "make things factor into a companys profitability"
any of the numbers (or symbols) that form a product when multiplied together
an independent variable in statistics
anything that contributes causally to a result; "a number of factors determined the outcome"
consider as relevant when making a decision; "You must factor in the recent developments" (同)factor in, factor out
resolve into factors; "a quantum computer can factor the number 15" (同)factor in, factor out
an event known to have happened or something known to have existed; "your fears have no basis in fact"; "how much of the story is fact and how much fiction is hard to tell"
a concept whose truth can be proved; "scientific hypotheses are not facts"
a piece of information about circumstances that exist or events that have occurred; "first you must collect all the facts of the case"
a statement or assertion of verified information about something that is the case or has happened; "he supported his argument with an impressive array of facts"
any of various controls or devices for regulating or controlling fluid flow, pressure, temperature, etc.
an official responsible for control and supervision of a particular activity or area of public interest

PrepTutorEJDIC

(…の)『要因』,(…を生み出す)要素《+『in』+『名』(do『ing』)》 / 囲数,約数 / 代理人,《おもに英》仲買人 / =factorize
〈C〉『事実』,実際にある(あった)事 / 〈U〉真相,真実(truth) / 《the~》(法律用語で)犯行
取り締まり人;調整者 / 調整装置

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/01/22 02:41:20」(JST)

wiki en

Myogenic regulatory factors are basic helix-loop-helix (bHLH) transcription factors that regulate myogenesis: MyoD, Myf5, myogenin, and MRF4.^[1]

These proteins contain a conserved basic DNA binding domain that binds the E box DNA motif.^[2] They dimerize with other HLH containing proteins through an HLH-HLH interaction.^[3]

References

^ Perry R, Rudnick M (2000). "Molecular mechanisms regulating myogenic determination and differentiation". Front Biosci 5: D750–67. doi:10.2741/Perry. PMID 10966875.
^ Weintraub H, Davis R, Tapscott S, Thayer M, Krause M, Benezra R, Blackwell T, Turner D, Rupp R, Hollenberg S (1991). "The myoD gene family: nodal point during specification of the muscle cell lineage". Science 251 (4995): 761–6. doi:10.1126/science.1846704. PMID 1846704.
^ Barndt R, Zhuang Y (1999). "Controlling lymphopoiesis with a combinatorial E-protein code". Cold Spring Harb Symp Quant Biol 64: 45–50. doi:10.1101/sqb.1999.64.45. PMID 11232321.

External links

Myogenic Regulatory Factors at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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1. 抗酸菌易感染性を示すメンデル型遺伝性疾患：特異的な遺伝子異常 mendelian susceptibility to mycobacterial diseases specific defects
2. 血友病患者における第VIIIおよび第IX因子阻害物質 factor viii and factor ix inhibitors in patients with hemophilia
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5. 血管新生阻害剤の概要 overview of angiogenesis inhibitors

English Journal

Rearing temperature induces changes in muscle growth and gene expression in juvenile pacu (Piaractus mesopotamicus).

Gutierrez de Paula T1, de Almeida FL2, Carani FR3, Vechetti-Júnior IJ4, Padovani CR5, Salomão RA6, Mareco EA7, Dos Santos VB8, Dal-Pai-Silva M9.Author information 1São Paulo State University, UNESP, Institute of Biosciences, Department of Morphology, 18618-970 Botucatu, SP, Brazil. Electronic address: ttgutierrez@gmail.com.2State University of Maringa, Biological Sciences Center, Department of Morphological Sciences, 18618-970 Botucatu, SP, Brazil. Electronic address: fernandalosi@gmail.com.3São Paulo State University, UNESP, Institute of Biosciences, Department of Morphology, 18618-970 Botucatu, SP, Brazil. Electronic address: fcarani@gmail.com.4São Paulo State University, UNESP, Institute of Biosciences, Department of Morphology, 18618-970 Botucatu, SP, Brazil. Electronic address: ijvechetti@ibb.unesp.br.5São Paulo State University, Institute of Biosciences, Department of Biostatistics, 18618-970 Botucatu, SP, Brazil. Electronic address: bioestatistica@ibb.unesp.br.6São Paulo State University, Aquaculture Center (CAUNESP), 14884-900 Jaboticabal, SP, Brazil. Electronic address: rondi_salomao@hotmail.com.7São Paulo State University, UNESP, Institute of Biosciences, Department of Morphology, 18618-970 Botucatu, SP, Brazil. Electronic address: edsonmareco@gmail.com.8Sao Paulo Agency for Agribusiness Technology-APTA-Pole High Sorocabana, 19015-970, Post office box: 298, Presidente Prudente, SP, Brazil. Electronic address: vander@apta.sp.gov.br.9São Paulo State University, UNESP, Institute of Biosciences, Department of Morphology and CAUNESP, 18618-970 Botucatu, Sao Paulo, Brazil. Electronic address: maeli@ibb.unesp.br.AbstractPacu (Piaractus mesopotamicus) is a fast-growing fish that is extensively used in Brazilian aquaculture programs and shows a wide range of thermal tolerance. Because temperature is an environmental factor that influences the growth rate of fish and is directly related to muscle plasticity and growth, we hypothesized that different rearing temperatures in juvenile pacu, which exhibits intense muscle growth by hyperplasia, can potentially alter the muscle growth patterns of this species. The aim of this study was to analyze the muscle growth characteristics together with the expression of the myogenic regulatory factors MyoD and myogenin and the growth factor myostatin in juvenile pacu that were submitted to different rearing temperatures. Juvenile fish (1.5g weight) were distributed in tanks containing water and maintained at 24°C (G24), 28°C (G28) and 32°C (G32) (three replicates for each group) for 60days. At days 30 and 60, the fish were anesthetized and euthanized, and muscle samples (n=12) were collected for morphological, morphometric and gene expression analyses. At day 30, the body weight and standard length were lower for G24 than for G28 and G32. Muscle fiber frequency in the <25μm class was significantly higher in G24, and the >50μm class was lower in G24. MyoD gene expression was higher in G24 compared with that in G28 and G32, and myogenin and myostatin mRNA levels were higher in G24 than G28. At day 60, the body weight and the standard length were higher in G32 but lower in G24. The frequency distribution of the <25μm diameter muscle fibers was higher in G24, and that of the >50μm class was lower in G24. MyoD mRNA levels were higher in G24 and G32, and myogenin mRNA levels were similar between G24 and G28 and between G24 and G32 but were higher in G28 compared to G32. The myostatin mRNA levels were similar between the studied temperatures. In light of our results, we conclude that low rearing temperature altered the expression of muscle growth-related genes and induced a delay in muscle growth in juvenile pacu (P. mesopotamicus). Our study provides a clear example of thermally induced phenotypic plasticity in pacu fish and shows that changing the rearing temperature during the juvenile stage can have a considerable effect on gene expression and muscle growth in this species.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.Comp Biochem Physiol B Biochem Mol Biol.2014 Mar;169:31-7. doi: 10.1016/j.cbpb.2013.12.004. Epub 2013 Dec 21.
Pacu (Piaractus mesopotamicus) is a fast-growing fish that is extensively used in Brazilian aquaculture programs and shows a wide range of thermal tolerance. Because temperature is an environmental factor that influences the growth rate of fish and is directly related to muscle plasticity and growth
PMID 24365169

Methionine improves breast muscle growth and alters myogenic gene expression in broilers.

Wen C, Chen X, Chen GY, Wu P, Chen YP, Zhou YM, Wang T.Author information College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, 210095, P. R. China.AbstractTo investigate the mechanism underlying the regulatory effect of Met on broiler growth, this study evaluated the performance, organ development, serum parameters, myogenic gene expression, and myostatin gene exon 1 region methylation of broilers in response to dietary Met status. A total of 192 1-day-old Arbor Acres broiler chicks were randomly allocated to 2 dietary treatments. Control starter and finisher diets contained 0.50% and 0.43% Met, respectively. Corresponding values for a +Met treatment were 0.60% and 0.53%. The birds receiving the +Met diets had a greater (P<0.05) G:F throughout the experiment. The +Met diets increased (P<0.05) the relative weight of breast muscle and the concentrations of uric acid and triglyceride in serum at 42 d of age, whereas those of other parameters were not affected by treatments. Increased myogenic factor 5 (Myf5) and myocyte enhancer factor2B (MEF2B) and decreased myostatin mRNA expression were observed in broilers fed the +Met diets (P<0.05). However, myostatin gene exon 1 region methylation was not significantly different between groups. In conclusion, broilers fed the +Met diets increased breast muscle growth that was reflected by expected expressions of myostatin, Myf5 and MEF2B genes.
Journal of animal science.J Anim Sci.2014 Feb 3. [Epub ahead of print]
To investigate the mechanism underlying the regulatory effect of Met on broiler growth, this study evaluated the performance, organ development, serum parameters, myogenic gene expression, and myostatin gene exon 1 region methylation of broilers in response to dietary Met status. A total of 192 1-da
PMID 24492548

Regulation of the Follistatin Gene by RSPO-LGR4 Signaling via Activation of the WNT/β-Catenin Pathway in Skeletal Myogenesis.

Han XH, Jin YR, Tan L, Kosciuk T, Lee JS, Yoon JK.Author information Program in Stem Cell Biology and Regenerative Medicine, Center for Molecular Medicine, Maine Medical Center Research Institute, Scarborough, Maine, USA.AbstractWNT signaling plays multiple roles in skeletal myogenesis during gestation and postnatal stages. The R-spondin (RSPO) family of secreted proteins and their cognate receptors, members of leucine-rich repeat-containing G protein-coupled receptor (LGR) family, have emerged as new regulatory components of the WNT signaling pathway. We previously showed that RSPO2 promoted myogenic differentiation via activation of WNT/β-catenin signaling in mouse myoblast C2C12 cells in vitro. However, the molecular mechanism by which RSPO2 regulates myogenic differentiation is unknown. Herein, we show that depletion of the LGR4 receptor severely disrupts myogenic differentiation and significantly diminishes the response to RSPO2 in C2C12 cells, showing a requirement of LGR4 in RSPO signaling during myogenic differentiation. We identify the transforming growth factor β (TGF-β) antagonist follistatin (Fst) as a key mediator of RSPO-LGR4 signaling in myogenic differentiation. We further demonstrate that Fst is a direct target of the WNT/β-catenin pathway. Activation and inactivation of β-catenin induced and inhibited Fst expression, respectively, in both C2C12 cells and mouse embryos. Specific TCF/LEF1 binding sites within the promoter and intron 1 region of the Fst gene were required for RSPO2 and WNT/β-catenin-induced Fst expression. This study uncovers a molecular cross talk between WNT/β-catenin and TGF-β signaling pivotal in myogenic differentiation.
Molecular and cellular biology.Mol Cell Biol.2014 Feb;34(4):752-64. doi: 10.1128/MCB.01285-13. Epub 2013 Dec 16.
WNT signaling plays multiple roles in skeletal myogenesis during gestation and postnatal stages. The R-spondin (RSPO) family of secreted proteins and their cognate receptors, members of leucine-rich repeat-containing G protein-coupled receptor (LGR) family, have emerged as new regulatory components
PMID 24344199

Japanese Journal

Expression of specific IGFBPs is associated with those of the proliferating and differentiating markers in regenerating rat plantaris muscle

Yamaguchi Akihiko,Sakuma Kunihiro,Fujikawa Takahiko [他]
The journal of physiological sciences 63(1), 71-77, 2013-01
NAID 40019538847

Selective Androgen Receptor Modulator, YK11, Regulates Myogenic Differentiation of C2C12 Myoblasts by Follistatin Expression

Kanno Yuichiro,Ota Rumi,Someya Kousuke,Kusakabe Taichi,Kato Keisuke,Inouye Yoshio
Biological and Pharmaceutical Bulletin 36(9), 1460-1465, 2013
… The myogenic differentiation of C2C12 myoblast cells is induced by the novel androgen receptor (AR) partial agonist, (17α,20E)-17,20-[(1-methoxyethylidene)bis-(oxy)]-3-oxo-19-norpregna-4,20-diene-21-carboxylic acid methyl ester (YK11), as well as by dihydrotestosterone (DHT). … In this study, we further investigated the mechanism by which YK11 induces myogenic differentiation of C2C12 cells. …
NAID 130003361518

In Vivo Real-Time Imaging of Exogenous HGF-Triggered Cell Migration in Rat Intact Soleus Muscles

Ishido Minenori,Kasuga Norikatsu
ACTA HISTOCHEMICA ET CYTOCHEMICA 45(3), 193-199, 2012
… The transplantation of myogenic cells is a potentially effective therapy for muscular dystrophy. … However, this therapy has achieved little success because the diffusion of transplanted myogenic cells is limited. … Hepatocyte growth factor (HGF) is one of the primary triggers to induce myogenic cell migration in vitro. …
NAID 130001854245