Ferulic acid regulates muscle fiber type formation through the Sirt1/AMPK signaling pathway

2019 ◽  
Vol 10 (1) ◽  
pp. 259-265 ◽  
Author(s):  
Xiaoling Chen ◽  
Yafei Guo ◽  
Gang Jia ◽  
Hua Zhao ◽  
Guangmang Liu ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Signaling Pathway ◽  
Muscle Fiber ◽  
Fiber Type ◽  
Muscle Fiber Type ◽  
Ampk Signaling ◽  
Slow Twitch ◽  
Fast Twitch

Ferulic acid promotes slow-twitch and inhibits fast-twitch myofiber formation via Sirt1/AMPK.

scholarly journals Up-regulation of bone morphogenetic protein and its signaling molecules following castration of bulls and their association with intramuscular fat content in Korean cattle

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Da Jin Sol Jung ◽  
Myunggi Baik
Keyword(s):  
Bone Morphogenetic Protein ◽  
Signaling Pathway ◽  
Muscle Fiber ◽  
Fiber Type ◽  
Glycolytic Enzyme ◽  
Bmp Signaling ◽  
Muscle Fiber Type ◽  
Mrna Levels ◽  
Korean Cattle ◽  
Morphogenetic Protein

AbstractWe evaluated whether castration affects bone morphogenetic protein 2 (BMP2) level and the expression of its signaling molecules in Korean cattle bulls. We also checked whether castration affects the expression of muscle fiber type and oxidative and glycolytic enzyme genes. Enzyme-linked immunosorbent assays revealed that steers had higher plasma BMP2 and leptin concentrations than bulls. Quantitative real-time PCR showed that steers had higher mRNA levels of the lysyl oxidase gene, a downstream target of the BMP signaling pathway, in the longissimus thoracis (LT) muscle. Steers had higher adipogenic peroxisome proliferator-activated receptor gamma and lipogenic fatty acid binding protein 4 mRNA levels in the LT than bulls. Steers had lower mRNA levels for several muscle fiber type 1 genes and fiber type 2A myosin heavy chain 2 gene than bulls. Steers had higher mRNA levels of the glycolytic enzyme phosphoglycerate kinase 1 gene than bulls. Transcript levels of oxidative enzyme genes did not differ between bulls and steers. Regression analysis revealed a positive association between plasma BMP2 levels and intramuscular fat (IMF) content in the steer group. These findings suggest that upregulation of the BMP signaling pathway in response to castration induces increased adipogenic gene expression, contributing to the increased IMF deposition observed in castrated animals.

Muscle fiber type distribution and architecture of the cat diaphragm

1983 ◽  
Vol 55 (5) ◽  
pp. 1386-1392 ◽  
Author(s):  
G. C. Sieck ◽  
R. R. Roy ◽  
P. Powell ◽  
C. Blanco ◽  
V. R. Edgerton ◽  
...  
Keyword(s):  
Muscle Fiber ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Muscle Fiber Type ◽  
Diaphragmatic Muscle ◽  
Band Area ◽  
Type Composition ◽  
Abdominal Surface ◽  
Fiber Type Distribution ◽  
Fast Twitch

Three types of diaphragmatic muscle fibers were identified histochemically in the sternal, costal, and crural regions of the cat diaphragm. Differences in the proportion of each muscle fiber type were observed between the abdominal and thoracic surfaces of the diaphragm but not among the different regions. A higher percentage of slow-twitch oxidative fibers was noted on the abdominal surface, whereas more fast-twitch fibers (fast-twitch oxidative-glycolytic and fast-twitch glycolytic) were found on the thoracic surface. Differences in muscle architecture were observed between diaphragmatic regions, but not between abdominal and thoracic sides. Overall, muscle fibers were longer in the crural regions, with the longest fibers being found in the crossing-band area of the crura. In the costal regions, fibers were longest in the center and became shorter toward the ventral and dorsal extent of these regions. Fiber lengths were similar throughout the sternal region. In each diaphragmatic region, the length of fibers extended from the origin of the muscle to its insertion. We conclude that functional differences between diaphragmatic regions could be attributed to fiber length and/or orientation, but not to differences in fiber-type composition.

scholarly journals Mdfi Promotes C2C12 Cell Differentiation and Positively Modulates Fast-to-Slow-Twitch Muscle Fiber Transformation

2021 ◽  
Vol 9 ◽  
Author(s):  
Bo Huang ◽  
Yiren Jiao ◽  
Yifan Zhu ◽  
Zuocheng Ning ◽  
Zijian Ye ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Muscle Fiber ◽  
Fiber Type ◽  
C2c12 Cell ◽  
C2c12 Cells ◽  
Muscle Fiber Type ◽  
Rna Seq ◽  
Type Transformation ◽  
Slow Twitch Muscle ◽  
Slow Twitch

Muscle development requires myoblast differentiation and muscle fiber formation. Myod family inhibitor (Mdfi) inhibits myogenic regulatory factors in NIH3T3 cells, but how Mdfi regulates myoblast myogenic development is still unclear. In the present study, we constructed an Mdfi-overexpression (Mdfi-OE) C2C12 cell line by the CRISPR/Cas9 system and performed RNA-seq on Mdfi-OE and wild-type (WT) C2C12 cells. The RNA-seq results showed that the calcium signaling pathway was the most significant. We also established the regulatory networks of Mdfi-OE on C2C12 cell differentiation and muscle fiber type transformation and identified hub genes. Further, both RNA-seq and experimental verification demonstrated that Mdfi promoted C2C12 cell differentiation by upregulating the expression of Myod, Myog, and Myosin. We also found that the positive regulation of Mdfi on fast-to-slow-twitch muscle fiber transformation is mediated by Myod, Camk2b, and its downstream genes, such as Pgc1a, Pdk4, Cs, Cox4, Acadm, Acox1, Cycs, and Atp5a1. In conclusion, our results demonstrated that Mdfi promotes C2C12 cell differentiation and positively modulates fast-to-slow-twitch muscle fiber transformation. These findings further our understanding of the regulatory mechanisms of Mdfi in myogenic development and muscle fiber type transformation. Our results suggest potential therapeutic targets for muscle- and metabolic-related diseases.

scholarly journals Skeletal muscle and fiber type-specific intramyocellular lipid accumulation in obese mice

2021 ◽  
Author(s):  
Nejc Umek ◽  
Simon Horvat ◽  
Erika Cvetko
Keyword(s):  
Muscle Fiber ◽  
Lipid Accumulation ◽  
High Fat Diet ◽  
Fiber Type ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Intramyocellular Lipid ◽  
Obese Mice ◽  
Slow Twitch ◽  
Fast Twitch

In obesity, accumulation of lipid droplets in skeletal muscle fibers and a shift towards fast muscle fiber types can both contribute to insulin resistance. However, it is not yet clear how intramyocellular lipid accumulation and fiber type changes are associated. Therefore, we investigated to what extent the lipids accumulated in a fiber type-specific manner in the functionally similar fast-, intermediate- and slow‑twitch gastrocnemius, plantaris, and soleus muscles, respectively, in high-fat diet-induced obese 54-week-old female C57BL/6JOlaHsd mice (n=9) compared to control standard-diet-treated lean mice (n=9). A high-fat diet was administered for 26 weeks. Fiber-type specific intramyocellular lipid content analysis and muscle fiber typing were performed using histochemical analysis of lipids with Sudan Black and immunohistochemical analysis of myosin heavy chains on serial sections of skeletal muscles. Compared to the lean mice, the lipid accumulation was most prominent in types 2a and 2x/d fibers (p<0.05) of fast-twitch gastrocnemius and intermediate plantaris muscles in the obese mice, while in slow-twitch soleus muscle, there was no significant lipid accumulation in the obese animals. Furthermore, the slow-twitch soleus muscle of the obese mice with no significant change in muscle fiber diameters exhibited the most pronounced shift towards fast-type myosin heavy chain isoform expression (p<0.05). In contrast, the fast-twitch and intermediate-twitch gastrocnemius and plantaris muscles, respectively, in which the muscle fiber diameters increased (p<0.05), were more resistant toward myosin heavy chain expression changes. In conclusion, we demonstrated both muscle- and fiber-type specificity in intramyocellular lipid accumulation in obese mice, suggesting that in obesity, similar muscle fiber types in different muscles accumulate lipids differentially.

Slow to fast alterations in skeletal muscle fibers caused by clenbuterol, a beta 2-receptor agonist

1988 ◽  
Vol 254 (6) ◽  
pp. E726-E732 ◽  
Author(s):  
R. J. Zeman ◽  
R. Ludemann ◽  
T. G. Easton ◽  
J. D. Etlinger
Keyword(s):  
Muscle Fiber ◽  
Receptor Agonist ◽  
Fiber Type ◽  
Fiber Types ◽  
Cross Sectional ◽  
Type Composition ◽  
Slow Twitch ◽  
Beta 2 ◽  
Slow Twitch Fibers ◽  
Fast Twitch

Chronic treatment of rats with clenbuterol, a beta 2-receptor agonist (8–12 wk), caused hypertrophy of histochemically identified fast- but not slow-twitch fibers within the soleus, while the mean areas of both fiber types were increased in the extensor digitorum longus (EDL). In contrast, treatment with the beta 2-receptor antagonist, butoxamine, reduced fast-twitch fiber size in both muscles. In the solei and to a lesser extent in the EDLs, the ratio of the number of fast- to slow-twitch fibers was increased by clenbuterol, while the opposite was observed with butoxamine. The muscle fiber hypertrophy observed in the EDL was accompanied by parallel increases in maximal tetanic tension and muscle cross-sectional area, while in the solei, progressive increases in rates of force development and relaxation toward values typical of fast-twitch muscles were also observed. Our results suggest a role of beta 2-receptors in regulating muscle fiber type composition as well as growth.

scholarly journals Mouse Skeletal Muscle Fiber-Type-Specific Macroautophagy and Muscle Wasting Are Regulated by a Fyn/STAT3/Vps34 Signaling Pathway

Cell Reports ◽  
2012 ◽  
Vol 1 (5) ◽  
pp. 557-569 ◽  
Author(s):  
Eijiro Yamada ◽  
Claire C. Bastie ◽  
Hiroshi Koga ◽  
Yichen Wang ◽  
Ana Maria Cuervo ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Signaling Pathway ◽  
Muscle Fiber ◽  
Muscle Wasting ◽  
Fiber Type ◽  
Skeletal Muscle Fiber ◽  
Muscle Fiber Type ◽  
Mouse Skeletal Muscle

scholarly journals Fnip1 regulates skeletal muscle fiber type specification, fatigue resistance, and susceptibility to muscular dystrophy

2014 ◽  
Vol 112 (2) ◽  
pp. 424-429 ◽  
Author(s):  
Nicholas L. Reyes ◽  
Glen B. Banks ◽  
Mark Tsang ◽  
Daciana Margineantu ◽  
Haiwei Gu ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscular Dystrophy ◽  
Muscle Fiber ◽  
Skeletal Muscles ◽  
Fiber Type ◽  
Skeletal Muscle Fiber ◽  
Muscle Fiber Type ◽  
Type I ◽  
Slow Twitch ◽  
Type Specification

Mammalian skeletal muscle is broadly characterized by the presence of two distinct categories of muscle fibers called type I “red” slow twitch and type II “white” fast twitch, which display marked differences in contraction strength, metabolic strategies, and susceptibility to fatigue. The relative representation of each fiber type can have major influences on susceptibility to obesity, diabetes, and muscular dystrophies. However, the molecular factors controlling fiber type specification remain incompletely defined. In this study, we describe the control of fiber type specification and susceptibility to metabolic disease by folliculin interacting protein-1 (Fnip1). Using Fnip1 null mice, we found that loss of Fnip1 increased the representation of type I fibers characterized by increased myoglobin, slow twitch markers [myosin heavy chain 7 (MyH7), succinate dehydrogenase, troponin I 1, troponin C1, troponin T1], capillary density, and mitochondria number. Cultured Fnip1-null muscle fibers had higher oxidative capacity, and isolated Fnip1-null skeletal muscles were more resistant to postcontraction fatigue relative to WT skeletal muscles. Biochemical analyses revealed increased activation of the metabolic sensor AMP kinase (AMPK), and increased expression of the AMPK-target and transcriptional coactivator PGC1α in Fnip1 null skeletal muscle. Genetic disruption of PGC1α rescued normal levels of type I fiber markers MyH7 and myoglobin in Fnip1-null mice. Remarkably, loss of Fnip1 profoundly mitigated muscle damage in a murine model of Duchenne muscular dystrophy. These results indicate that Fnip1 controls skeletal muscle fiber type specification and warrant further study to determine whether inhibition of Fnip1 has therapeutic potential in muscular dystrophy diseases.

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