The cell adhesion molecule M-cadherin is specifically expressed in developing and regenerating, but not denervated skeletal muscle

Development ◽  
1993 ◽  
Vol 117 (4) ◽  
pp. 1409-1420 ◽  
Author(s):  
R. Moore ◽  
F.S. Walsh
Keyword(s):  
Skeletal Muscle ◽  
Tissue Distribution ◽  
Cell Adhesion Molecule ◽  
Muscle Denervation ◽  
Regulatory Factor ◽  
Myogenic Regulatory Factor ◽  
Adult Skeletal Muscle ◽  
Specific Tissue ◽  
Alpha Actin

The spatiotemporal distribution of M-cadherin mRNA has been determined by in situ hybridization in the mouse embryo and in adult skeletal muscle following experimental regeneration and denervation. M-cadherin mRNA is highly tissue specific and is found only in developing skeletal muscle. In contrast, N-cadherin mRNA has a broader tissue distribution in the embryo, being found on both neural elements and skeletal and cardiac muscle. M-cadherin is expressed in the myotomes shortly after they form, along with the myogenic regulatory factor myogenin. M-cadherin is expressed in muscles derived from the myotomes and is detected in forelimb bud precursor cells at embryonic day 11.5. In the latter case M-cadherin expression appears co-ordinately with that of myogenin and cardiac alpha-actin. Shortly before birth, M-cadherin expression is down regulated. M-cadherin can, however, be re-expressed following experimental regeneration of skeletal muscle. Here M-cadherin is transiently expressed on regenerating myoblasts but not myotubes. Following muscle denervation no evidence was found for re-expression of M-cadherin under conditions where there was strong expression of the nicotinic acetylcholine receptor on myofibres. The highly specific tissue distribution and unique developmental profile distinguishes M-cadherin from other cadherins and suggests a role in cell surface events during early myogenesis.

scholarly journals Myogenic Regulatory Factor Expression Is Downregulated Following Formoterol Stimulation In Thyroid Hormone Depleted Skeletal Muscle

2020 ◽  
Vol 52 (7S) ◽  
pp. 910-910
Author(s):  
Ryan A. Gordon ◽  
Gena D. Guerin ◽  
Emily L. Zumbro ◽  
Chase M. White ◽  
Dreanna M. McAdams ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Thyroid Hormone ◽  
Regulatory Factor ◽  
Myogenic Regulatory Factor ◽  
Factor Expression

Differential expression of myogenic regulatory factor MyoD in pacu skeletal muscle (Piaractus mesopotamicus Holmberg 1887: Serrasalminae, Characidae, Teleostei) during juvenile and adult growth phases

Micron ◽  
2008 ◽  
Vol 39 (8) ◽  
pp. 1306-1311 ◽  
Author(s):  
Fernanda Losi Alves de Almeida ◽  
Robson Francisco Carvalho ◽  
Danillo Pinhal ◽  
Carlos Roberto Padovani ◽  
Cesar Martins ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Differential Expression ◽  
Growth Phases ◽  
Regulatory Factor ◽  
Myogenic Regulatory Factor ◽  
Piaractus Mesopotamicus ◽  
Adult Growth

Flounder (Paralichthys olivaceus) FoxD1 and its regulation on the expression of myogenic regulatory factor, MyoD

Biologia ◽  
2012 ◽  
Vol 67 (5) ◽  
Author(s):  
Yuqing Zhang ◽  
Xungang Tan ◽  
Wei Sun ◽  
Pei-Jun Zhang
Keyword(s):  
Muscle Development ◽  
Paralichthys Olivaceus ◽  
Fish Muscle ◽  
Regulatory Factor ◽  
Myogenic Regulatory Factor ◽  
Functional Studies ◽  
And Function ◽  
Myod Expression ◽  
Adaxial Cells

AbstractIt has been reported that FoxD1 plays important roles in formation of several different tissues, such as retina and kidney in vertebrates. The function of FoxD1 in muscle development is, however, unclear although it is expressed in muscle cells in zebrafish. Muscles are the major tissue in fish, which serves as a rich protein source in our diet. To further understand the function of FoxD1 in fish muscle development, here we isolated and characterized the FoxD1 gene from flounder (Paralichthys olivaceus), a valuable sea food and an important fish species in aquaculture in Asia. We analyzed its expression pattern and function in regulating myogenic regulatory factor, MyoD, one of the earliest marker of myogenic commitment. In situ hybridization revealed that FoxD1 was expressed in the tailbud, adaxial cells, posterior intestine, forebrain, midbrain and half of the retina in flounder embryos. Functional studies demonstrated that when flounder FoxD1 was over-expressed in zebrafish by microinjection, MyoD expression was decreased, suggesting that FoxD1 may be involved in myogenesis by regulating the expression of MyoD.

Myogenic regulatory factor response to resistance exercise volume in skeletal muscle

2009 ◽  
Vol 108 (4) ◽  
pp. 771-778 ◽  
Author(s):  
Micah J. Drummond ◽  
Robert K. Conlee ◽  
Gary W. Mack ◽  
Sterling Sudweeks ◽  
G. Bruce Schaalje ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Resistance Exercise ◽  
Regulatory Factor ◽  
Myogenic Regulatory Factor

scholarly journals MYOD1 functions as a clock amplifier as well as a critical co-factor for downstream circadian gene expression in muscle

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Brian A Hodge ◽  
Xiping Zhang ◽  
Miguel A Gutierrez-Monreal ◽  
Yi Cao ◽  
David W Hammers ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Molecular Clock ◽  
Bimolecular Fluorescence Complementation ◽  
Regulatory Factor ◽  
Circadian Gene ◽  
Myogenic Regulatory Factor ◽  
E Box ◽  
Positive Modulator ◽  
Positive Core ◽  
Synergistic Regulation

In the present study we show that the master myogenic regulatory factor, MYOD1, is a positive modulator of molecular clock amplitude and functions with the core clock factors for expression of clock-controlled genes in skeletal muscle. We demonstrate that MYOD1 directly regulates the expression and circadian amplitude of the positive core clock factor Bmal1. We identify a non-canonical E-box element in Bmal1 and demonstrate that is required for full MYOD1-responsiveness. Bimolecular fluorescence complementation assays demonstrate that MYOD1 colocalizes with both BMAL1 and CLOCK throughout myonuclei. We demonstrate that MYOD1 and BMAL1:CLOCK work in a synergistic fashion through a tandem E-box to regulate the expression and amplitude of the muscle specific clock-controlled gene, Titin-cap (Tcap). In conclusion, these findings reveal mechanistic roles for the muscle specific transcription factor MYOD1 in the regulation of molecular clock amplitude as well as synergistic regulation of clock-controlled genes in skeletal muscle.

Myogenic Regulatory Factor Gene Expression Is Impaired In Obese Mice During Skeletal Muscle Regeneration

2014 ◽  
Vol 46 ◽  
pp. 638-639
Author(s):  
Lemuel A. Brown ◽  
Jillian F. Patton ◽  
Alyssa M. Papineau ◽  
Nicholas P. Greene ◽  
Tyrone A. Washington
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Muscle Regeneration ◽  
Skeletal Muscle Regeneration ◽  
Obese Mice ◽  
Regulatory Factor ◽  
Myogenic Regulatory Factor ◽  
Factor Gene

p38γ MAPK regulation of glucose transporter expression and glucose uptake in L6 myotubes and mouse skeletal muscle

2004 ◽  
Vol 286 (2) ◽  
pp. R342-R349 ◽  
Author(s):  
Richard C. Ho ◽  
Oscar Alcazar ◽  
Nobuharu Fujii ◽  
Michael F. Hirshman ◽  
Laurie J. Goodyear
Keyword(s):  
Skeletal Muscle ◽  
Glucose Uptake ◽  
Glucose Transporter ◽  
Adult Skeletal Muscle ◽  
Peripheral Tissues ◽  
L6 Myotubes ◽  
Regulation Of Contraction ◽  
Transporter Expression

Skeletal muscle expresses at least three p38 MAPKs (α, β, γ). However, no studies have examined the potential regulation of glucose uptake by p38γ, the isoform predominantly expressed in skeletal muscle and highly regulated by exercise. L6 myotubes were transfected with empty vector (pCAGGS), activating MKK6 (MKK6CA), or p38γ-specific siRNA. MKK6CA-transfected cells had higher rates of basal 2-deoxy-d-[3H]glucose (2-DG) uptake ( P < 0.05) but lower rates of 2,4-dinitrophenol (DNP)-stimulated glucose uptake, an uncoupler of oxidative phosphorylation that operates through an insulin-independent mechanism ( P < 0.05). These effects were reversed when MKK6CA cells were cotransfected with p38γ-specific siRNA. To determine whether the p38γ isoform is involved in the regulation of contraction-stimulated glucose uptake in adult skeletal muscle, the tibialis anterior muscles of mice were injected with pCAGGS or wild-type p38γ (p38γWT) followed by intramuscular electroporation. Basal and contraction-stimulated 2-DG uptake in vivo was determined 14 days later. Overexpression of p38γWT resulted in higher basal rates of glucose uptake compared with pCAGGS ( P < 0.05). Muscles overexpressing p38γWT showed a trend for lower in situ contraction-mediated glucose uptake ( P = 0.08) and significantly lower total GLUT4 levels ( P < 0.05). These data suggest that p38γ increases basal glucose uptake and decreases DNP- and contraction-stimulated glucose uptake, partially by affecting levels of glucose transporter expression in skeletal muscle. These findings are consistent with the hypothesis that activation of stress kinases such as p38 are negative regulators of stimulated glucose uptake in peripheral tissues.

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