Talk:Musculoskeletal System - Muscle Development
centrosome proteins - muscle cell differentiation
- Centrosome proteins form an insoluble perinuclear matrix during muscle cell differentiation. Srsen V, Fant X, Heald R, Rabouille C, Merdes A. BMC Cell Biol. 2009 Apr 21;10:28. PMID: 19383121 | BMC Cell Biol.
- Nuclei of non-muscle cells bind centrosome proteins upon fusion with differentiating myoblasts. Fant X, Srsen V, Espigat-Georger A, Merdes A. PLoS One. 2009 Dec 14;4(12):e8303. PMID: 20011525
- Reorganization of microtubule nucleation during muscle differentiation. Bugnard E, Zaal KJ, Ralston E. Cell Motil Cytoskeleton. 2005 Jan;60(1):1-13.PMID: 15532031
Skeletal Dysplasias Associated with Mild Myopathy—A Clinical and Molecular Review
Good figures for bone
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2875749/?tool=pubmed
Phenotypes induced by NM causing α-skeletal muscle actin mutants in fibroblasts, Sol 8 myoblasts and myotubes
http://www.biomedcentral.com/1756-0500/2/40/
The chemokine Sdf-1 and its receptor Cxcr4 are required for formation of muscle in zebrafish
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1904199
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1904199/pdf/1471-213X-7-54.pdf
Kindlin-2 is required for myocyte elongation and is essential for myogenesis
http://www.biomedcentral.com/1471-2121/9/36
Integrins are required for normal muscle differentiation and disruptions in integrin signaling result in human muscle disease. The intracellular components that regulate integrin function during myogenesis are poorly understood. Unc-112 is an integrin-associated protein required for muscle development in C. elegans. To better understand the intracellular effectors of integrin signaling in muscle, we examined the mammalian homolog of Unc-112, kindlin-2.
Schematic of kindlin-2 function during early myogenesis. A. Undifferentiated C2C12 cells with typical fibroblast-like morphology B. Upon change to differentiation media, control cells withdraw from the cell cycle and elongate. In cells with reduced levels of kindlin-2, cells fail to elongate, and instead maintain a "pro-migratory" phenotype. C. By differentiation day 4, elongated control cells fuse into multinucleated myotubes. Reduced levels of kindlin-2 result in failure of myotube formation, likely as a result of decreased elongation, inadequate cell adhesion and impaired myoblast fusion. One mechanism underlying these alterations is a failure of redistribution of ILK containing focal adhesions.
PITX2 gain-of-function induced defects in mouse forelimb development
http://www.biomedcentral.com/1471-213X/8/25
Extensive molecular differences between anterior- and posterior-half-sclerotomes underlie somite polarity and spinal nerve segmentation
http://www.biomedcentral.com/1471-213X/9/30
We have identified a set of genes that warrant further investigation as regulators of somite polarity and vertebral morphogenesis, as well as repellents of spinal axon growth. Moreover the results indicate that, unlike the posterior half-sclerotome, the central region of the anterior-half-sclerotome does not contribute bone and cartilage to the vertebral column, being associated instead with the development of the segmented spinal nerves.
- Figure 1. Somite patterning and fate. Somite development involves two patterning systems operating along the A-P and D-V axes. (i) Unsegmented presomite mesoderm and nascent somites showing the oscillations and gradients of gene activity that determine A-P polarity prior to overt somite formation (green: anterior half-somite; red: posterior half-somite). (ii) Transverse section through an A-half-epithelial somite (esm, left) and a differentiated somite (right). Patterning along the D-V axis sub-divides the somite into dermatome (dr), myotome (m) and sclerotome (s). The sclerotome is further sub-divided into ventral (v), central (s, red) and (d) dorsal regions. (iii) Representation of two somites viewed laterally, showing the central sclerotome A-P sub-division. Only the anterior-half (green) is permissive for PNS components. (iv) In differentiated vertebrae, posterior-central sclerotomes form the paired transverse processes and pedicles of the neural arches (red) that encase the spinal cord and provide attachment points for epaxial muscles. Anterior central-sclerotome derivatives (green) contribute to peripheral nerve sheaths and prefigure the positions of the intervertebral foraminae (ivf). Spinous process (sp), intervertebral disc (ivd), vertebral body (vb).
© 2009 Hughes et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Glycogenome expression dynamics during mouse C2C12 myoblast differentiation suggests a sequential reorganization of membrane glycoconjugates
Several global transcriptomic and proteomic approaches have been applied in order to obtain new molecular insights on skeletal myogenesis, but none has generated any specific data on glycogenome expression, and thus on the role of glycan structures in this process, despite the involvement of glycoconjugates in various biological events including differentiation and development. In the present study, a quantitative real-time RT-PCR technology was used to profile the dynamic expression of 375 glycogenes during the differentiation of C2C12 myoblasts into myotubes.
http://www.biomedcentral.com/1471-2164/10/483
Nuclear envelope transmembrane proteins (NETs) that are up-regulated during myogenesis
Conclusion: This work identified 6 NETs that are predicted to have important functions in muscle development and/or maintenance from their expression patterns during myoblast differentiation and in mouse tissues. We confirmed that 5 of these NETs are authentic nuclear envelope proteins. Four members of this group have potential signaling functions at the NE, based on their sequence homologies.
http://www.biomedcentral.com/bmccellbiol/imageofthemonth/archive/2006/11
http://www.biomedcentral.com/content/pdf/1471-2121-7-38.pdf
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