Talk:Musculoskeletal System - Muscle Development

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On this website the Discussion Tab or "talk pages" for a topic has been used for several purposes: References - recent and historic that relates to the topic Additional topic information - currently prepared in draft format Links - to related webpages Topic page - an edit history as used on other Wiki sites Lecture/Practical - student feedback Student Projects - online project discussions. Links: Pubmed Most Recent | Reference Tutorial | Journal Searches Glossary Links Glossary: A | B | C | D | E | F | G | H | I | J | K | L | M | N | O | P | Q | R | S | T | U | V | W | X | Y | Z | Numbers | Symbols | Term Link Cite this page: Hill, M.A. (2026, August 14) Embryology Musculoskeletal System - Muscle Development. Retrieved from https://embryology.med.unsw.edu.au/embryology/index.php/Talk:Musculoskeletal_System_-_Muscle_Development

2010

To build a synapse: signaling pathways in neuromuscular junction assembly

Development. 2010 Apr;137(7):1017-33.

Wu H, Xiong WC, Mei L.

Program of Developmental Neurobiology, Institute of Molecular Medicine and Genetics, Department of Neurology, Medical College of Georgia, Augusta, GA 30912, USA. Abstract Synapses, as fundamental units of the neural circuitry, enable complex behaviors. The neuromuscular junction (NMJ) is a synapse type that forms between motoneurons and skeletal muscle fibers and that exhibits a high degree of subcellular specialization. Aided by genetic techniques and suitable animal models, studies in the past decade have brought significant progress in identifying NMJ components and assembly mechanisms. This review highlights recent advances in the study of NMJ development, focusing on signaling pathways that are activated by diffusible cues, which shed light on synaptogenesis in the brain and contribute to a better understanding of muscular dystrophy.

PMID: 20215342 http://www.ncbi.nlm.nih.gov/pubmed/20215342

http://dev.biologists.org/content/137/7/1017.full

Muscle-derived collagen XIII regulates maturation of the skeletal neuromuscular junction

J Neurosci. 2010 Sep 15;30(37):12230-41.

Latvanlehto A, Fox MA, Sormunen R, Tu H, Oikarainen T, Koski A, Naumenko N, Shakirzyanova A, Kallio M, Ilves M, Giniatullin R, Sanes JR, Pihlajaniemi T.

Oulu Center for Cell-Matrix Research, and Department of Medical Biochemistry and Molecular Biology, 90014 University of Oulu, Finland.

Abstract

Formation, maturation, stabilization, and functional efficacy of the neuromuscular junction (NMJ) are orchestrated by transsynaptic and autocrine signals embedded within the synaptic cleft. Here, we demonstrate that collagen XIII, a nonfibrillar transmembrane collagen, is another such signal. We show that collagen XIII is expressed by muscle and its ectodomain can be proteolytically shed into the extracellular matrix. The collagen XIII protein was found present in the postsynaptic membrane and synaptic basement membrane. To identify a role for collagen XIII at the NMJ, mice were generated lacking this collagen. Morphological and ultrastructural analysis of the NMJ revealed incomplete adhesion of presynaptic and postsynaptic specializations in collagen XIII-deficient mice of both genders. Strikingly, Schwann cells erroneously enwrapped nerve terminals and invaginated into the synaptic cleft, resulting in a decreased contact surface for neurotransmission. Consistent with morphological findings, electrophysiological studies indicated both postsynaptic and presynaptic defects in Col13a1(-/-) mice, such as decreased amplitude of postsynaptic potentials, diminished probabilities of spontaneous release and reduced readily releasable neurotransmitter pool. To identify the role of collagen XIII at the NMJ, shed ectodomain of collagen XIII was applied to cultured myotubes, and it was found to advance acetylcholine receptor (AChR) cluster maturation. Together with the delay in AChR cluster development observed in collagen XIII-deficient mutants in vivo, these results suggest that collagen XIII plays an autocrine role in postsynaptic maturation of the NMJ. Altogether, the results presented here reveal that collagen XIII is a novel muscle-derived cue necessary for the maturation and function of the vertebrate NMJ.

PMID: 2084411 http://www.ncbi.nlm.nih.gov/pubmed/20844119

2009

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

Move this ref to correct page

Fragile X

http://hmg.oxfordjournals.org/content/10/24/2803.full

The RNA-binding Protein Fragile X-related 1 Regulates Somite Formation in Xenopus laevis

http://www.molbiolcell.org/cgi/content/full/16/9/4350

TGF-β

Differentiation plasticity regulated by TGF-β family proteins in development and disease

http://www.nature.com/ncb/journal/v9/n9/full/ncb434.html

PDGF signalling controls the migration of mesoderm cells during chick gastrulation by regulating N-cadherin expression

http://dev.biologists.org/content/135/21/3521.full