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Cadherin 15

M-cadherin, cadherin-14, CDH15
This gene is a member of the cadherin superfamily of genes, encoding calcium-dependent intercellular adhesion glycoproteins. Cadherins consist of an extracellular domain containing 5 cadherin domains, a transmembrane region, and a conserved cytoplasmic domain. Transcripts from this particular cadherin are expressed in myoblasts and upregulated in myotubule-forming cells. The protein is thought to be essential for the control of morphogenetic processes, specifically myogenesis, and may provide a trigger for terminal muscle cell differentiation. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MyoD, CAN, Myogenin, HAD, Myf5
Papers using M-cadherin antibodies
Salamander limb regeneration involves the activation of a multipotent skeletal muscle satellite cell population
Simon András et al., In The Journal of Cell Biology, 2003
... Hybridoma Bank), mouse monoclonal anti–myosin heavy chain IgG (MF20; Developmental Studies Hybridoma Bank), mouse monoclonal anti–M-cadherin IgG (Clone 1B11 used for immunofluorescence; nanotools GmbH), rabbit polyclonal anti–collagen type IV antibody (Rockland Immunochemicals, Inc.), rabbit polyclonal ...
Expression of a dominant negative cadherin mutant inhibits proliferation and stimulates terminal differentiation of human epidermal keratinocytes
Rudnicki Michael A. et al., In The Journal of Cell Biology, 1995
... ) and anti–M-cadherin antibody sc-6470 (Santa Cruz Biotechnology ...
Papers on M-cadherin
Penetrance of pathogenic mutations in haploinsufficient genes for intellectual disability and related disorders.
Wienker et al., Mainz, Germany. In Eur J Med Genet, Dec 2015
Apparently benign LOF variants were also detected in several other genes for ID and related disorders, including CDH15, KATNAL2, DEPDC5, ARID1B and AUTS2, both in the ExAC database and in the 6,500 exomes of the Exome Variant Server (
Modulation of satellite cells activity and MyoD in rat thyroarytenoid muscle after reinnervation.
Yumoto et al., Kumamoto, Japan. In Laryngoscope, Jul 2015
OBJECTIVES/HYPOTHESIS: To examine modulation of M-cadherin, a marker for satellite cells (SCs); and MyoD, which may indicate the myogenic activity following recurrent laryngeal nerve (RLN) denervation and immediate reinnervation; and to elucidate the correlation between their modulations and establishment of neuromuscular junctions (NMJs) in the reinnervated rat thyroarytenoid (TA) muscle.
E-cadherin cytoplasmic domain inhibits cell surface localization of endogenous cadherins and fusion of C2C12 myoblasts.
Ozawa, Kagoshima, Japan. In Biol Open, 2014
Mouse myoblasts lacking either N-cadherin or M-cadherin can still fuse to form myotubes, indicating that they have no specific function in this process and may be functionally replaced by either M-cadherin or N-cadherin, respectively.
Double homeobox gene, Duxbl, promotes myoblast proliferation and abolishes myoblast differentiation by blocking MyoD transactivation.
Wang et al., Huazhou, China. In Cell Tissue Res, 2014
However, Duxbl overexpression in C2C12 cells inhibited myogenic differentiation by decreasing MyoD downstream gene expressions, including M-cadherin, MyoG, p21 and cyclin D3 but not MyoD itself.
Competence of in vitro cultured mouse embryonic stem cells for myogenic differentiation and fusion with myoblasts.
Moraczewski et al., Warsaw, Poland. In Stem Cells Dev, 2014
We found that ES cells lacked M-cadherin and vascular cell adhesion molecule-1, which may account for the low frequency of hybrid myotube formation in ES cell-myoblast co-cultures and the inability of ES cells alone to form myotubes.
Two desmin gene mutations associated with myofibrillar myopathies in Polish families.
Zekanowski et al., Warsaw, Poland. In Plos One, 2013
Additional staining for M-cadherin, α-actinin, and myosin heavy chains confirmed severe disruption of myofibrill organization.
M-cadherin-mediated intercellular interactions activate satellite cell division.
Izpisua Belmonte et al., Barcelona, Spain. In J Cell Sci, 2013
It has been previously proposed that, under these circumstances, satellite cells first become activated, divide and differentiate, and only later fuse to the existing myofiber through M-cadherin-mediated intercellular interactions.
Regulation of pre-fusion events: recruitment of M-cadherin to microrafts organized at fusion-competent sites of myogenic cells.
Hashimoto et al., Japan. In Bmc Cell Biol, 2012
However, Rac1 activity was unnecessary for recruitment of M-cadherin to lipid rafts.
Adhesion proteins--an impact on skeletal myoblast differentiation.
Brzoska et al., Warsaw, Poland. In Plos One, 2012
To follow the function of these molecules in myoblast differentiation we analysed integrin alpha3, integrin beta1, ADAM12, CD9, CD81, M-cadherin, and VCAM-1 during muscle regeneration.
Isolation, characterization, and molecular regulation of muscle stem cells.
Yamaguchi et al., Ōsaka, Japan. In Front Physiol, 2012
Many studies have demonstrated proteins expressed by satellite cells, including Pax7, M-cadherin, Cxcr4, syndecan3/4, and c-met.
Cadherins and neuropsychiatric disorders.
Hübner et al., Jena, Germany. In Brain Res, 2012
For example, CDH15 and PCDH19 are associated with cognitive impairment; CDH5, CDH8, CDH9, CDH10, CDH13, CDH15, PCDH10, PCDH19 and PCDHb4 with autism; CDH7, CDH12, CDH18, PCDH12 and FAT with bipolar disease and schizophrenia; and CDH11, CDH12 and CDH13 with methamphetamine and alcohol dependency.
Suppression of GSK-3β activation by M-cadherin protects myoblasts against mitochondria-associated apoptosis during myogenic differentiation.
Alway et al., Morgantown, United States. In J Cell Sci, 2011
Inhibition of GSK-3beta activation by M-cadherin protects myoblasts against mitochondria-associated apoptosis during myogenic differentiation.
Toxoplasma gondii down modulates cadherin expression in skeletal muscle cells inhibiting myogenesis.
Barbosa et al., Rio de Janeiro, Brazil. In Bmc Microbiol, 2010
These data suggest that Toxoplasma gondii is able to down regulate M-cadherin expression, leading to molecular modifications in the host cell surface that interfere with membrane fusion and consequently affect the myogenesis process.
Regulation of promyogenic signal transduction by cell-cell contact and adhesion.
Krauss, New York City, United States. In Exp Cell Res, 2010
M-cadherin activates Rac1 to enhance fusion.
Myogenic regulatory factors regulate M-cadherin expression by targeting its proximal promoter elements.
Chen et al., Taiwan. In Biochem J, 2010
Observations identify a molecular mechanism by which MRFs regulate M-cadherin expression directly to ensure the terminal differentiation of myoblasts.
Autocrine and paracrine angiopoietin 1/Tie-2 signaling promotes muscle satellite cell self-renewal.
Chazaud et al., Créteil, France. In Cell Stem Cell, 2009
Ang1/Tie-2 signaling, through ERK1/2 pathway, decreased mpc proliferation and differentiation, increased the number of cells in G0, increased expression of RC-associated markers (p130, Pax7, Myf-5, M-cadherin), and downregulated expression of differentiation-associated markers.
Alterations in CDH15 and KIRREL3 in patients with mild to severe intellectual disability.
Srivastava et al., Greenwood, United States. In Am J Hum Genet, 2008
Alterations in CDH15 in patients with mild to severe intellectual disability are reported.
Cadherin 23 and protocadherin 15 interact to form tip-link filaments in sensory hair cells.
Kachar et al., Los Angeles, United States. In Nature, 2007
Biochemical experiments show that CDH23 homodimers interact in trans with PCDH15 homodimers to form a filament with structural similarity to tip links
Stem and progenitor cells in skeletal muscle development, maintenance, and therapy.
Huard et al., Pittsburgh, United States. In Mol Ther, 2007
In addition to anatomic location, satellite cells are typified by markers such as M-cadherin, Pax7, Myf5, and neural cell adhesion molecule-1.
M-cadherin and its sisters in development of striated muscle.
Starzinski-Powitz et al., Frankfurt am Main, Germany. In Cell Tissue Res, 1999
Cadherins are calcium-dependent, transmembrane intercellular adhesion proteins with morphoregulatory functions in the development and maintenance of tissues.
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