Disease relevance of Cdh15

• Moreover, the three transcripts were transiently upregulated in the distal stump of neurotomized sciatic nerve during Wallerian degeneration: N-cadherin was abundant in myelinating Schwann cells during myelin degradation, while M-cadherin and cadherin-11 may be upregulated in proliferating Schwann cells [1].

High impact information on Cdh15

• The numbers of satellite cells detected in this way are significantly greater than those identified by the other three markers.We conclude that the expression of CD34, Myf5, and M-cadherin defines quiescent, committed precursors and speculate that the CD34(-ve), Myf5(-ve) minority may be involved in maintaining the lineage-committed majority [2].
• Expression of M-cadherin, a member of the cadherin multigene family, correlates with differentiation of skeletal muscle cells [3].
• M-cadherin mRNA is present at low levels in myoblasts and is upregulated in myotube-forming cells [3].
• Here we report the identification and characterization of the cDNA of another member of the cadherin family, M-cadherin (M for muscle), from differentiating muscle cells [3].
• In mouse L cells (fibroblasts), M-cadherin mRNA is undetectable [3].

Biological context of Cdh15

• These observations are in line with the idea that Mcad plays a crucial role in myogenesis [4].
• A putative morphoregulatory molecule involved in myogenesis is M-cadherin (Mcad), a calcium-dependent cell adhesion protein [4].
• Sites of imprinted methylation were also detected at the loci for neuronatin on Chr 2 and for M-cadherin on Chr 8 [5].
• The longest open reading frame of the cDNAs isolated contains almost the entire coding region of the mature M-cadherin as determined by sequence homology to the known cadherins [3].
• 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 [6].

Anatomical context of Cdh15

• At early stages of regeneration, Mcad was exclusively and strongly expressed in myoblasts [4].
• Enhanced staining at sites of contact between satellite cells and the parent muscle fiber suggests an additional, spatially restricted expression of Mcad in muscle fibers [4].
• M-cadherin is a Ca2+-dependent cell adhesion molecule of the cadherin family, initially localized at the areas of contact between myotubes during myogenesis, but also detected in the peripheral nerve and at the adult neuromuscular junction [7].
• M-cadherin, which appears as a molecular marker of glomerulus maturation, might be implicated in the formation, and be the ligand, of adherens junctions encountered in this structure [7].
• M-cadherin expression was first detected at postnatal day (P) 11, after the establishment of the synaptic connections between mossy fibers and granule cell dendrites [7].

Associations of Cdh15 with chemical compounds

• Mcad positive cells in normal and denervated muscles did not incorporate bromodeoxyuridine within 24 hr after injection in vivo, indicating that Mcad is expressed on mitotically quiescent satellite cells [4].
• 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 [6].
• (1) Analysis by laser scan microscopy revealed that the destruction of microtubules by nocodazole leads to an altered cell surface distribution of M-cadherin in differentiating myogenic cells [8].

Physical interactions of Cdh15

• M-cadherin formed complexes with the catenins in skeletal muscle cells similar to E-cadherin in epithelial cells [8].
• We showed that M-cadherin-dependent adhesion activates Rac1 and demonstrated the formation of a multiproteic complex containing M-cadherin, the Rho-GEF Trio, and Rac1 at the onset of myoblast fusion [9].

Co-localisations of Cdh15

• Neural cell adhesion molecule (NCAM) co-localized with Mcad in nearly all satellite cells in denervated muscles but rarely in intact muscles [4].

Regulatory relationships of Cdh15

• Moreover, neither M-cadherin nor E-cadherin could be found in a complex with microtubules in epithelial cells ectopically expressing M-cadherin [8].

Other interactions of Cdh15

• M-cadherin was undetectable in the cerebella of the weaver and staggerer mutants, lacking granule cells, and therefore mature glomeruli and puncta adherentia [7].
• In denervated muscles, alpha- and beta-catenins are upregulated like N- and M-cadherin, while the levels of gamma-catenin/plakoglobin remain unchanged [10].
• Furthermore, other components classically associated with intercellular junctions, i.e., alpha-caterin, beta-catenin and actin filaments, closely paralleled M-cadherin appearance and colocalized with M-cadherin in the mature glomeruli [7].
• M-cadherin is found in embryonic somitic and nonsomitic striated muscles [11].
• M-cadherin is expressed in the myotomes shortly after they form, along with the myogenic regulatory factor myogenin [6].

Analytical, diagnostic and therapeutic context of Cdh15

• The expression of Mcad was studied by immunofluorescence in regenerating, denervated, and normal mouse muscles [4].
• Based on its expression pattern and observations in cell culture, it has been postulated that M-cadherin may be important for the fusion of myoblasts to form myotubes, the correct localization and function of satellite cells during muscle regeneration, and the specialized architecture of adhering junctions in granule cells of cerebellar glomeruli [12].
• 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 [6].
• Using a multiplex single-cell RT-PCR assay we simultaneously monitored expression of all four MyoD family regulators of muscle determination and differentiation (MRFs) together with two candidate markers of satellite cell identity, c-met and m-cadherin [13].
• Serial frozen sections were prepared for immunohistochemistry using specific antibodies to M-cadherin, myoD, Myogenin, myosin heavy chain, and alfa-actin molecule [14].

References