ResearchReplicating myoblasts and fused myotubes express the calcium-regulated proteins S100A1 and S100B
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Integrated procedures for accelerating, deepening, and leading genetic inquiry: A first application on human muscle secretome
2023, Molecular Genetics and MetabolismS100B in myoblasts regulates the transition from activation to quiescence and from quiescence to activation and reduces apoptosis
2011, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :We have reported that administration of S100B to myoblasts in differentiation medium (DM) results in inhibition of differentiation, stimulation of proliferation, and protection against apoptosis via inactivation of the promyogenic p38 MAPK and activation of the mitogenic ERK1/2 [21,22]. However, S100B is expressed in myoblast cell lines [23] and in muscle satellite cells in situ [24], raising the possibility that intracellular S100B might have a role in myoblast proliferation/survival and/or differentiation. Indeed, increasing intracellular S100B levels resulted in a dramatically reduced myogenic differentiation via IKKβ/NF-κB-dependent inhibition of the expression of the myogenic transcription factor, MyoD, and its downstream effectors, myogenin and p21WAF1, while inhibition of S100B expression resulted in a significant acceleration of differentiation as a result of reduction of NF-κB activity and consequent upregulation of MyoD [24].
S100B's double life: Intracellular regulator and extracellular signal
2009, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :S100B is a member of a family of Ca2+-binding proteins of the EF-hand type comprising some 25 members (see Refs. [1–5] for reviews). S100B is expressed in varying abundance in a restricted number of cell types such as astrocytes, maturing oligodendrocytes, kidney epithelial cells, neural progenitor cells, pituicytes, ependymocytes, certain neuronal populations, chondrocytes, adipocytes, melanocytes, Langerhans cells, dendritic cells, certain lymphocyte subpopulations, skeletal myofibers, myoblasts [1,3,6–12], and muscle satellite cells.1 Also, S100B expression is enhanced in several tumors arising from cell types normally expressing the protein as well as in the aging brain and in the brain of patients affected by Alzheimer's disease, chronic epilepsy or HIV infection and other brain pathological conditions [1,2,13–15].
S100B increases proliferation in PC12 neuronal cells and reduces their responsiveness to nerve growth factor via Akt activation
2005, Journal of Biological ChemistryCitation Excerpt :As a positive control, S100B– PC12 cells were cultivated in the presence of 500 nm S100B as described previously (18) to document the neurite extension activity of S100B. Immunofluorescence—For indirect immunofluorescence, PC12 cells cultivated as described for the proliferation assay were fixed and processed as described previously (21). S100B and p53 were detected using a monoclonal anti-S100B antibody (1:20; Sigma) and a polyclonal anti-p53 antibody (1:50; Santa Cruz Biotechnology), respectively.
Capping protein: New insights into mechanism and regulation
2004, Trends in Biochemical SciencesCapping protein binding to S100B: Implications for the "tentacle" model for capping the actin filament barbed end
2004, Journal of Biological ChemistryCitation Excerpt :Therefore, it remains possible that some environment in the cell has a similar effect, enabling CP to bind S100B and be inhibited from binding actin. In skeletal muscle, CP(α/β1) (CapZ) is concentrated at the Z-disc, but S100B is not found at the Z-disc (3, 36). High Ca2+ concentrations (∼2 mm) are required for binding of S100B to the αC28 and TRTK-12 peptides, which also suggests that an interaction between S100B and CP is unlikely to occur in cells.