Cited by 114Muscle Physiology and DisordersNutrition and Health in AgingS100 Proteins and Annexins

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Cellular and molecular mechanisms of sarcopenia: the S100B perspective

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Riuzzi, Francesca, Sorci, Guglielmo, Arcuri, Cataldo, Giambanco, Ileana, Bellezza, Ilaria, Minelli, Alba, Donato, Rosario·2018·Journal of Cachexia Sarcopenia and Muscle

DOI 10.1002/jcsm.12363PMC PMC6351675

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Abstract

Abstract Primary sarcopenia is a condition of reduced skeletal muscle mass and strength, reduced agility, and increased fatigability and risk of bone fractures characteristic of aged, otherwise healthy people. The pathogenesis of primary sarcopenia is not completely understood. Herein, we review the essentials of the cellular and molecular mechanisms of skeletal mass maintenance; the alterations of myofiber metabolism and deranged properties of muscle satellite cells (the adult stem cells of skeletal muscles) that underpin the pathophysiology of primary sarcopenia; the role of the Ca 2+ ‐sensor protein, S100B, as an intracellular factor and an extracellular signal regulating cell functions; and the functional role of S100B in muscle tissue. Lastly, building on recent results pointing to S100B as to a molecular determinant of myoblast–brown adipocyte transition, we propose S100B as a transducer of the deleterious effects of accumulation of reactive oxygen species in myoblasts and, potentially, myofibers concurring to the pathophysiology of sarcopenia.

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Figure 1 Schematic representation of cellular and molecular mechanisms driving adult myogenesis. Following acute (reversible) skeletal muscle injury serum factors (i.e. hormones and growth factors) and molecules passively released from damaged muscle tissue (e.g. DAMPs, among which S100B and HMGB1) or secreted by infiltrating proinflammatory (M1) and anti‐inflammatory/reparative (M2) macrophages (e.g. cytokines, S100B, and HMGB1), and components of the extracellular matrix participate in the activation of quiescent muscle SCs and their commitment to myoblasts, proliferation and/or differentiation into fusion‐competent myocytes, which form new myofibers and/or repair the damaged ones. It is not known whether S100B and/or HMGB1 can activate quiescent SCs. A minority of proliferating myoblasts return to a state of quiescence to replenish the SC reserve pool. Fibroblasts concur to the repair process by depositing extracellular matrix, but excess extracellular matrix deposition interferes with the regeneration process. Pericytes and IL‐4‐activated FAPs also participate in the regeneration process. DAMP, damage‐associated molecular pattern; FAPs, fibro/adipogenic precursors; IL‐4, interleukin‐4; SC, satellite cell.CC BY-NC-ND · PubMed Central

Figure 2 Physical exercise and caloric restriction exert trophic/protective effects on skeletal muscles via several mechanisms. A moderate and balanced production of ROS is beneficial to muscle trophism. Green and light blue boxes/pathways refer to anabolic and/or antioxidant mechanisms leading to muscle structure/function preservation, enhanced insulin sensitivity, myofiber remodelling, and redox homeostasis. Pink boxes/pathways refer to catabolic mechanisms required for protein and organelle quality control and, hence, normal muscle trophism. However, hyperfunction of these pathways leads to muscle hypotrophy/atrophy. Released by exercising muscles, myokines (listed in the grey box; ↑ = increased release, ↓ = decreased release) exert either protective (e.g. IL‐1β, IL‐6, IL‐8, and decorin; magenta boxes and symbols) or detrimental (e.g. myostatin; pink boxes and symbols) effects on muscle trophism. ACVRs, activin A receptors; Akt, protein kinase B; AMP, adenosine monophosphate; AMPK, adenosine monophosphate kinase; ATGs, autophagy genes; eNOS, endothelial nitrix oxide synthase; IL‐1β and IL‐6 promote muscle trophism, stimulating glucose uptake and fatty acid (FA) oxidation. FOXO, forkhead box O; IGFR/IR, insulin growth factor receptor/insulin receptor; IL, interleukin; mTOR, mammalian target of rapamycin; NRF2, NF‐E2‐related factor 2; NO, nitrix oxide; NPRL2, Nitrogen permease regulator‐like 2; NT‐3, neutrophin 3; PGC‐1α, peroxisome proliferator‐activated receptor‐γ coactivator‐1α; PI3K, phosphoinositol‐3‐kinase; ROS, reactive oxygen species.CC BY-NC-ND · PubMed Central

Figure 3 Extrinsic and intrinsic, cell‐autonomous factors concurring to determine changes in SCs with aging ultimately leading to reduced SCs' ability to maintain muscle mass (sarcopenia). Redox imbalance, due to either ROS overproduction or consequent to defective ROS removal, is a common trait of factors/lifestyle leading to cell senescence, reduction of SC self‐renewal, and muscle atrophy (refer to text). CDK, cyclin‐dependent kinase; FGF21, fibroblast growth factor 21; FOXO, forkhead box O; JAK/SAT, janus kinase/signal transducer and activator of transcription; MAPK, mitogen activated protein kinase; ROS, reactive oxygen species; SC, satellite cell.CC BY-NC-ND · PubMed Central

Figure 4 Intracellular S100B levels dictate myoblast properties and fate. Oxidative stress leads to abnormally high levels of S100B in myoblasts via stimulation of NF‐κB activity. Accumulation of S100B under chronic oxidative conditions might be consequent to reduced p38 MAPK activity and reduced p38 MAPK‐driven S100B proteasomal degradation. Aged myoblasts show remarkably reduced ability to secrete S100B. Whether disulfide‐linked formation of S100B oligomers under oxidative conditions interferes with S100B release remains to be investigated (?). In turn, S100B activates NF‐κB with resultant up‐regulation of YY1 and down‐regulation of MyoD, and blockade of myogenic differentiation. S100B‐mediated NF‐κB activation also results in enhanced propensity of myoblasts to proliferate and to resist to apoptotic stimuli leading to reduced myogenic differentiation and reduced acquisition of quiescence. Although intracellular accumulation of S100B leads to defective p53 activity and uncontrolled proliferation in certain cell types (refer to text), no information is available regarding S100B's regulatory effects on p53 or p53‐induced cell senescence in myoblasts (?). Lastly, oxidative stress‐induced accumulation of S100B converts myoblasts into brown adipocytes via an NF‐κB/YY1/miR‐133 axis and NF‐κB/YY1/BMP7 axis. BMP7, bone morphogenetic protein 7; BMPR, bone morphogenetic factor receptor; ROS, reactive oxygen species; UCP‐1, uncoupling protein 1; YY1, Yin Yang 1.CC BY-NC-ND · PubMed Central

Figure 5 S100B is found to be associated with mitochondria in myoblasts. Proliferating L6 myoblasts91 show co‐localization of S100B (red signal) with the mitochondrial marker, cytochrome c (cytC; green signal). Shown is a merged image. Bar = 100 μm.CC BY-NC-ND · PubMed Central

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Ethical guidelines for publishing in the journal of cachexia, sarcopenia and muscle: update 2017
von Haehling, S., Morley, J. E., Coats, A. J. S., & Anker, S. D. (2017) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12261 · Cited by 351 · cited 1×
“guidelines for publishing in the Journal of Cachexia, Sarcopenia and Muscle: update 2017.(152)”
S100B expression defines a state in which GFAP‐expressing cells lose their neural stem cell potential and acquire a more mature developmental stage
Raponi, É., Agenès, F., Delphin, C., Assard, N., Baudier, J., Legraverend, C., & Deloulme, J. (2006) · Glia · doi:10.1002/glia.20445 · Cited by 347
Loss of fibronectin from the aged stem cell niche affects the regenerative capacity of skeletal muscle in mice
Lukjanenko, L., Jung, M. J., Hegde, N., Perruisseau-Carrier, C., Migliavacca, E., Rozo, M., Karaz, S., Jacot, G. E., Schmidt, M., Li, L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4126 · Cited by 347
Signalling pathways regulating muscle mass in ageing skeletal muscle. The role of the IGF1-Akt-mTOR-FoxO pathway
Sandri, M., Barberi, L., Bijlsma, A. Y., Blaauw, B., Dyar, K. A., Milan, G., Mammucari, C., Meskers, C. G. M., Pallafacchina, G., Paoli, A., et al. (2013) · Biogerontology · doi:10.1007/s10522-013-9432-9 · Cited by 340 · cited 1×
“tivation of the ubiquitin ligase atrogin-1 were found to paradoxically cause muscle pathology.(25) Yet a ROS–FoxO cross-talk”
Background
Muscle as a paracrine and endocrine organ
Giudice, J., & Taylor, J. M. (2017) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2017.05.005 · Cited by 331 · cited 1×
“contributing to the broad beneficial effects of exercise on cardiovascular, metabolic, and mental health.(62) Among the vari-”
Macrophages: Supportive cells for tissue repair and regeneration
Chazaud, B. (2013) · Immunobiology · doi:10.1016/j.imbio.2013.09.001 · Cited by 326
Nrf2 mediates redox adaptations to exercise
Done, A. J., & Traustadóttir, T. (2016) · Redox Biology · doi:10.1016/j.redox.2016.10.003 · Cited by 308 · cited 1×
“43 ), an event counteracted by a regular exercise that attenuates the age-related changes in Nrf2-mediated pathways and potentially restores the redox homeostasis 28,44 – 46 ( Figure 2).”
Sustained Activation of mTORC1 in Skeletal Muscle Inhibits Constitutive and Starvation-Induced Autophagy and Causes a Severe, Late-Onset Myopathy
Castets, P., Lin, S., Rion, N., Di Fulvio, S., Romanino, K., Guridi, M., Frank, S., Tintignac, L. A., Sinnreich, M., & Rüegg, M. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.015 · Cited by 302
Epidemiology of sarcopenia and insight into possible therapeutic targets
Dennison, E. M., Sayer, A. A., & Cooper, C. C. (2017) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2017.60 · Cited by 302 · cited 1×
“…muscle strength and agility and increased fatiga-bility inherent to sarcopenic subjects, coupled to a relatively excessive caloric intake, is likely to be one main cause especially if associated with cigarette smoking, alcohol consumption, and low protein and vegetable intake 76 ( Figure 3).”
MicroRNA-133 Controls Brown Adipose Determination in Skeletal Muscle Satellite Cells by Targeting Prdm16
Yin, H., Pasut, A., Soleimani, V. D., Bentzinger, C. F., Antoun, G., Thorn, S., Seale, P., Fernando, P., van IJcken, W., Grosveld, F., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.01.004 · Cited by 293
Characterization of the tumor suppressor protein p53 as a protein kinase C substrate and a S100b-binding protein.
Baudier, J., Delphin, C., Grünwald, D., Khochbin, S., & Lawrence, J. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.23.11627 · Cited by 285
Lifelong physical exercise delays age-associated skeletal muscle decline
Zampieri, S., Pietrangelo, L., Loefler, S., Fruhmann, H., Vogelauer, M., Burggraf, S., Pond, A., Grim-Stieger, M., Cvecka, J., Sedliak, M., et al. (2015) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glu006 · Cited by 282
Muscle stem cells contribute to myofibres in sedentary adult mice
Keefe, A. C., Lawson, J. A., Flygare, S. D., Fox, Z. D., Colasanto, M. P., Mathew, S. J., Yandell, M., & Kardon, G. (2015) · Nature Communications · doi:10.1038/ncomms8087 · Cited by 279 · cited 3×
“might not concur to sarcopenia while leading to defective regeneration following acute muscle injury and contributing to age-related muscle fibrosis.(84,85) This would imply that pri-”
Stem Cell Review Series: Aging of the skeletal muscle stem cell niche
Gopinath, S. D., & Rando, T. A. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00399.x · Cited by 265 · cited 1×
“of senescent cells being proliferation and differentiation defective.(69,135,136) It is presently unknown whether the elevated levels of S100B found in senescent myoblasts(135) are a consequence or a cause of senescence.”
MyomiR-133 regulates brown fat differentiation through Prdm16
Trajkovski, M., Ahmed, K., Esau, C., & Stoffel, M. (2012) · Nature Cell Biology · doi:10.1038/ncb2612 · Cited by 263 · cited 1×
“In turn, S100B stimulates NF-κ B activity with resultant up-regulation of YY1 and YY1-dependent inhibition of miR-133, a promyogenic and anti-adipogenic microRNA, 142 – 144 ultimately leading to transition of myoblasts to brown adipocytes 137 ( Figure 4).”
Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells in vivo
Francoz, S., Froment, P., Bogaerts, S., De Clercq, S., Maetens, M., Doumont, G., Bellefroid, E., & Marine, J.-C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508476103 · Cited by 260 · cited 1×
“This potential S100B activity, however, might be mitigated or even abolished by the reported ability of S100B to block the ubiquitin E3 ligases, MDM2 and MDM4,(133) that drive proteasomal degradation of p53.(134) Thus, appropriate levels of S100B in myoblasts appear to be required for myoblasts”
Targeting β1-integrin signaling enhances regeneration in aged and dystrophic muscle in mice
Rozo, M., Li, L., & Fan, C. (2016) · Nature Medicine · doi:10.1038/nm.4116 · Cited by 260
NF-κB Regulation of YY1 Inhibits Skeletal Myogenesis through Transcriptional Silencing of Myofibrillar Genes
Wang, H., Hertlein, E. K., Bakkar, N., Sun, H., Acharyya, S., Wang, J., Carathers, M., Davuluri, R. V., & D, D. C. G. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02020-06 · Cited by 259 · cited 1×
“MyoD and the MyoD-downstream effectors, myogenin and p21, and to up-regulate Yin Yang 1 (YY1)(93) (Figure 4), a transcriptional repressor induced by NF-κB with antimyogenic activity.(119) Interestingly, myoblasts down-regulate”
Independent regulation of JNK/p38 mitogen-activated protein kinases by metabolic oxidative stress in the liver
Mendelson, K. G., Contois, L. W., Tevosian, S. G., Davis, R. J., & Paulson, K. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.12908 · Cited by 232 · cited 2×
“phosphatase MKP-1, which inactivates the promyogenic p38 MAPK.(141) Indeed, ROS overproduction in myoblasts causes accumulation of S100B partly owing to MKP-1-dependent inactivation of p38 MAPK and stimulates NF-κB activity, which cause up-regulation of S100B(137) (Figure 4).”
Quantification of GDF11 and Myostatin in Human Aging and Cardiovascular Disease
Schafer, M. J., Atkinson, E. J., Vanderboom, P. M., Kotajarvi, B. R., White, T. A., Moore, M. M., Bruce, C. J., Greason, K. L., Suri, R. M., Khosla, S., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.023 · Cited by 211 · cited 1×
“Instead, GDF11 is risk factor for age-related frailty and disease in humans.(83)”
Sarcopenia
Fuggle, N. R., Shaw, S., Dennison, E. M., & Cooper, C. C. (2017) · Best Practice & Research Clinical Rheumatology · doi:10.1016/j.berh.2017.11.007 · Cited by 199
Modulation of reactive oxygen species in skeletal muscle by myostatin is mediated through NF-κB
Sriram, S., Subramanian, S., Sathiakumar, D., Venkatesh, R., Salerno, M. S., McFarlane, C. D., Kambadur, R., & Sharma, M. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00734.x · Cited by 189 · cited 1×
“proteasomal-mediated catabolism of intracellular proteins.(77)”
S100B Protein Regulates Astrocyte Shape and Migration via Interaction with Src Kinase
Brozzi, F., Arcuri, C., Giambanco, I., & Donato, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m805897200 · Cited by 174 · cited 1×
“120 126 Yet differentiated myoblasts (myocytes) resume expressing S100B under the action of myogenin, 120 and S100B is found expressed in mature myo ﬁ bers as mentioned earlier.”
Proteins of the S100 family regulate the oligomerization of p53 tumor suppressor
Fernández-Fernández, M. R., Veprintsev, D. B., & Fersht, A. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501459102 · Cited by 172
Cellular adaptation to xenobiotics: Interplay between xenosensors, reactive oxygen species and FOXO transcription factors
Klotz, L., & Steinbrenner, H. (2017) · Redox Biology · doi:10.1016/j.redox.2017.07.015 · Cited by 165 · cited 1×
“ROS overproduction, owing to altered mitochondrial function and/or defective ROS management, might be one cause of sarcopenia.(41,57,74,75) ROS imbalance might determine the ab-”
Differential response of skeletal muscles to mTORC1 signaling during atrophy and hypertrophy
Bentzinger, C. F., Lin, S., Romanino, K., Castets, P., Guridi, M., Summermatter, S., Handschin, C., Tintignac, L. A., Hall, M. N., & Rüegg, M. A. (2013) · Skeletal Muscle · doi:10.1186/2044-5040-3-6 · Cited by 153
Inhibition of p53 Transcriptional Activity by the S100B Calcium-binding Protein
Lin, J., Blake, M., Tang, C., Zimmer, D. B., Rustandi, R. R., Weber, D. J., & Carrier, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104379200 · Cited by 141
Starring or supporting role? Satellite cells and skeletal muscle fiber size regulation
Murach, K. A., Fry, C. S., Kirby, T. J., Jackson, J. R., Lee, J. D., White, S. H., Dupont-Versteegden, E. E., McCarthy, J. J., & Peterson, C. A. (2018) · Physiology · doi:10.1152/physiol.00019.2017 · Cited by 137
Current understanding of sarcopenia: possible candidates modulating muscle mass
Sakuma, K., Aoi, W., & Yamaguchi, A. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1527-x · Cited by 133 · cited 1×
“Sarcopenia may be either secondary to chronic inflammatory statuses, diabetes, hormonal alterations, vascular disturbances, renal, respiratory and/or cardiac failure, and immobilization(3) or primary, occurring in otherwise healthy, usually aged persons.(1,2) The pathogenesis of primary”
Stem cells in the hood: the skeletal muscle niche
Pannérec, A., Marazzi, G., & Sassoon, D. A. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.07.004 · Cited by 130 · cited 1×
“In ﬁ ltrating immune cells, among which macrophages play an essential role, 9 – 12 vascular pericytes 13,14 and ﬁ bro/adipogenic precursors (FAPs) 15,16 participate in muscle regeneration ( Figure 1).”
Inhibiting S100B Restores p53 Levels in Primary Malignant Melanoma Cancer Cells
Lin, J., Yang, Q., Yan, Z., Markowitz, J., Wilder, P. T., Carrier, F., & Weber, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405419200 · Cited by 128
HDAC1 activates FoxO and is both sufficient and required for skeletal muscle atrophy
Beharry, A. W., Sandesara, P. B., Roberts, B. M., Ferreira, L. F., Senf, S. M., & Judge, A. R. (2014) · Journal of Cell Science · doi:10.1242/jcs.136390 · Cited by 128
The many roles of PGC-1α in muscle — recent developments
Chan, M. C., & Arany, Z. P. (2014) · Metabolism · doi:10.1016/j.metabol.2014.01.006 · Cited by 127 · cited 1×
“health and disease regulating endurance, fibre-type switching, and insulin sensitivity.(29) PGC1α is induced by oxida-”
Amphoterin Stimulates Myogenesis and Counteracts the Antimyogenic Factors Basic Fibroblast Growth Factor and S100B via RAGE Binding
Sorci, G., Riuzzi, F., Arcuri, C., Giambanco, I., & Donato, R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.11.4880-4894.2004 · Cited by 125
Modulation of the Oligomerization State of p53 by Differential Binding of Proteins of the S100 Family to p53 Monomers and Tetramers
van Dieck, J., Fernández-Fernández, M. R., Veprintsev, D. B., & Fersht, A. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901351200 · Cited by 118
S100B Interaction With the Receptor for Advanced Glycation End Products (RAGE): A Novel Receptor-Mediated Mechanism for Myocyte Apoptosis Postinfarction
Tsoporis, J. N., Izhar, S., Leong-Poi, H., Desjardins, J.-F., Huttunen, H. J., & Parker, T. G. (2010) · Circulation Research · doi:10.1161/circresaha.109.195834 · Cited by 118 · cited 2×
“22 Also, S100B is passively released from injured brain 88,89 and heart 103 and from acutely and chronically injured muscle tissue, 104 behaving like a DAMP.”
The Calcium-binding Protein S100B Down-regulates p53 and Apoptosis in Malignant Melanoma
Lin, J., Yang, Q., Wilder, P. T., Carrier, F., & Weber, D. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.155382 · Cited by 117 · cited 1×
“…to stem cell exhaustion 79 and since S100B inhibits p53 phosphorylation and tetramerization, i.e. its activation, 127 – 130 and reduces p53 levels, 131,132 it is tempting to speculate that high S100B levels might interfere with myo-blast senescence by decreasing p53/p21 CIP1 activity ( Figure 4).”
Lifelong training preserves some redox-regulated adaptive responses after an acute exercise stimulus in aged human skeletal muscle
Cobley, J. N., Sakellariou, G. K., Owens, D. J., Murray, S. W., Waldron, S., Gregson, W. A., Fraser, W. D., Burniston, J. G., Iwanejko, L., McArdle, A., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.004 · Cited by 108
S100A1 and S100B, transcriptional targets of SOX trio, inhibit terminal differentiation of chondrocytes
Saito, T., Ikeda, T., Nakamura, K., Chung, U., & Kawaguchi, H. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400934 · Cited by 105
S100 Calcium Binding Proteins and Ion Channels
Hermann, A., Donato, R., Weiger, T. M., & Chazin, W. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00067 · Cited by 104
A Novel YY1-miR-1 Regulatory Circuit in Skeletal Myogenesis Revealed by Genome-Wide Prediction of YY1-miRNA Network
Lu, L., Zhou, L., Chen, E. Z., Sun, K., Jiang, P., Wang, L., Su, X., Sun, H., & Wang, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0027596 · Cited by 103
The Danger Signal S100B Integrates Pathogen– and Danger–Sensing Pathways to Restrain Inflammation
Sorci, G., Giovannini, G., Riuzzi, F., Bonifazi, P., Zelante, T., Zagarella, S., Bistoni, F., Donato, R., & Romani, L. R. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001315 · Cited by 100
Activation of mTORC1 in skeletal muscle regulates whole-body metabolism through FGF21
Guridi, M., Tintignac, L. A. J., Lin, S., Kupr, B., Castets, P., & Rüegg, M. A. (2015) · Science Signaling · doi:10.1126/scisignal.aab3715 · Cited by 98
FoxO3 inactivation promotes human cholangiocarcinoma tumorigenesis and chemoresistance through Keap1‐Nrf2 signaling
Guan, L., Zhang, L., Gong, Z., Hou, X., Xu, Y., Feng, X., Wang, H., & You, H. (2016) · Hepatology · doi:10.1002/hep.28496 · Cited by 95 · cited 1×
“25 Yet a ROS – FoxO cross-talk occurs in cells whereby ROS and FoxO reciprocally regulate their levels, 40,41 and old sedentary rat muscles show elevated levels of the atrophy genes (atrogenes), atrogin-1 and MuRF-1.”
Physical exercise in aging human skeletal muscle increases mitochondrial calcium uniporter expression levels and affects mitochondria dynamics
Zampieri, S., Mammucari, C., Romanello, V., Barberi, L., Pietrangelo, L., Fusella, A., Mosole, S., Gherardi, G., Höfer, C., Löfler, S., et al. (2016) · Physiological Reports · doi:10.14814/phy2.13005 · Cited by 92 · cited 1×
“DAMP, damage-associated molecular pattern; FAPs, ﬁ bro/ adipogenic precursors; IL-4, interleukin-4; SC, satellite cell. muscles 27 likely mediated by preserved expression levels of mitochondrial fusion protein 28 optic atrophy 1 ( Figure 2).”
HMGB1/RAGE regulates muscle satellite cell homeostasis via p38 MAPK/myogenin-dependent repression of Pax7 transcription
Riuzzi, F., Sorci, G., Sagheddu, R., & Donato, R. (2012) · Journal of Cell Science · doi:10.1242/jcs.092163 · Cited by 91 · cited 1×
“damage sites, and prolongs the M1 macrophage inflammatory phase.(20) Yet as observed with cultured astrocytes and neurons,(88,89) at high local concentrations, S100B directly causes myoblast apoptosis(116) and RAGE dependently perpet-”
HuR and miR-1192 regulate myogenesis by modulating the translation of HMGB1 mRNA
Dormoy-Raclet, V., Cammas, A., Celona, B., Lian, X. J., van der Giessen, K., Zivojnovic, M., Brunelli, S., Riuzzi, F., Sorci, G., Wilhelm, B. T., et al. (2013) · Nature Communications · doi:10.1038/ncomms3388 · Cited by 89
A Systematic Review of the Biomarker S100B: Implications for Sport-Related Concussion Management
Schulte, S., Podlog, L. W., Hamson-Utley, J. J., Strathmann, F. G., & Strüder, H. K. (2014) · Journal of Athletic Training · doi:10.4085/1062-6050-49.3.33 · Cited by 88 · cited 1×
“marathon, swimming races, and soccer games).(106) These elevated serum S100B levels have been suggested to result from brain concussion known to”
Gα i2 Signaling Promotes Skeletal Muscle Hypertrophy, Myoblast Differentiation, and Muscle Regeneration
Minetti, G., Feige, J. N., Rosenstiel, A., Bombard, F., Meier, V., Werner, A., Bassilana, F., Sailer, A. W., Kahle, P., Lambert, C., et al. (2011) · Science Signaling · doi:10.1126/scisignal.2002038 · Cited by 87
S100B Expression Modulates Left Ventricular Remodeling After Myocardial Infarction in Mice
Tsoporis, J. N., Marks, A., Haddad, A., Dawood, F., Liu, P. P., & Parker, T. G. (2005) · Circulation · doi:10.1161/01.cir.0000154554.65287.f5 · Cited by 82 · cited 1×
“the peri-infarct heart tissue) and inhibits cardiomyocyte hypertrophic response.(95) Also, bronchial epithe-”
S100B Inhibits Myogenic Differentiation and Myotube Formation in a RAGE-Independent Manner
Sorci, G., Riuzzi, F., Agneletti, A. L., Marchetti, C., & Donato, R. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.14.4870-4881.2003 · Cited by 78 · cited 1×
“ture conditions, S100B inhibits myoblast differentiation and myotube formation and stimulates myoblast proliferation via bFGF/FGFR1 activation.(111,113,114) On the other hand, in”
S100B Increases Proliferation in PC12 Neuronal Cells and Reduces Their Responsiveness to Nerve Growth Factor via Akt Activation
Arcuri, C., Bianchi, R., Brozzi, F., & Donato, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406440200 · Cited by 76
Interaction of Developmental Transcription Factor HOXC11 with Steroid Receptor Coactivator SRC-1 Mediates Resistance to Endocrine Therapy in Breast Cancer
McIlroy, M., McCartan, D. P., Early, S. A., Gaora, P. Ó., Pennington, S. R., Hill, A. D. K., & Young, L. S. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3713 · Cited by 73
S100B causes apoptosis in a myoblast cell line in a RAGE‐independent manner
Sorci, G., Riuzzi, F., Agneletti, A. L., Marchetti, C., & Donato, R. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10462 · Cited by 71 · cited 2×
“nase (GAPDH) activity by enhanced poly(ADP-ribosyl)ation of GAPDH with no apparent role for RAGE or FGFR.(116) Notably, muscles of S100B KO mice show reduced levels of poly(ADP-ribosyl)ated GAPDH,(118) but there is no information”
BackgroundInfluential
Lack of evidence for GDF 11 as a rejuvenator of aged skeletal muscle satellite cells
Hinken, A. C., Powers, J. M., Luo, G., Holt, J. A., Billin, A. N., & Russell, A. J. (2016) · Aging Cell · doi:10.1111/acel.12475 · Cited by 71 · cited 4×
“The initial enthusiasm about the ﬁ nding that growth differentiation factor 11 (GDF11), a myostatin homologue, might support muscle trophism and regeneration and contrast muscle aging 80 was dampened by reports showing that, on the contrary, GDF11 levels increases with age and inhibits muscle regeneration, behaving li…”
Influential
Histone deacetylase inhibition suppresses myogenin-dependent atrogene activation in spinal muscular atrophy mice
Bricceno, K. V., Sampognaro, P. J., Meerbeke, J. P. V., Sumner, C. J., Fischbeck, K. H., & Burnett, B. G. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds286 · Cited by 70
S100B protein regulates myoblast proliferation and differentiation by activating FGFR1 in a bFGF-dependent manner
Riuzzi, F., Sorci, G., & Donato, R. (2011) · Journal of Cell Science · doi:10.1242/jcs.084491 · Cited by 70 · cited 2×
“factor (bFGF)/FGF receptor 1 (FGFR1) complex depending on its own local concentration, myoblast density, and bFGF availability.(22,104,111,112) In standard (high-density) myoblast cul-”
Nuclear factor (erythroid derived 2)-like 2 activation increases exercise endurance capacity via redox modulation in skeletal muscles
Oh, S., Komine, S., Warabi, E., Akiyama, K., Ishii, A., Ishige, K., Mizokami, Y., Kuga, K., Horie, M., Miwa, Y., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-12926-y · Cited by 70 · cited 1×
“and downstream genes and attenuates muscle fatigue via reduction of oxidative stress caused by exhaustive exercise.(47)”
Alterations in the in vitro and in vivo regulation of muscle regeneration in healthy ageing and the influence of sarcopenia
Brzeszczyńska, J., Meyer, A. S., McGregor, R. A., Schilb, A., Degen, S., Tadini, V., Johns, N., LANGEN, R. C. J., Schols, A. M. W. J., Glass, D. J., et al. (2017) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12252 · Cited by 69 · cited 2×
“HSPA1A, a stress-induced chaperone acting upon misfolded proteins.(57) These results suggest that reduced cellular de-”
PRDM16: the interconvertible adipo-myocyte switch
Frühbeck, G., Sesma, P., & Burrell, M. A. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.01.007 · Cited by 67 · cited 1×
“139 Besides inhibiting myoblast differentiation and participating in the process of myoblast aging, elevated S100B levels also promote myoblast – brown adipocyte transition, and myoblasts from sarcopenic subjects show properties of brown (pre)adipocytes.”
Human muscle satellite cells show age-related differential expression of S100B protein and RAGE
Beccafico, S., Riuzzi, F., Puglielli, C., Mancinelli, R., Fulle, S., Sorci, G., & Donato, R. (2010) · AGE · doi:10.1007/s11357-010-9197-x · Cited by 66
Role of reactive oxygen species in the defective regeneration seen in aging muscle
Vasilaki, A., & Jackson, M. J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.008 · Cited by 65 · cited 1×
“ROS overproduction, owing to altered mitochondrial function and/or defective ROS management, might be one cause of sarcopenia.(41,57,74,75) ROS imbalance might determine the ab-”
Annexin V, annexin VI, S100A1 and S100B in developing and adult avian skeletal muscles
Arcuri, C., Giambanco, I., Bianchi, R., & Donato, R. (2002) · Neuroscience · doi:10.1016/s0306-4522(01)00330-x · Cited by 64
Serum S100B Protein Is Increased in Fasting Rats
Netto, C. B. O., Conte, S., Leite, M. C., Pires, C., Martins, T. L., Vidal, P. R., Benfato, M. S., Giugliani, R., & Gonçalves, C. (2006) · Archives of Medical Research · doi:10.1016/j.arcmed.2005.11.005 · Cited by 64 · cited 1×
“98 101 Indeed, S100B is secreted constitutively by astrocytes 88 and following stimulation with catecholamines by white adipocytes, 102 and by activated macrophages.”
The Role of Reactive Oxygen Species in Adipogenic Differentiation
de Villiers, D., Potgieter, M., Ambele, M. A., Adam, L. T., Durandt, C., & Pepper, M. S. (2017) · Advances in experimental medicine and biology · doi:10.1007/5584_2017_119 · Cited by 62 · cited 1×
“tioxidants or ROS scavengers suppress ROS effects on adipogenesis.(140) Chronically high ROS levels induce the”
S100B Engages RAGE or bFGF/FGFR1 in Myoblasts Depending on Its Own Concentration and Myoblast Density. Implications for Muscle Regeneration
Riuzzi, F., Sorci, G., Beccafico, S., & Donato, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0028700 · Cited by 60 · cited 2×
“promoting the transition of infiltrating macrophages from M1 (proinflammatory) to M2 (anti-inflammatory and reparative) phenotype.(22,104) Incidentally, promyogenic effects of”
S100A1: A Regulator of Striated Muscle Sarcoplasmic Reticulum Ca 2+ Handling, Sarcomeric, and Mitochondrial Function
Völkers, M., Rohde, D., Goodman, C. R., & Most, P. (2010) · BioMed Research International · doi:10.1155/2010/178614 · Cited by 58 · cited 3×
“Given the S100B’s localization to the sarcoplasmic reticulum and transverse tubules similar to S100A1,92,93 a member of the S100 family of Ca2+-binding proteins that is 56% identical to S100B,89 one may hypothesize that S100B might regulate ryanodine receptor 1 and/or sarco(endo)plasmic reticulum calcium-ATPase activi…”
Background
Oxidative stress-induced S100B accumulation converts myoblasts into brown adipocytes via an NF-κB/YY1/miR-133 axis and NF-κB/YY1/BMP-7 axis
Morozzi, G., Beccafico, S., Bianchi, R., Riuzzi, F., Bellezza, I., Giambanco, I., Arcuri, C., Minelli, A., & Donato, R. (2017) · Cell Death & Differentiation · doi:10.1038/cdd.2017.132 · Cited by 58
S100B protein in myoblasts modulates myogenic differentiation via NF‐κB‐dependent inhibition of MyoD expression
Tubaro, C., Arcuri, C., Giambanco, I., & Donato, R. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22035 · Cited by 57
Role of muscle stem cells in sarcopenia
Snijders, T., & Parise, G. (2017) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000360 · Cited by 56
S100B-RAGE dependent VEGF secretion by cardiac myocytes induces myofibroblast proliferation
Tsoporis, J. N., Izhar, S., Proteau, G. A., Slaughter, G., & Parker, T. G. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.08.015 · Cited by 53 · cited 1×
“secretion and VEGF-dependent myofibroblast proliferation potentially contributing to scar formation.(105) In acute muscle injury, a transient release of S100B(104) is required for a rapid”
Loss of a Negative Regulator of mTORC1 Induces Aerobic Glycolysis and Altered Fiber Composition in Skeletal Muscle
Dutchak, P. A., Estill-Terpack, S. J., Plec, A. A., Zhao, X., Yang, C., Chen, J., Ko, B., Deberardinis, R. J., Yu, Y., & Tu, B. P. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.058 · Cited by 53
The Calcium-Dependent Interaction between S100B and the Mitochondrial AAA ATPase ATAD3A and the Role of This Complex in the Cytoplasmic Processing of ATAD3A
Gilquin, B., Cannon, B. R., Hubstenberger, A., Moulouel, B., Falk, E., Merle, N., Assard, N., Kieffer‐Jaquinod, S., Rousseau, D. L., Wilder, P. T., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01468-09 · Cited by 52 · cited 1×
“143 While a physical and functional association of S100B with mitochondria was excluded in a previous study, 151 we found that a fraction of S100B co-localizes with the mitochondrial marker, cytochrome c , in proliferating myoblasts 113 ( Figure 5).”
Is Peripheral Immunity Regulated by Blood-Brain Barrier Permeability Changes?
Bargerstock, E., Puvenna, V., Iffland, P. H., Falcone, T., Hossain, M. S., Vetter, S., Man, S., Dickstein, L. P., Marchi, N., Ghosh, C., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101477 · Cited by 51
Effects of calcium‐binding proteins (S‐100a o , S‐100a, S‐100b) on desmin assembly in vitro
Garbuglia, M., Verzini, M., Giambanco, I., Spreca, A., & Donato, R. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.2.8641565 · Cited by 48 · cited 1×
“found to be associated with Type III intermediate filaments in myoblasts and myotubes in part(91) and to exert an inhibitory effect on desmin assembly in vitro.(94) Functional corre-”
Background
Levels of S100B protein drive the reparative process in acute muscle injury and muscular dystrophy
Riuzzi, F., Beccafico, S., Sagheddu, R., Chiappalupi, S., Giambanco, I., Bereshchenko, O., Riccardi, C., Sorci, G., & Donato, R. (2017) · Scientific Reports · doi:10.1038/s41598-017-12880-9 · Cited by 45 · cited 6×
“uates muscle damage by fuelling inflammation as observed during the acute phase of muscular dystrophy.(22) In this latter”
Influential
Expression of S100B during embryonic development of the mouse cerebellum
Hachem, S., Laurenson, A.-S., Hugnot, J., & Legraverend, C. (2007) · BMC Developmental Biology · doi:10.1186/1471-213x-7-17 · Cited by 44
Zinc Binding to S100B Affords Regulation of Trace Metal Homeostasis and Excitotoxicity in the Brain
Hagmeyer, S., Cristóvão, J. S., Mulvihill, J. J., Boeckers, T. M., Gomes, C. M., & Grabrucker, A. M. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00456 · Cited by 44 · cited 1×
“98 101 Indeed, S100B is secreted constitutively by astrocytes 88 and following stimulation with catecholamines by white adipocytes, 102 and by activated macrophages.”
Transcription Factor Tfe3 Directly Regulates Pgc‐1alpha in Muscle
Salma, N., Song, J. S., Arany, Z. P., & Fisher, D. E. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.24978 · Cited by 42 · cited 1×
“…induced by oxidative stress, is a powerful regulator of reactive oxygen species (ROS) removal by increasing the expression of numerous ROS-detoxifying enzymes and factors such as NF-E2-related factor 2 (Nrf2), 30 and is directly regulated by the transcription factor Tfe3 in muscles 31 ( Figure 2).”
Resistance training regulates gene expression of molecules associated with intramyocellular lipids, glucose signaling and fiber size in old rats
Ribeiro, M. B. T., Guzzoni, V., Hord, J. M., Lopes, G. N., Marqueti, R. D. C., de Andrade, R. V., Selistre-de-Araújo, H. S., & Durigan, J. L. Q. (2017) · Scientific Reports · doi:10.1038/s41598-017-09343-6 · Cited by 42
AAV1.NT-3 gene therapy increases muscle fiber diameter through activation of mTOR pathway and metabolic remodeling in a CMT mouse model
YALVAÇ, M. E., Amornvit, J., Chen, L., Shontz, K. M., Lewis, S., & Sahenk, Z. (2018) · Gene Therapy · doi:10.1038/s41434-018-0009-8 · Cited by 41
Serum S100B level increases after running but not cycling exercise
Stocchero, C. M. A., Oses, J. P., Cunha, G. D. S., Martins, J. B., Brum, L. M. B. D. P., Zimmer, E. R., Souza, D. O., Portela, L. V., & Reischak-Oliveira, Á. (2013) · Applied Physiology Nutrition and Metabolism · doi:10.1139/apnm-2013-0308 · Cited by 38 · cited 1×
“106 108 Extracellular effects of S100B are largely brought about by its interaction with RAGE (receptor for advanced glycation end products, encoded by AGER/ Ager ) 109,110 ; however, at least in the case of muscle injury, S100B can activate either RAGE or the basic ﬁ broblast growth factor…”
S100 proteins interact with the N‐terminal domain of MDM2
van Dieck, J., Lum, J. K., Teufel, D. P., & Fersht, A. R. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.06.024 · Cited by 38
S100 calcium binding protein affects neuronal electrical discharge activity by modulation of potassium currents
Kubista, H., Donato, R., & Hermann, A. (1999) · Neuroscience · doi:10.1016/s0306-4522(98)00422-9 · Cited by 35
Muscle PGC-1α modulates satellite cell number and proliferation by remodeling the stem cell niche
Dinulović, I., Furrer, R., Beer, M., Ferry, A., Cardel, B., & Handschin, C. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0111-9 · Cited by 35 · cited 1×
“tial for mitochondriogenesis promoting oxidative fibre formation at the expense of glycolytic fibre formation,(32) improving exercise performance,(33) increasing muscle mass and strength and resistance to muscle wasting,(34) and augmenting early steps in the activation and proliferation of adult muscle stem cells.(35)…”
HOXC6 and HOXC11 increase transcription of S100β gene in BrdU‐induced in vitro differentiation of GOTO neuroblastoma cells into Schwannian cells
Zhang, X., Hamada, J., Nishimoto, A., Takahashi, Y., Murai, T., Tada, M., & Moriuchi, T. (2007) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00020.x · Cited by 34
S100B stimulates myoblast proliferation and inhibits myoblast differentiation by independently stimulating ERK1/2 and inhibiting p38 MAPK
Riuzzi, F., Sorci, G., & Donato, R. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20580 · Cited by 34 · cited 1×
“ture conditions, S100B inhibits myoblast differentiation and myotube formation and stimulates myoblast proliferation via bFGF/FGFR1 activation.(111,113,114) On the other hand, in”
Age-dependent increase in angiopoietin-like protein 2 accelerates skeletal muscle loss in mice
Zhao, J., Tian, Z., Kadomatsu, T., Xie, P., Miyata, K., Sugizaki, T., Endo, M., Zhu, S., Fan, H., Horiguchi, H., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.814996 · Cited by 34 · cited 1×
“rophy, accompanied by increased SC activity and inhibition of muscular atrophy, than have wild-type mice.(78)”
Neutrophils Provide a Favorable IL-1-Mediated Immunometabolic Niche that Primes GLUT4 Translocation and Performance in Skeletal Muscles
Tsuchiya, M., Sekiai, S., Hatakeyama, H., Koide, M., Chaweewannakorn, C., Yaoita, F., Tan–No, K., Sasaki, K., Watanabe, M., Sugawara, S., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.067 · Cited by 34 · cited 1×
“performance by priming exercise-dependent glucose transporter 4 translocation.(63) In addition, voluntary exercise was shown to elicit an acute oxidation-induced increase in Ca”
Background
Targeting RAGE as a potential therapeutic approach to Duchenne muscular dystrophy
Sagheddu, R., Chiappalupi, S., Salvadori, L., Riuzzi, F., Donato, R., & Sorci, G. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy288 · Cited by 34 · cited 1×
“ment of dystrophic muscles with a RAGE blocking antibody results in reduced necrosis and inflammatory infiltrate.(117)”
Replicating myoblasts and fused myotubes express the calcium-regulated proteins S100A1 and S100B
Sorci, G., Bianchi, R., Giambanco, I., Rambotti, M. G., & Donato, R. (1999) · Cell Calcium · doi:10.1054/ceca.1998.0012 · Cited by 33
S100B in myoblasts regulates the transition from activation to quiescence and from quiescence to activation and reduces apoptosis
Tubaro, C., Arcuri, C., Giambanco, I., & Donato, R. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.11.015 · Cited by 30 · cited 2×
“few hours of culture in differentiation medium is permissive for differentiation as persistence of relatively high S100B levels results in the inhibition of myogenic differentiation.(120)”
Chromatin signaling in muscle stem cells: interpreting the regenerative microenvironment
Brancaccio, A., & Palacios, D. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00036 · Cited by 24
The many faces of S100B protein: when an extracellular factor inactivates its own receptor and activates another one
Sorci, G., Riuzzi, F., Arcuri, C., Bianchi, R., Brozzi, F., Tubaro, C., Giambanco, I., & Donato, R. (2010) · Italian Journal of Anatomy and Embryology · doi:10.36253/ijae-1073 · Cited by 21
RAGE signaling deficiency in rhabdomyosarcoma cells causes upregulation of PAX7 and uncontrolled proliferation
Riuzzi, F., Sorci, G., Sagheddu, R., Sidoni, A., Alaggio, R., Ninfo, V., & Donato, R. (2014) · Journal of Cell Science · doi:10.1242/jcs.136259 · Cited by 17
Physiological and biochemical characteristics of skeletal muscles in sedentary and active rats
Xu, H., Ren, X., Lamb, G. D., & Murphy, R. M. (2018) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-018-9493-0 · Cited by 17 · cited 1×
“sensitivity in Type II fibres, and specific force production was found to be 10–25% lower in muscle fibres of sedentary compared with active rats with accompanying decrease in excitability of skinned fibres.(64) Thus, physical exercise appears to be the most efficient means to contrast sarcopenia.”
The Activation of Protein Kinase A by the Calcium-Binding Protein S100A1 Is Independent of Cyclic AMP
Melville, Z., Hernández‐Ochoa, E. O., Pratt, S. J. P., Liu, Y., Pierce, A. D., Wilder, P. T., Adipietro, K. A., Breysse, D. H., Varney, K. M., Schneider, M. F., et al. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00117 · Cited by 16 · cited 3×
“Given the S100B ’ s localization to the sarcoplasmic reticulum and transverse tubules similar to S100A1, 92,93 a member of the S100 family of Ca 2+ -binding proteins that is 56% identical to S100B, 89 one may hypothesize that S100B might regulate ryanodine receptor 1 and/or sarco(endo)plasmic reticulum calcium-ATPase…”
Deficiency of S100B confers resistance to experimental diabetes in mice
Mohammadzadeh, F., Tsoporis, J. N., Izhar, S., Desjardins, J., & Parker, T. G. (2018) · Experimental Cell Research · doi:10.1016/j.yexcr.2018.02.030 · Cited by 11 · cited 1×
“Further, S100B becomes expressed in activated CD3 T lymphocytes infiltrating pancreatic islets in an animal model of diabetes.(97) Moreover, S100B becomes expressed in breast tumour epithelial cells”
Causes of elevated serum levels of S100B protein in athletes
Donato, R., Riuzzi, F., & Sorci, G. (2012) · European Journal of Applied Physiology · doi:10.1007/s00421-012-2566-7 · Cited by 9
S100B impairs glycolysis via enhanced poly(ADP-ribosyl)ation of glyceraldehyde-3-phosphate dehydrogenase in rodent muscle cells
Hosokawa, K., Hamada, Y., Fujiya, A., Murase, M., Maekawa, R., Niwa, Y., Izumoto, T., Seino, Y., Tsunekawa, S., & Arima, H. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00328.2016 · Cited by 6 · cited 1×
“not been committed to differentiation resume expressing S100B once transferred back to proliferation medium.(118)”
Background

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Authors: Riuzzi, F., Sorci, G., Arcuri, C., Giambanco, I., Bellezza, I., Minelli, A., & Donato, R.
Affiliations: University of Perugia (IT)
Corresponding author: Donato, Rosario
ORCID: Riuzzi, Francesca
Sorci, Guglielmo
Arcuri, Cataldo
Giambanco, Ileana
Bellezza, Ilaria
Minelli, Alba
Donato, Rosario
Venue: Journal of Cachexia Sarcopenia and Muscle
Publisher: Wiley
Published: 2018-11-30
Volume: 9
Issue: 7
Pages: 1255-1268
ISSN: 2190-5991 (ISSN-L)
2190-6009
DOI: 10.1002/jcsm.12363
PMC: PMC6351675
OpenAlex: W2903461337
Cited by: 114
References: 152
Citations by year: 2026: 7 · 2025: 17 · 2024: 22 · 2023: 16 · 2022: 17 · 2021: 13 · 2020: 16 · 2019: 5 · 2018: 1
FWCI: 0.86
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by-nc-nd
creativecommons.org/licenses/by-nc-nd/4.0/ (vor)
Locations: Journal of Cachexia Sarcopenia and Muscle (publishedVersion, cc-by-nc-nd)
Europe PMC (PubMed Central) (publishedVersion, other-oa)
PubMed Central (publishedVersion, cc-by-nc-nd)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Fondazione Cassa di Risparmio di Perugia (2016‐0136.021, 2012.0241.021, 2015.0325.021)
Associazione Italiana per la Ricerca sul Cancro (17581)
French Muscular Dystrophy Association (16812, 12992)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Physiology (medical) › Nutrition and Health in Aging
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
Keywords: sarcopenia, S100B, satellite cells, calcium-sensing proteins, reactive oxygen species, aging, muscle stem cells
MeSH terms: Humans, Biomarkers, Muscle, Skeletal, Muscle Fibers, Skeletal, Satellite Cells, Skeletal Muscle, Sarcopenia, S100 Calcium Binding Protein beta Subunit

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Cellular and molecular mechanisms of sarcopenia: the S100B perspective

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