Researchers identified an active form of AMP‐activated protein kinase (AMPK) localized at the intercalated disks in the heart, a specific cell–cell junction present between cardiomyocytes.
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Yashirogi, S., Nagao, T., Nishida, Y., Takahashi, Y., Qaqorh, T., Yazawa, I., Katayama, T., Kioka, H., Matsui, T. S., Saito, S., Masumura, Y., Tsukamoto, O., Kato, H., Ueda, H., Yamaguchi, O., Yashiro, K., Yamazaki, S., Takashima, S., & Shintani, Y. (2020). AMPK regulates cell shape of cardiomyocytes by modulating turnover of microtubules through CLIP-170. EMBO Reports, n/a(n/a), e50949. https://doi.org/10.15252/embr.202050949 Cite
To determine the intracellular mechanisms involved in the cardiac effects of oxidized low-density lipoprotein (oxLDL), the authors analyzed the in vitro effect of oxLDL on intracellular Ca2+ handling in adult rat ventricular cardiomyocytes using confocal microscopy.
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Rodríguez-Sánchez, E., Navarro-García, J. A., González-Lafuente, L., Aceves-Ripoll, J., Vázquez-Sánchez, S., Poveda, J., Mercado-García, E., Corbacho-Alonso, N., Calvo-Bonacho, E., Fernández-Velasco, M., Álvarez-Llamas, G., Barderas, M. G., Ruilope, L. M., & Ruiz-Hurtado, G. (2020). Oxidized Low-Density Lipoprotein Associates with Ventricular Stress in Young Adults and Triggers Intracellular Ca2+ Alterations in Adult Ventricular Cardiomyocytes. Antioxidants, 9(12), 1213. https://doi.org/10.3390/antiox9121213 Cite
Activation of free fatty acid receptors which are G protein-coupled receptors with established (patho)physiological roles in a variety of obesity-related disorders, induce human airway smooth muscle (HASM) cell proliferation and shortening. Scientists reported amplified agonist-induced cell shortening in HASM cells obtained from obese lung donors.
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Xu, S., Schwab, A., Karmacharya, N., Cao, G., Woo, J., Kim, N., An, S. S., Panettieri Jr, R. A., & Jude, J. A. (2020). FFAR1 activation attenuates histamine-induced myosin light chain phosphorylation and cortical tension development in human airway smooth muscle cells. Respiratory Research, 21(1), 317. https://doi.org/10.1186/s12931-020-01584-w Cite
Researchers investigated the role of sodium‑glucose cotransporter 1 (SGLT1) in rat H9c2 cardiomyocytes subjected to glucose fluctuation and the underlying mechanisms. They indicated that SGLT1 knockdown was able to restore cell proliferation and suppress cytotoxicity induced by glucose fluctuation.
[Biochemistry and Cell Biology]
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Chai, M. Q., Miao, M. J., Liu, M. M., Zhang, M. Z., Meng, M. Z., & Wu, P. W. (2020, December 1). SGLT1 knockdown prevents glucose fluctuation-induced apoptosis of cardiomyocytes through attenuating oxidative stress and mitochondrial dysfunction [Research-article]. Https://Doi.Org/10.1139/Bcb-2020-0491. https://doi.org/10.1139/bcb-2020-0491 Cite
Scientists examined several proteomic- and RNA-Seq-based datasets of cardiac-enriched, cell-surface and membrane-associated proteins in human fetal and mouse neonatal ventricular cardiomyocytes.
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Lee, S.-H., Hadipour-Lakmehsari, S., Kim, D. H., Di Paola, M., Kuzmanov, U., Shah, S., Lee, J. J.-H., Kislinger, T., Sharma, P., Oudit, G. Y., & Gramolini, A. O. (2020). Bioinformatic analysis of membrane and associated proteins in murine cardiomyocytes and human myocardium. Scientific Data, 7(1), 425. https://doi.org/10.1038/s41597-020-00762-1 Cite
Scientists showed that protein levels of the Bromodomain and extra-terminal domain (BET) protein BRD4 were significantly increased in the muscle of the mouse model of Duchenne muscular dystrophy, the mdx mouse, and that pharmacological inhibition of the BET proteins had a beneficial outcome, tempering oxidative stress and muscle damage.
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Segatto, M., Szokoll, R., Fittipaldi, R., Bottino, C., Nevi, L., Mamchaoui, K., Filippakopoulos, P., & Caretti, G. (2020). BETs inhibition attenuates oxidative stress and preserves muscle integrity in Duchenne muscular dystrophy. Nature Communications, 11(1), 6108. https://doi.org/10.1038/s41467-020-19839-x Cite
The authors demonstrated that the Hippo pathway effectors YAP and TAZ play a critical role in maintaining the differentiated contractile phenotype of vascular smooth muscle cells.
Scientists discuss recent findings of miR‐128 in relation to bone metabolism and muscle regeneration to determine its potential therapeutic effects in musculoskeletal diseases, and to propose directions for future research in this significant field.
[Journal of Cellular Physiology]
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Shang, Q., Shen, G., Chen, G., Zhang, Z., Yu, X., Zhao, W., Zhang, P., Chen, H., Tang, K., Yu, F., Tang, J., Liang, D., Jiang, X., & Ren, H. (n.d.). The emerging role of miR-128 in musculoskeletal diseases. Journal of Cellular Physiology, n/a(n/a). https://doi.org/https://doi.org/10.1002/jcp.30179 Cite
The authors observed altered interactions between coactivator-associated arginine methyltransferase 1 (CARM1) and AMP-activated protein kinase (AMPK) and its network, including forkhead box protein O1, during muscle disuse.
Researchers identified nine distinct major clusters including myeloid‐derived cells, fibroblast/fibro/adipogenic progenitors, and skeletal muscle stem cells in glycerol‐injured skeletal muscle.
[Journal of Cachexia Sarcopenia and Muscle]
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Xu, Z., You, W., Chen, W., Zhou, Y., Nong, Q., Valencak, T. G., Wang, Y., & Shan, T. (n.d.). Single-cell RNA sequencing and lipidomics reveal cell and lipid dynamics of fat infiltration in skeletal muscle. Journal of Cachexia, Sarcopenia and Muscle, n/a(n/a). https://doi.org/https://doi.org/10.1002/jcsm.12643 Cite
Investigators generated muscle stem cell‐specific androgen receptor and estrogen receptor 2 double knockout mice and pharmacologically inhibited the hypothalamic–pituitary–gonadal axis to mimic decreased serum levels of sex steroid hormones in aged mice.
[Journal of Cachexia Sarcopenia and Muscle]
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Kim, J.-H., Park, I., Shin, H. R., Rhee, J., Seo, J.-Y., Jo, Y.-W., Yoo, K., Hann, S.-H., Kang, J.-S., Park, J., Kim, Y. L., Moon, J.-Y., Choi, M. H., & Kong, Y.-Y. (n.d.). The hypothalamic–pituitary–gonadal axis controls muscle stem cell senescence through autophagosome clearance. Journal of Cachexia, Sarcopenia and Muscle, n/a(n/a). https://doi.org/https://doi.org/10.1002/jcsm.12653 Cite