PKM2 is a Novel Osteoporosis-Associated Protein in Chinese

References

• Sharma R, Callaway D, Vanegas D, et al. Caspase-2 maintains bone homeostasis by inducing apoptosis of oxidatively-damaged osteoclasts. PLoS One. 2014;9(4):e93696. doi:10.1371/journal.pone.0093696.
   PubMed Web of Science ®Google Scholar
• Curtis EM, Moon RJ, Harvey NC, Cooper C. The Impact of Fragility Fracture and Approaches to Osteoporosis Risk Assessment Worldwide. Vol. 104. Bone; 2017:29–38. doi:10.1016/j.bone.2017.01.024.
   Google Scholar
• Pulkkinen P, Partanen J, Jalovaara P, Jamsa T. Combination of bone mineral density and upper femur geometry improves the prediction of hip fracture. Osteoporos Int. 2004;15(4):274–280. doi:10.1007/s00198-003-1556-3.
   PubMed Web of Science ®Google Scholar
• Dy CJ, McCollister KE, Lubarsky DA, Lane JM. An economic evaluation of a systems-based strategy to expedite surgical treatment of hip fractures. J Bone Joint Surg Am. 2011;93(14):1326–1334. doi:10.2106/JBJS.I.01132.
   PubMedGoogle Scholar
• Cheng CH, Chen LR, Chen KH. Osteoporosis due to hormone imbalance: an overview of the effects of estrogen deficiency and glucocorticoid overuse on bone turnover. Int J Mol Sci. 2022;23(3):23. doi:10.3390/ijms23031376.
   Web of Science ®Google Scholar
• Cheng C, Wentworth K, Shoback DM. New frontiers in osteoporosis therapy. Annu Rev Med. 2020;71(1):277–288. doi:10.1146/annurev-med-052218-020620.
   PubMedGoogle Scholar
• Hu LF, Yin C, Zhao F, Ali A, Ma JH, Qian AR. Mesenchymal stem cells: cell fate decision to osteoblast or adipocyte and application in osteoporosis treatment. Int J Mol Sci. 2018;19(2):360. doi:10.3390/ijms19020360.
   PubMed Web of Science ®Google Scholar
• Macías I, Alcorta-Sevillano N, Rodríguez CI, Infante A. Osteoporosis and the potential of cell-based therapeutic strategies. Int J Mol Sci. 2020;21(5):21. doi:10.3390/ijms21051653.
   Web of Science ®Google Scholar
• Narni-Mancinelli E, Soudja SM, Crozat K, et al. Inflammatory monocytes and neutrophils are licensed to kill during memory responses in vivo. PloS Pathog. 2011;7(12):e1002457. doi:10.1371/journal.ppat.1002457.
   PubMed Web of Science ®Google Scholar
• Zhou Y, Deng HW, Shen H. Circulating monocytes: an appropriate model for bone-related study. Osteoporos Int. 2015;26(11):2561–72. doi:10.1007/s00198-015-3250-7.
   PubMed Web of Science ®Google Scholar
• Deng FY, Long JR, Lei SF, Li MX, Deng HW. Potential effect of inter-genic action on peak bone mass (PBM) in Chinese females. Yi Chuan Xue Bao = Acta Genetica Sinica. 2005;32:1003–1010.
   PubMedGoogle Scholar
• Fredoni M, Ghatrehsamani M, Abdollahifar MA, Bayat S, Bayat M. Evaluation of the effects of photobiomodulation on vertebras in two rat models of experimental osteoporosis. Lasers Med Sci. 2017;32(7):1545–1560. doi:10.1007/s10103-017-2278-7.
   PubMed Web of Science ®Google Scholar
• Hwang MH, Kim KS, Yoo CM, et al. Photobiomodulation on human annulus fibrosus cells during the intervertebral disk degeneration: extracellular matrix-modifying enzymes. Lasers Med Sci. 2016;31(4):767–777. doi:10.1007/s10103-016-1923-x.
   PubMed Web of Science ®Google Scholar
• Schurman L, Sedlinsky C, Mangano A, et al. Estrogenic status influences nitric oxide-regulated TNF-α release from human peripheral blood monocytes. Exp Clin Endocrinol Diabetes. 2001;109(6):340–344. doi:10.1055/s-2001-17401.
   PubMed Web of Science ®Google Scholar
• Gordon S, Taylor PR. Monocyte and macrophage heterogeneity. Nat Rev Immunol. 2005;5(12):953–64. doi:10.1038/nri1733.
   PubMed Web of Science ®Google Scholar
• Ly T, Endo A, Brenes A, Gierlinski M, Afzal V, Pawellek A, et al. Proteome-wide analysis of protein abundance and turnover remodelling during oncogenic transformation of human breast epithelial cells. Wellcome Open Res. 2018;3:51. doi:10.12688/wellcomeopenres.14392.1.
   PubMedGoogle Scholar
• Eliuk S, Makarov A. Evolution of orbitrap mass spectrometry instrumentation. Annu Rev Anal Chem (Palo Alto Calif). 2015;8(1):61–80. doi:10.1146/annurev-anchem-071114-040325.
   PubMedGoogle Scholar
• Michalski A, Damoc E, Hauschild JP, et al. Mass spectrometry-based proteomics using Q exactive, a high-performance benchtop quadrupole orbitrap mass spectrometer. Mol Cell Proteomics. 2011;10(9):M111 011015. doi:10.1074/mcp.M111.011015.
   PubMed Web of Science ®Google Scholar
• Zhou X, Wu LF, Wang WY, et al. Anxa2 attenuates osteoblast growth and is associated with hip BMD and osteoporotic fracture in Chinese elderly. PLoS One. 2018;13(3):e0194781. doi:10.1371/journal.pone.0194781.
   PubMed Web of Science ®Google Scholar
• Marques GS, Silva Z, Videira PA. Antitumor efficacy of human monocyte-derived dendritic cells: comparing effects of two monocyte isolation methods. Biol Proced Online. 2018;20. doi:10.1186/s12575-018-0069-6.
   PubMed Web of Science ®Google Scholar
• Cox J, Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol. 2008;26(12):1367–72. doi:10.1038/nbt.1511.
   PubMed Web of Science ®Google Scholar
• Cox J, Neuhauser N, Michalski A, Scheltema RA, Olsen JV, Mann M. Andromeda: a peptide search engine integrated into the MaxQuant environment. J Proteome Res. 2011;10(4):1794–1805. doi:10.1021/pr101065j.
   PubMed Web of Science ®Google Scholar
• China Health Promotion Foundation White Paper China. Osteoporosis a summary statement of China. Beijing, 2008.
   Google Scholar
• Cox J, Hein MY, Luber CA, Paron I, Nagaraj N, Mann M. Accurate Proteome-Wide Label-Free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ. Mol Cell Proteomics. 2014;13(9):2513-26.
   Google Scholar
• Nahnsen S, Bielow C, Reinert K, Kohlbacher O. Tools for Label-Free Peptide Quantification. Molecular & Cellular Proteomics; 2013;12(3):549–556.
   Google Scholar
• Maycas M, Portoles MT, Matesanz MC, Buendia I, Linares J, Feito MJ, Arcos D, Vallet‐Regí M, Plotkin LI, Esbrit P, AR Gortázar. High glucose alters the secretome of mechanically stimulated osteocyte-like cells affecting osteoclast precursor recruitment and differentiation. J Cell Physiol. 2017;232(12):3611–21. doi:10.1002/jcp.25829.
   PubMed Web of Science ®Google Scholar
• Zhou X, Li CH, He P, et al. Ab1 interactor 1: a novel biomarker for osteoporosis in Chinese elderly men. J Proteomics. 2019;207:103440. doi:10.1016/j.jprot.2019.103440.
   PubMed Web of Science ®Google Scholar
• Parfitt AM. Osteoclast Precursors as Leukocytes: Importance of the Area Code. Bone. 1998;23(6):491–494.
   Google Scholar
• Sapkota M, Li L, Choi H, Gerwick WH, Soh Y. Bromo-honaucin a inhibits osteoclastogenic differentiation in RAW 264.7 cells via akt and ERK signaling pathways. Eur J Pharmacol. 2015;769:100–109. doi:10.1016/j.ejphar.2015.11.003.
   PubMed Web of Science ®Google Scholar
• Teitelbaum SL. Bone resorption by osteoclasts. Science. 2000;289(5484):1504–8. doi:10.1126/science.289.5484.1504.
   PubMed Web of Science ®Google Scholar
• Drake MT, Clarke BL, Oursler MJ, Khosla S. Cathepsin K inhibitors for osteoporosis: biology, potential clinical utility, and lessons learned. Endocr Rev. 2017;38(4):325–50. doi:10.1210/er.2015-1114.
   PubMed Web of Science ®Google Scholar
• Padamsey Z, McGuinness L, Bardo SJ, Reinhart M, Tong R, Hedegaard A, et al. Activity-dependent exocytosis of lysosomes regulates the structural plasticity of dendritic spines. Neuron. 2017;93(1):132–46. doi:10.1016/j.neuron.2016.11.013.
   PubMed Web of Science ®Google Scholar
• Guo JC, Ren RY, Yao XD, Ye YP, Sun K, Lin JM, et al. PKM2 suppresses osteogenesis and facilitates adipogenesis by regulating β-catenin signaling and mitochondrial fusion and fission. Aging-Us. 2020;12(4):3976–92. doi:10.18632/aging.102866.
   Web of Science ®Google Scholar
• Murakami K, Yoshino M. Zinc inhibition of pyruvate kinase of M-type isozyme. Biometals. 2017;30(3):335–40. doi:10.1007/s10534-017-0009-y.
   PubMed Web of Science ®Google Scholar
• Yang W, Lu Z. Pyruvate kinase M2 at a glance. J Cell Sci. 2015;128:1655–60. doi:10.1242/jcs.166629.
   PubMed Web of Science ®Google Scholar
• Yang WW, Xia Y, Ji HT, et al. Nuclear PKM2 regulates β-catenin transactivation upon EGFR activation. Nature. 2011;480(7375):118–122. doi:10.1038/nature10598.
   PubMed Web of Science ®Google Scholar
• Gao X, Wang H, Yang JJ, Liu X, Liu ZR. Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase. Mol Cell. 2012;45(5):598–609. doi:10.1016/j.molcel.2012.01.001.
   PubMed Web of Science ®Google Scholar
• Dong G, Mao Q, Xia W, Xu Y, Wang J, Xu L, Jiang F PKM2 and cancer: the function of PKM2 beyond glycolysis. Oncol Lett. 2016;11(3):1980–6. doi:10.3892/ol.2016.4168.
   PubMed Web of Science ®Google Scholar
• Han DW, Choi YS, Kim HW, Shin S, Ha YJ, Kang EH, Park, JW, Park, JK, Shin, K, Song, YW, Lee, YJ Extracellular pyruvate kinase M2 promotes osteoclastogenesis and is associated with radiographic progression in early rheumatoid arthritis. SCI REP-UK. 2022;12(1):12. doi:10.1038/s41598-022-07667-6.
   PubMed Web of Science ®Google Scholar
• Kim H, Takegahara N, Choi Y. IgSF11-mediated phosphorylation of pyruvate kinase M2 regulates osteoclast differentiation and prevents pathological bone loss. Bone Res. 2023;11(1):11. doi:10.1038/s41413-023-00251-2.
   PubMed Web of Science ®Google Scholar
• Dayton TL, Jacks T, Vander Heiden MG. PKM2, cancer metabolism, and the road ahead. EMBO Rep. 2016;17(12):1721–1730. doi:10.15252/embr.201643300.
   PubMed Web of Science ®Google Scholar
• Liang J, Cao R, Zhang Y, Xia Y, Zheng Y, Li X, Wang, L, Yang, W, Lu, Z PKM2 dephosphorylation by Cdc25A promotes the Warburg effect and tumorigenesis. Nat Commun. 2016;7(1):12431. doi:10.1038/ncomms12431.
   PubMedGoogle Scholar
• Liu F, Ma F, Wang Y, Hao L, Zeng H, Jia C, et al. PKM2 methylation by CARM1 activates aerobic glycolysis to promote tumorigenesis. Nat Cell Biol. 2017;19(11):1358–70. doi:10.1038/ncb3630.
   PubMed Web of Science ®Google Scholar
• Wong N, Ojo D, Yan J, Tang D. PKM2 contributes to cancer metabolism. Cancer Lett. 2015;356(2):184–91. doi:10.1016/j.canlet.2014.01.031.
   PubMed Web of Science ®Google Scholar
• Hsu MC, Hung WC, Yamaguchi H, et al. Extracellular PKM2 induces cancer proliferation by activating the EGFR signaling pathway. Am J Cancer Res. 2016;6(3):628–638.
   PubMed Web of Science ®Google Scholar
• Dai JL, Escara-Wilke J, Keller JM, Jung Y, Taichman R, Pienta KJ, Keller ET Primary prostate cancer educates bone stroma through exosomal pyruvate kinase M2 to promote bone metastasis. J Exp Med. 2019;216(12):2883–99. doi:10.1084/jem.20190158.
   PubMed Web of Science ®Google Scholar