Определение протеомных маркеров, включенных в молекулярные сети нарушений в костной системе во время продолжительных космических полетов

Л.Х. Пастушкова; А.Г. Гончарова; Д.Н. Каширина; А.В. Поляков; И.М. Ларина

doi:10.18127/j20700997-202501-01

Определение протеомных маркеров, включенных в молекулярные сети нарушений в костной системе во время продолжительных космических полетов

Л.Х. Пастушкова¹, А.Г. Гончарова², Д.Н. Каширина³, А.В. Поляков⁴, И.М. Ларина⁵

научная статья УДК 577.29, 611.018.41 Страницы: 5-21 doi.org/10.18127/j20700997-202501-01

^1,2,3,4,5 Государственный научный центр Российской Федерации – Институт медико-биологических проблем РАН (Москва, Россия)

Ключевые слова: Длительные космические полеты сухие пятна крови протеом костная система

Аннотация

Постановка проблемы. Учитывая снижение минеральной плотности костной ткани, выявляемое во время длительных космических полетов (КП), актуально изучение молекулярных механизмов регуляции состояния костной ткани во время КП методами протеомики.

Цель работы – определение протеомных маркеров, включенных в молекулярные сети компенсации морфофункциональных изменений костной системы в разные сроки длительных КП.

Результаты. Установлено достоверное изменение белков – участников адаптивных процессов, происходящих в костной ткани на 7-е сутки, 3- и 6-й месяцы КП. Биоинформационные методы анализа протеома сухих пятен крови показали, что на 7-е сутки полета с биологическими процессами костной системы связаны 11 белков. На 3-й месяц в биологических процессах участвует 13 достоверно изменяющихся белков, из них 6 протеинов выявлены только в этом временно́м периоде. На 6-й месяц определены 10 белков, из них – 2 новых. Отмечено, что в каждой точке исследования все характерные для структурно-функциональной адаптации костной системы белки были связаны в единую молекулярную сеть. Приведены краткая аннотация функций и значения каждого белка.

Практическая значимость. Полученные данные углубляют представления о молекулярных механизмах, сопровождающих процессы адаптации костной ткани в условиях КП, в том числе – выявление сети белок-белковых взаимодействий. Это, в свою очередь, позволяет предложить определенные белки в качестве потенциальных мишеней в программе разработки эффективных мер профилактики нарушений костной системы в длительных КП.

Поступила: 24.12.2024
Одобрена: 13.01.2025
Принята: 14.02.2025

Для цитирования

Пастушкова Л.Х., Гончарова А.Г., Каширина Д.Н., Поляков А.В., Ларина И.М. Определение протеомных маркеров, включенных в молекулярные сети нарушений в костной системе во время продолжительных космических полетов // Технологии живых систем. 2025. T. 22. № 1. С. 5-21. DOI: https://doi.org/10.18127/j20700997-202501-01

Список источников

Levin V.A., Jiang X., Kagan R. Estrogen therapy for osteoporosis in the modern era // Osteoporos Int. 2018. V. 29(5). P. 1049-1055. DOI: 10.1007/s00198-018-4414-z
Grimm D., Grosse J., Wehland M. et al. The impact of microgravity on bone in humans // Bone. 2016. V. 87. P.44-56. DOI: 10.1016/j.bone.2015.12.057
Man J., Graham T., Squires-Donelly G., Laslett A.L. The effects of microgravity on bone structure and function// NPJ Microgravity. 2022. V. 8(1). P. 9. DOI: 10.1038/s41526-022-00194-8
Gao H., Peng X., Li N. et al. Emerging role of liver-bone axis in osteoporosis // J. Orthop. Translat. 2024. V. 48. P. 217-231. DOI: 10.1016/j.jot.2024.07.008
Lee Satcher R., Fiedler B., Ghali A., Dirschl D.R. Effect of Spaceflight and Microgravity on the Musculoskeletal System: A Review // Am. Acad. Orthop. Surg. 2024. V. 32(12). P. 535-541. DOI: 10.5435/JAAOS-D-23-00954
Dakkumadugula A., Pankaj L., Alqahtani A.S. et al. Space nutrition and the biochemical changes caused in Astronauts Health due to space flight: A review // Food Chem X. 2023. V. 20. Article 100875. DOI: 10.1016/j.fochx.2023.100875
Меркурьева О.Н., Бабкина И.В., Булычева И.В. и др. Клинико-лабораторное значение эндостатина в сыворотке крови подростков с саркомами костей // Технологии живых систем. 2022. Т. 19. № 4. С. 24-32.
Оганов В.С., Григорьев А.И. О механизмах остеопении и особенностях метаболизма костной ткани человека в условиях невесомости // Российский физиологический журнал им. И.М. Сеченова. 2012. Т. 98. № 3. С. 91-105.
Vico L., Hargens A. Skeletal changes during and after spaceflight // Nat. Rev. Rheumatol. 2018. V. 14(4). P. 229-245. DOI: 10.1038/nrrheum.2018.37
Smith S.M., Wastney M.E., O'Brien K.O. et al. Bone markers, calcium metabolism, and calcium kinetics during extended-duration space flight on the mir space station // J. Bone Miner. Res. 2005. V. 20(2). P. 208-218. DOI: 10.1359/JBMR.041105
Xu J., Cai X., Miao Z. et al. Proteome-wide profiling reveals dysregulated molecular features and accelerated aging in osteoporosis: A 9.8-year prospective study // Aging Cell. 2024. V. 23(2). Article 14035. DOI: 10.1111/acel.14035
Пастушкова Л.Х., Гончарова А.Г., Васильева Г.Ю. и др. Поиск белков протеома крови-регуляторов костного ремоделирования у космонавтов // Физиология человека. 2019. № 5. С. 91-98.
Kononikhin A.S., Starodubtseva N.L., Brzhozovskiy A.G. et al. Absolute Quantitative Targeted Monitoring of Potential Plasma Protein Biomarkers: A Pilot Study on Healthy Individuals // Biomedicines. 2024. № 12. P. 2403. https://doi.org/10.3390/biomedicines 12102403
Mori K., Emoto M., Inaba M. Fetuin-A: a multifunctional protein // Recent Pat Endocr. Metab. Immune Drug Discov. 2011. V. 5(2). P. 124-146. DOI: 10.2174/187221411799015372
Mattinzoli D., Rastaldi M.P., Ikehata M. et al. FGF23-regulated production of Fetuin-A (AHSG) in osteocytes // Bone. 2016. V. 83. P. 35-47. DOI: 10.1016/j.bone.2015.10.008
Polan C., Brenner C., Herten M. et al. Increased UHMWPE Particle-Induced Osteolysis in Fetuin-A-Deficient Mice // J. Funct. Biomater. 2023. V. 14(1). P. 30. DOI: 10.3390/jfb14010030
van den Akker G.G.H., Steijns J.S.J.J., Stassen R.H.M.J. et al. Development of a cyclic-inverso AHSG/Fetuin A-based peptide for inhibition of calcification in osteoarthritis // Osteoarthritis Cartilage. 2023. V. 31(6). P. 727-740. DOI: 10.1016/j.joca.2022.11.007
Muzasti R.A., Suhardjono D., Purwanto B., Juwita Sembiring R. Is there an association between alpha 2-Heremans-Schmid glycoprotein (AHSG) gene Thr256Ser polymorphisms with aortic calcification in regular hemodialysis patients in Medan Indonesia // Med. Glas. (Zenica). 2020. V. 17(1). P. 46-53. DOI: 10.17392/1072-20
Keskin M., Culha C., Gulcelik N.E. et al. The evaluation of preoperative and postoperative fetuin-A levels in patients with primary hyperparathyroidism // Niger. J. Clin. Pract. 2019. V. 22(3). P. 320-327. DOI: 10.4103/njcp.njcp_323_18
Duan X., Xing F., Zhang J. et al. Bioinformatic analysis of related immune cell infiltration and key genes in the progression of osteonecrosis of the femoral head // Front. Immunol. 2024. V. 14. Article 1340446. DOI: 10.3389/fimmu.2023.1340446
Pereira L.C., Nascimento J.C.R., Rêgo J.M.C. et al. Apolipoprotein E, periodontal disease and the risk for atherosclerosis: a review // Arch. Oral. Biol. 2019. V. 98. P. 204-212. DOI: 10.1016/j.archoralbio.2018.11.009
Souza L.S., Rochette N.F., Pedrosa D.F. et al. Role of APOE Gene in Bone Mineral Density and Incidence of Bone Fractures in Brazilian Postmenopausal Women // J. Clin. Densitom. 2018. V. 21(2). P. 227-235. DOI: 10.1016/j.jocd.2017.03.005
Xu X., Luo H., Chen Q. et al. Detecting potential mechanism of vitamin D in treating rheumatoid arthritis based on network pharmacology and molecular docking // Front. Pharmacol. 2022. V. 13. Article 1047061. DOI: 10.3389/fphar.2022.1047061
Li Q., Zhu M., Liu X. et al. Abnormally low serum albumin levels are associated with abnormal bone mineral density and osteoporotic fractures: a retrospective studies // BMC Musculoskelet. Disord. 2024. V. 25(1). P. 888. DOI: 10.1186/s12891-024-08021-9
Kingston C.D., Santini S., Hauke D., Valderrabano V. Vitamin D and Albumin Deficiency in a Swiss Orthopaedic Surgery In-Patient Cohort // J. Clin. Med. 2024. V. 13(9). P. 2577. DOI: 10.3390/jcm13092577
Sadowska-Krępa E., Rzetecki A., Zając-Gawlak I. et al. Comparison of selected prooxidant-antioxidant balance and bone metabolism indicators and BDNF levels between older women with different levels of physical activity // BMC Geriatr. 2023. V. 23(1). P. 489. DOI: 10.1186/s12877-023-04205-5
Baxter R.C. Endocrine and cellular physiology and pathology of the insulin-like growth factor acid-labile subunit // Nat. Rev. Endocrinol. 2024. V. 20(7). P. 414-425. DOI: 10.1038/s41574-024-00970-4
Yakar S., Bouxsein M.L., Canalis E. et al. The ternary IGF complex influences postnatal bone acquisition and the skeletal response to intermittent parathyroid hormone // J. Endocrinol. 2006. V. 189(2). P. 289-299. DOI: 10.1677/joe.1.06657
Racine H.L., Serrat M.A. The Actions of IGF-1 in the Growth Plate and Its Role in Postnatal Bone Elongation // Curr. Osteoporos. Rep. 2020. V. 18(3). P. 210-227. DOI: 10.1007/s11914-020-00570-x
Тахчиди Х.П., Гаврилова Н.А., Гаджиева Н.С. и др. Клинические нормы. Офтальмология. М.: ГЭОТАР-Медиа. 2020. 272 c.
Duh E.J., Yang H.S., Suzuma I. et al. Pigment epithelium-derived factor suppresses ischemia-induced retinal neovascularization and VEGF-induced migration and growth // Invest. Ophthalmol. Vis. Sci. 2002. V. 43(3). P.821-829.
Chang X., Zheng Y., Yang Q. et al. Carbonic anhydrase I (CA1) is involved in the process of bone formation and is susceptible to ankylosing spondylitis // Arthritis Res. Ther. 2012. V. 14(4). P. R176. DOI: 10.1186/ar3929
Chang X., Han J., Zhao Y. et al. Increased expression of carbonic anhydrase I in the synovium of patients with ankylosing spondylitis // BMC Musculoskelet. Disord. 2010. V. 11. P. 279. DOI: 10.1186/1471-2474-11-279
Feng L., Wang Y., Zhou J. et al. Screening of differentially expressed genes in male idiopathic osteoporosis via RNA sequencing // Mol. Med. Rep. 2018. V. 18(1). P. 67-76. DOI: 10.3892/mmr.2018.8985
Sadvakassova G., Tiedemann K., Steer K.J.D. et al. Active hematopoiesis triggers exosomal release of PRDX2 that promotes osteoclast formation // Physiol. Rep. 2021. V. 9. Iss. 3. Article e14745. DOI: 10.14814/phy2.14745
Lee J.Y., Kim D.A., Kim E.Y. et al. Lumican Inhibits Osteoclastogenesis and Bone Resorption by Suppressing Akt Activity // Int. J. Mol. Sci. 2021. V. 22(9). P. 4717. DOI: 10.3390/ijms22094717
Huang Y., Wang C., Zhou T. et al. Lumican promotes calcific aortic valve disease through H3 histone lactylation // Eur. Heart J. 2024. V. 45(37). P. 3871-3885. DOI: 10.1093/eurheartj/ehae407
Park S.J., Ji E., Yoo H.J. et al. Circulating lumican as a potential biomarker for osteosarcopenia in older adults // Bone. 2024. V. 179. P. 116959. DOI: 10.1016/j.bone.2023.116959
Lee Y.S., Park S.J., Lee J.Y. et al. Benefits of lumican on human bone health: clinical evidence using bone marrow aspirates // Korean J. Intern. Med. 2022. V. 37(4). P. 821-829. DOI: 10.3904/kjim.2022.015
Park J., Jung M.J., Chung W.Y. The downregulation of IGFBP3 by TGF-β signaling in oral cancer contributes to the osteoclast differentiation // Biochem. Biophys. Res. Commun. 2021. V. 534. P. 381-386. DOI: 10.1016/j.bbrc.2020.11.073
Wang X., Qiu L., Yang Z. et al. Association between serum iron status and the risk of five bone and joint-related diseases: a Mendelian randomization analysis // Front. Endocrinol. (Lausanne). 2024. V. 15. P. 1364375. DOI: 10.3389/fendo.2024.1364375
Nay K., Koechlin-Ramonatxo C., Rochdi S. et al. Simulated microgravity disturbs iron metabolism and distribution in humans: Lessons from dry immersion, an innovative ground-based human model // FASEB J. 2020. V. 34(11). P. 14920-14929. DOI: 10.1096/fj.202001199RR
O'Leary T.J., Jackson S., Izard R.M. et al. Iron status is associated with tibial structure and vitamin D metabolites in healthy young men // Bone. 2024. V. 186. P. 117145. DOI: 10.1016/j.bone.2024.117145
Yanagihara Y., Inoue K., Saeki N. et al. Zscan10 suppresses osteoclast differentiation by regulating expression of Haptoglobin // Bone. 2019. V. 122. P. 93-100. DOI: 10.1016/j.bone.2019.02.011
Lerner U.H., Fröhlander N. Haptoglobin-stimulated bone resorption in neonatal mouse calvarial bones in vitro // Arthritis Rheum. 1992. V. 35(5). P. 587-591. DOI: 10.1002/art.1780350517
Mizumoto S., Yamada S. The Specific Role of Dermatan Sulfate as an Instructive Glycosaminoglycan in Tissue Development // Int. J. Mol. Sci. 2022. V. 23(13). P. 7485. DOI: 10.3390/ijms23137485
Min H.K., Kim S.H., Lee J.Y. et al. DJ-1 controls T cell differentiation and osteoclastogenesis in rheumatoid arthritis // Sci. Rep. 2022. V. 12(1). P. 12767. DOI: 10.1038/s41598-022-16285-1
Chen J., Ikeda S.I., Yang Y. et al. Scleral remodeling during myopia development in mice eyes: a potential role of thrombospondin-1 // Mol. Med. 2024. V. 30(1). P. 25. DOI: 10.1186/s10020-024-00795-x
Amend S.R., Uluckan O., Hurchla M. et al. Thrombospondin-1 regulates bone homeostasis through effects on bone matrix integrity and nitric oxide signaling in osteoclasts // J. Bone Miner. Res. 2015. V. 30(1). P. 106-115. DOI: 10.1002/jbmr.2308
Shi D., Liu X., Li X. et al. Yth m6A RNA-Binding Protein 1 Regulates Osteogenesis of MC3T3-E1 Cells under Hypoxia via Translational Control of Thrombospondin-1 // Int. J. Mol. Sci. 2023. V. 24(2). P. 1741. DOI: 10.3390/ijms24021741
Liu Z., Yuan X., Liu M. et al. Antimicrobial Peptide Combined with BMP2-Modified Mesenchymal Stem Cells Promotes Calvarial Repair in an Osteolytic Model // Mol. Ther. 2018. V. 26(1). P. 199-207. DOI: 10.1016/j.ymthe.2017.09.011
Li X.S., Zhang J.R., Zhao Y.L. et al. Reduced prealbumin is associated with bone mineral density in women with osteoporosis // Nutrition. 2017. V. 33. P. 338-342. DOI: 10.1016/j.nut.2016.08.002
Nakashima M., Suzuki A., Hashimoto K. et al. Vitronectin regulates osteoclastogenesis and bone remodeling in a mouse model of osteoporosis // Anat. Cell Biol. 2024. V. 57(2). P. 305-315. DOI: 10.5115/acb.23.251

[1] Levin V.A., Jiang X., Kagan R. Estrogen therapy for osteoporosis in the modern era // Osteoporos Int. 2018. V. 29(5). P. 1049-1055. DOI: 10.1007/s00198-018-4414-z

[2] Grimm D., Grosse J., Wehland M. et al. The impact of microgravity on bone in humans // Bone. 2016. V. 87. P.44-56. DOI: 10.1016/j.bone.2015.12.057

[3] Man J., Graham T., Squires-Donelly G., Laslett A.L. The effects of microgravity on bone structure and function// NPJ Microgravity. 2022. V. 8(1). P. 9. DOI: 10.1038/s41526-022-00194-8

[4] Gao H., Peng X., Li N. et al. Emerging role of liver-bone axis in osteoporosis // J. Orthop. Translat. 2024. V. 48. P. 217-231. DOI: 10.1016/j.jot.2024.07.008

[5] Lee Satcher R., Fiedler B., Ghali A., Dirschl D.R. Effect of Spaceflight and Microgravity on the Musculoskeletal System: A Review // Am. Acad. Orthop. Surg. 2024. V. 32(12). P. 535-541. DOI: 10.5435/JAAOS-D-23-00954

[6] Dakkumadugula A., Pankaj L., Alqahtani A.S. et al. Space nutrition and the biochemical changes caused in Astronauts Health due to space flight: A review // Food Chem X. 2023. V. 20. Article 100875. DOI: 10.1016/j.fochx.2023.100875

[7] Меркурьева О.Н., Бабкина И.В., Булычева И.В. и др. Клинико-лабораторное значение эндостатина в сыворотке крови подростков с саркомами костей // Технологии живых систем. 2022. Т. 19. № 4. С. 24-32.

[8] Оганов В.С., Григорьев А.И. О механизмах остеопении и особенностях метаболизма костной ткани человека в условиях невесомости // Российский физиологический журнал им. И.М. Сеченова. 2012. Т. 98. № 3. С. 91-105.

[9] Vico L., Hargens A. Skeletal changes during and after spaceflight // Nat. Rev. Rheumatol. 2018. V. 14(4). P. 229-245. DOI: 10.1038/nrrheum.2018.37

[10] Smith S.M., Wastney M.E., O'Brien K.O. et al. Bone markers, calcium metabolism, and calcium kinetics during extended-duration space flight on the mir space station // J. Bone Miner. Res. 2005. V. 20(2). P. 208-218. DOI: 10.1359/JBMR.041105

[11] Xu J., Cai X., Miao Z. et al. Proteome-wide profiling reveals dysregulated molecular features and accelerated aging in osteoporosis: A 9.8-year prospective study // Aging Cell. 2024. V. 23(2). Article 14035. DOI: 10.1111/acel.14035

[12] Пастушкова Л.Х., Гончарова А.Г., Васильева Г.Ю. и др. Поиск белков протеома крови-регуляторов костного ремоделирования у космонавтов // Физиология человека. 2019. № 5. С. 91-98.

[13] Kononikhin A.S., Starodubtseva N.L., Brzhozovskiy A.G. et al. Absolute Quantitative Targeted Monitoring of Potential Plasma Protein Biomarkers: A Pilot Study on Healthy Individuals // Biomedicines. 2024. № 12. P. 2403. https://doi.org/10.3390/biomedicines 12102403

[14] Mori K., Emoto M., Inaba M. Fetuin-A: a multifunctional protein // Recent Pat Endocr. Metab. Immune Drug Discov. 2011. V. 5(2). P. 124-146. DOI: 10.2174/187221411799015372

[15] Mattinzoli D., Rastaldi M.P., Ikehata M. et al. FGF23-regulated production of Fetuin-A (AHSG) in osteocytes // Bone. 2016. V. 83. P. 35-47. DOI: 10.1016/j.bone.2015.10.008

[16] Polan C., Brenner C., Herten M. et al. Increased UHMWPE Particle-Induced Osteolysis in Fetuin-A-Deficient Mice // J. Funct. Biomater. 2023. V. 14(1). P. 30. DOI: 10.3390/jfb14010030

[17] van den Akker G.G.H., Steijns J.S.J.J., Stassen R.H.M.J. et al. Development of a cyclic-inverso AHSG/Fetuin A-based peptide for inhibition of calcification in osteoarthritis // Osteoarthritis Cartilage. 2023. V. 31(6). P. 727-740. DOI: 10.1016/j.joca.2022.11.007

[18] Muzasti R.A., Suhardjono D., Purwanto B., Juwita Sembiring R. Is there an association between alpha 2-Heremans-Schmid glycoprotein (AHSG) gene Thr256Ser polymorphisms with aortic calcification in regular hemodialysis patients in Medan Indonesia // Med. Glas. (Zenica). 2020. V. 17(1). P. 46-53. DOI: 10.17392/1072-20

[19] Keskin M., Culha C., Gulcelik N.E. et al. The evaluation of preoperative and postoperative fetuin-A levels in patients with primary hyperparathyroidism // Niger. J. Clin. Pract. 2019. V. 22(3). P. 320-327. DOI: 10.4103/njcp.njcp_323_18

[20] Duan X., Xing F., Zhang J. et al. Bioinformatic analysis of related immune cell infiltration and key genes in the progression of osteonecrosis of the femoral head // Front. Immunol. 2024. V. 14. Article 1340446. DOI: 10.3389/fimmu.2023.1340446

[21] Pereira L.C., Nascimento J.C.R., Rêgo J.M.C. et al. Apolipoprotein E, periodontal disease and the risk for atherosclerosis: a review // Arch. Oral. Biol. 2019. V. 98. P. 204-212. DOI: 10.1016/j.archoralbio.2018.11.009

[22] Souza L.S., Rochette N.F., Pedrosa D.F. et al. Role of APOE Gene in Bone Mineral Density and Incidence of Bone Fractures in Brazilian Postmenopausal Women // J. Clin. Densitom. 2018. V. 21(2). P. 227-235. DOI: 10.1016/j.jocd.2017.03.005

[23] Xu X., Luo H., Chen Q. et al. Detecting potential mechanism of vitamin D in treating rheumatoid arthritis based on network pharmacology and molecular docking // Front. Pharmacol. 2022. V. 13. Article 1047061. DOI: 10.3389/fphar.2022.1047061

[24] Li Q., Zhu M., Liu X. et al. Abnormally low serum albumin levels are associated with abnormal bone mineral density and osteoporotic fractures: a retrospective studies // BMC Musculoskelet. Disord. 2024. V. 25(1). P. 888. DOI: 10.1186/s12891-024-08021-9

[25] Kingston C.D., Santini S., Hauke D., Valderrabano V. Vitamin D and Albumin Deficiency in a Swiss Orthopaedic Surgery In-Patient Cohort // J. Clin. Med. 2024. V. 13(9). P. 2577. DOI: 10.3390/jcm13092577

[26] Sadowska-Krępa E., Rzetecki A., Zając-Gawlak I. et al. Comparison of selected prooxidant-antioxidant balance and bone metabolism indicators and BDNF levels between older women with different levels of physical activity // BMC Geriatr. 2023. V. 23(1). P. 489. DOI: 10.1186/s12877-023-04205-5

[27] Baxter R.C. Endocrine and cellular physiology and pathology of the insulin-like growth factor acid-labile subunit // Nat. Rev. Endocrinol. 2024. V. 20(7). P. 414-425. DOI: 10.1038/s41574-024-00970-4

[28] Yakar S., Bouxsein M.L., Canalis E. et al. The ternary IGF complex influences postnatal bone acquisition and the skeletal response to intermittent parathyroid hormone // J. Endocrinol. 2006. V. 189(2). P. 289-299. DOI: 10.1677/joe.1.06657

[29] Racine H.L., Serrat M.A. The Actions of IGF-1 in the Growth Plate and Its Role in Postnatal Bone Elongation // Curr. Osteoporos. Rep. 2020. V. 18(3). P. 210-227. DOI: 10.1007/s11914-020-00570-x

[30] Тахчиди Х.П., Гаврилова Н.А., Гаджиева Н.С. и др. Клинические нормы. Офтальмология. М.: ГЭОТАР-Медиа. 2020. 272 c.

[31] Duh E.J., Yang H.S., Suzuma I. et al. Pigment epithelium-derived factor suppresses ischemia-induced retinal neovascularization and VEGF-induced migration and growth // Invest. Ophthalmol. Vis. Sci. 2002. V. 43(3). P.821-829.

[32] Chang X., Zheng Y., Yang Q. et al. Carbonic anhydrase I (CA1) is involved in the process of bone formation and is susceptible to ankylosing spondylitis // Arthritis Res. Ther. 2012. V. 14(4). P. R176. DOI: 10.1186/ar3929

[33] Chang X., Han J., Zhao Y. et al. Increased expression of carbonic anhydrase I in the synovium of patients with ankylosing spondylitis // BMC Musculoskelet. Disord. 2010. V. 11. P. 279. DOI: 10.1186/1471-2474-11-279

[34] Feng L., Wang Y., Zhou J. et al. Screening of differentially expressed genes in male idiopathic osteoporosis via RNA sequencing // Mol. Med. Rep. 2018. V. 18(1). P. 67-76. DOI: 10.3892/mmr.2018.8985

[35] Sadvakassova G., Tiedemann K., Steer K.J.D. et al. Active hematopoiesis triggers exosomal release of PRDX2 that promotes osteoclast formation // Physiol. Rep. 2021. V. 9. Iss. 3. Article e14745. DOI: 10.14814/phy2.14745

[36] Lee J.Y., Kim D.A., Kim E.Y. et al. Lumican Inhibits Osteoclastogenesis and Bone Resorption by Suppressing Akt Activity // Int. J. Mol. Sci. 2021. V. 22(9). P. 4717. DOI: 10.3390/ijms22094717

[37] Huang Y., Wang C., Zhou T. et al. Lumican promotes calcific aortic valve disease through H3 histone lactylation // Eur. Heart J. 2024. V. 45(37). P. 3871-3885. DOI: 10.1093/eurheartj/ehae407

[38] Park S.J., Ji E., Yoo H.J. et al. Circulating lumican as a potential biomarker for osteosarcopenia in older adults // Bone. 2024. V. 179. P. 116959. DOI: 10.1016/j.bone.2023.116959

[39] Lee Y.S., Park S.J., Lee J.Y. et al. Benefits of lumican on human bone health: clinical evidence using bone marrow aspirates // Korean J. Intern. Med. 2022. V. 37(4). P. 821-829. DOI: 10.3904/kjim.2022.015

[40] Park J., Jung M.J., Chung W.Y. The downregulation of IGFBP3 by TGF-β signaling in oral cancer contributes to the osteoclast differentiation // Biochem. Biophys. Res. Commun. 2021. V. 534. P. 381-386. DOI: 10.1016/j.bbrc.2020.11.073

[41] Wang X., Qiu L., Yang Z. et al. Association between serum iron status and the risk of five bone and joint-related diseases: a Mendelian randomization analysis // Front. Endocrinol. (Lausanne). 2024. V. 15. P. 1364375. DOI: 10.3389/fendo.2024.1364375

[42] Nay K., Koechlin-Ramonatxo C., Rochdi S. et al. Simulated microgravity disturbs iron metabolism and distribution in humans: Lessons from dry immersion, an innovative ground-based human model // FASEB J. 2020. V. 34(11). P. 14920-14929. DOI: 10.1096/fj.202001199RR

[43] O'Leary T.J., Jackson S., Izard R.M. et al. Iron status is associated with tibial structure and vitamin D metabolites in healthy young men // Bone. 2024. V. 186. P. 117145. DOI: 10.1016/j.bone.2024.117145

[44] Yanagihara Y., Inoue K., Saeki N. et al. Zscan10 suppresses osteoclast differentiation by regulating expression of Haptoglobin // Bone. 2019. V. 122. P. 93-100. DOI: 10.1016/j.bone.2019.02.011

[45] Lerner U.H., Fröhlander N. Haptoglobin-stimulated bone resorption in neonatal mouse calvarial bones in vitro // Arthritis Rheum. 1992. V. 35(5). P. 587-591. DOI: 10.1002/art.1780350517

[46] Mizumoto S., Yamada S. The Specific Role of Dermatan Sulfate as an Instructive Glycosaminoglycan in Tissue Development // Int. J. Mol. Sci. 2022. V. 23(13). P. 7485. DOI: 10.3390/ijms23137485

[47] Min H.K., Kim S.H., Lee J.Y. et al. DJ-1 controls T cell differentiation and osteoclastogenesis in rheumatoid arthritis // Sci. Rep. 2022. V. 12(1). P. 12767. DOI: 10.1038/s41598-022-16285-1

[48] Chen J., Ikeda S.I., Yang Y. et al. Scleral remodeling during myopia development in mice eyes: a potential role of thrombospondin-1 // Mol. Med. 2024. V. 30(1). P. 25. DOI: 10.1186/s10020-024-00795-x

[49] Amend S.R., Uluckan O., Hurchla M. et al. Thrombospondin-1 regulates bone homeostasis through effects on bone matrix integrity and nitric oxide signaling in osteoclasts // J. Bone Miner. Res. 2015. V. 30(1). P. 106-115. DOI: 10.1002/jbmr.2308

[50] Shi D., Liu X., Li X. et al. Yth m6A RNA-Binding Protein 1 Regulates Osteogenesis of MC3T3-E1 Cells under Hypoxia via Translational Control of Thrombospondin-1 // Int. J. Mol. Sci. 2023. V. 24(2). P. 1741. DOI: 10.3390/ijms24021741

[51] Liu Z., Yuan X., Liu M. et al. Antimicrobial Peptide Combined with BMP2-Modified Mesenchymal Stem Cells Promotes Calvarial Repair in an Osteolytic Model // Mol. Ther. 2018. V. 26(1). P. 199-207. DOI: 10.1016/j.ymthe.2017.09.011

[52] Li X.S., Zhang J.R., Zhao Y.L. et al. Reduced prealbumin is associated with bone mineral density in women with osteoporosis // Nutrition. 2017. V. 33. P. 338-342. DOI: 10.1016/j.nut.2016.08.002

[53] Nakashima M., Suzuki A., Hashimoto K. et al. Vitronectin regulates osteoclastogenesis and bone remodeling in a mouse model of osteoporosis // Anat. Cell Biol. 2024. V. 57(2). P. 305-315. DOI: 10.5115/acb.23.251

Аннотация

Для цитирования

Похожие статьи