Kas İskelet Sistemi Hastalıklarında Biyobelirteçler
Özet
Kas-iskelet sistemi hastalıklarında biyobelirteçlerin tanı, prognoz ve tedavi takibindeki kritik rollerini ele aldığımız bu bölümde ekstraselüler matriks (ECM) metabolitleri, inflamatuar sitokinler/kemokinler ve ağrıyla ilişkili nöropeptitler olmak üzere biyobelirteçler üç ana başlıkta toplanmıştır. Kas-iskelet sistemi hastalıkları, dünya genelinde milyonlarca insanı etkileyen ve yaşam kalitesini ciddi şekilde düşüren rahatsızlıklardır. Bu hastalıkların patofizyolojisinin karmaşıklığı, biyobelirteçlerin erken tanı ve hastalık ilerleyişinin izlenmesinde kullanılmalarını giderek daha önemli hale getirmektedir. ECM bileşenleri olan kollajenler, proteoglikanlar ve glikozaminoglikanlar, dokuların yapısal bütünlüğünün korunmasında ve hastalık süreçlerinde merkezi bir rol oynamaktadır. İnflamatuar sitokinler ve kemokinler, özellikle romatoid artrit (RA) ve osteoartrit (OA) gibi dejeneratif hastalıklarda inflamasyon ve doku yıkımına katkıda bulunur. Ağrıyla ilişkili nöropeptitler ise bu hastalıkların neden olduğu kronik ağrının gelişiminde önemli bir rol oynar. Çalışmada ayrıca, biyobelirteçlerin tedavi hedeflerinin belirlenmesine ve tedavi etkinliğinin izlenmesine olanak tanıyarak kişiselleştirilmiş tıbbın gelişimine katkıda bulunabileceği vurgulanmıştır.
In this chapter, in which we discuss the crucial role of biomarkers in the diagnosis, prognosis and treatment monitoring of musculoskeletal disorders, biomarkers are summarised under three main headings: Extracellular Matrix Metabolites (ECM), Inflammatory Cytokines/Chemokines and Pain- Related Neuropeptides. Musculoskeletal disorders are diseases that affect millions of people worldwide and have a major impact on quality of life. The complexity of the pathophysiology of these diseases makes the use of biomarkers for early diagnosis and monitoring of disease progression increasingly important. The ECM components collagens, proteoglycans and glycosaminoglycans play a central role in maintaining the structural integrity of tissues and in disease processes. Inflammatory cytokines and chemokines contribute to inflammation and tissue destruction, particularly in degenerative diseases such as rheumatoid arthritis (RA) and osteoarthritis (OA). Pain-related neuropeptides play an important role in the development of chronic pain caused by these diseases. The study also highlights that biomarkers can contribute to the development of personalized medicine by enabling the identification of treatment targets and the monitoring of treatment efficacy.
Referanslar
Jin Z, Wang D, Zhang H, Liang J, Feng X, Zhao J, et al. Incidence trend of five common musculoskeletal disorders from 1990 to 2017 at the global, regional and national level: results from the global burden of disease study 2017. Ann Rheum Dis. 2020;79(8):1014-22.
Poole AR. Biochemical/immunochemical biomarkers of osteoarthritis: utility for prediction of incident or progressive osteoarthritis. Rheum Dis Clin North Am. 2003;29(4):803-18.
Huang W, Sowa G. Biomarker development for musculoskeletal diseases. PM&R. 2011;3(6):S39-S44.
Jayabalan P, Sowa GA. The development of biomarkers for degenerative musculoskeletal conditions. Discov Med. 2014;17(92):59-66.
Halper J, Kjaer M. Basic components of connective tissues and extracellular matrix: elastin, fibrillin, fibulins, fibrinogen, fibronectin, laminin, tenascins and thrombospondins. Adv Exp Med Biol. 2014;802:31-47.
Theocharis AD, Manou D, Karamanos NK. The extracellular matrix as a multitasking player in disease. Febs j. 2019;286(15):2830-69.
Kadler KE, Baldock C, Bella J, Boot-Handford RP. Collagens at a glance. J Cell Sci. 2007;120(Pt 12):1955-8.
Arseni L, Lombardi A, Orioli D. From Structure to Phenotype: Impact of Collagen Alterations on Human Health. Int J Mol Sci. 2018;19(5).
Ouyang Z, Dong L, Yao F, Wang K, Chen Y, Li S, et al. Cartilage-Related Collagens in Osteoarthritis and Rheumatoid Arthritis: From Pathogenesis to Therapeutics. Int J Mol Sci. 2023;24(12).
Henriksen K, Karsdal M. Type I collagen. Biochemistry of collagens, laminins and elastin: Elsevier; 2024. p. 1-11.
Chubb SP. Measurement of C-terminal telopeptide of type I collagen (CTX) in serum. Clinical biochemistry. 2012;45(12):928-35.
Szulc P, Naylor K, Hoyle NR, Eastell R, Leary ET. Use of CTX-I and PINP as bone turnover markers: National Bone Health Alliance recommendations to standardize sample handling and patient preparation to reduce pre-analytical variability. Osteoporos Int. 2017;28(9):2541-56.
Nagy EE, Nagy-Finna C, Popoviciu H, Kovács B. Soluble Biomarkers of Osteoporosis and Osteoarthritis, from Pathway Mapping to Clinical Trials: An Update. Clin Interv Aging. 2020;15:501-18.
Vallet S, Hoyle NR, Kyle RA, Podar K, Pecherstorfer M. A role for bone turnover markers β-CrossLaps (CTX) and amino-terminal propeptide of type I collagen (PINP) as potential indicators for disease progression from MGUS to multiple myeloma. Leuk Lymphoma. 2018;59(10):2431-8.
Sophia Fox AJ, Bedi A, Rodeo SA. The basic science of articular cartilage: structure, composition, and function. Sports Health. 2009;1(6):461-8.
Nguyen LT, Sharma AR, Chakraborty C, Saibaba B, Ahn ME, Lee SS. Review of Prospects of Biological Fluid Biomarkers in Osteoarthritis. Int J Mol Sci. 2017;18(3).
Bancroft JD, Layton C. Connective and other mesenchymal tissues with their stains. Bancroft’s theory and practice of histological techniques. 2018:153-75.
Singh D, Rai V, Agrawal DK. Regulation of Collagen I and Collagen III in Tissue Injury and Regeneration. Cardiol Cardiovasc Med. 2023;7(1):5-16.
Berry SD, Ramachandran VS, Cawthon PM, Gona P, McLean RR, Cupples LA, et al. Procollagen type III N-terminal peptide (P3NP) and lean mass: a cross-sectional study. J Frailty Aging. 2013;2(3):129-34.
Schaefer L, Schaefer RM. Proteoglycans: from structural compounds to signaling molecules. Cell Tissue Res. 2010;339(1):237-46.
Hurysz B, Bottini N. Emerging proteoglycans and proteoglycan-targeted therapies in rheumatoid arthritis. Am J Physiol Cell Physiol. 2022;322(6):C1061-c7.
Kiani C, Chen L, Wu YJ, Yee AJ, Yang BB. Structure and function of aggrecan. Cell Research. 2002;12(1):19-32.
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Farach-Carson MC, Carson DD. Perlecan--a multifunctional extracellular proteoglycan scaffold. Glycobiology. 2007;17(9):897-905.
Gracey E, Burssens A, Cambré I, Schett G, Lories R, McInnes IB, et al. Tendon and ligament mechanical loading in the pathogenesis of inflammatory arthritis. Nat Rev Rheumatol. 2020;16(4):193-207.
Pomin VH, Mulloy B. Glycosaminoglycans and Proteoglycans. Pharmaceuticals. 2018;11(1):27.
Sodhi H, Panitch A. Glycosaminoglycans in Tissue Engineering: A Review. Biomolecules. 2020;11(1).
Marinho A, Nunes C, Reis S. Hyaluronic Acid: A Key Ingredient in the Therapy of Inflammation. Biomolecules. 2021;11(10).
Migliore A, Procopio S. Effectiveness and utility of hyaluronic acid in osteoarthritis. Clin Cases Miner Bone Metab. 2015;12(1):31-3.
Jerosch J. Effects of Glucosamine and Chondroitin Sulfate on Cartilage Metabolism in OA: Outlook on Other Nutrient Partners Especially Omega-3 Fatty Acids. Int J Rheumatol. 2011;2011:969012.
Trowbridge JM, Gallo RL. Dermatan sulfate: new functions from an old glycosaminoglycan. Glycobiology. 2002;12(9):117r-25r.
Caterson B, Melrose J. Keratan sulfate, a complex glycosaminoglycan with unique functional capability. Glycobiology. 2018;28(4):182-206.
Sarrazin S, Lamanna WC, Esko JD. Heparan sulfate proteoglycans. Cold Spring Harb Perspect Biol. 2011;3(7).
Matsuzaka Y, Yashiro R. Classification and Molecular Functions of Heparan Sulfate Proteoglycans and Their Molecular Mechanisms with the Receptor. Biologics. 2024;4(2):105-29.
Varki A, Cummings R, Esko J, Freeze H, Hart G, Marth J. Proteoglycans and glycosaminoglycans. Essentials of glycobiology: Cold Spring Harbor Laboratory Press; 1999.
Kjaer M. Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol Rev. 2004;84(2):649-98.
Anborgh PH, Mutrie JC, Tuck AB, Chambers AF. Role of the metastasis-promoting protein osteopontin in the tumour microenvironment. J Cell Mol Med. 2010;14(8):2037-44.
Rangaswami H, Bulbule A, Kundu GC. Osteopontin: role in cell signaling and cancer progression. Trends Cell Biol. 2006;16(2):79-87.
Bai RJ, Li YS, Zhang FJ. Osteopontin, a bridge links osteoarthritis and osteoporosis. Front Endocrinol (Lausanne). 2022;13:1012508.
Gravallese EM. Osteopontin: a bridge between bone and the immune system. J Clin Invest. 2003;112(2):147-9.
Dakin SG, Buckley CD, Al-Mossawi MH, Hedley R, Martinez FO, Wheway K, et al. Persistent stromal fibroblast activation is present in chronic tendinopathy. Arthritis Res Ther. 2017;19(1):16.
Du Y, Mao L, Wang Z, Yan K, Zhang L, Zou J. Osteopontin - The stirring multifunctional regulatory factor in multisystem aging. Front Endocrinol (Lausanne). 2022;13:1014853.
Lee HJ, Tomasini-Johansson BR, Gupta N, Kwon GS. Fibronectin-targeted FUD and PEGylated FUD peptides for fibrotic diseases. J Control Release. 2023;360:69-81.
Pérez-García S, Carrión M, Gutiérrez-Cañas I, Villanueva-Romero R, Castro D, Martínez C, et al. Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin. Cells. 2019;9(1).
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Referanslar
Jin Z, Wang D, Zhang H, Liang J, Feng X, Zhao J, et al. Incidence trend of five common musculoskeletal disorders from 1990 to 2017 at the global, regional and national level: results from the global burden of disease study 2017. Ann Rheum Dis. 2020;79(8):1014-22.
Poole AR. Biochemical/immunochemical biomarkers of osteoarthritis: utility for prediction of incident or progressive osteoarthritis. Rheum Dis Clin North Am. 2003;29(4):803-18.
Huang W, Sowa G. Biomarker development for musculoskeletal diseases. PM&R. 2011;3(6):S39-S44.
Jayabalan P, Sowa GA. The development of biomarkers for degenerative musculoskeletal conditions. Discov Med. 2014;17(92):59-66.
Halper J, Kjaer M. Basic components of connective tissues and extracellular matrix: elastin, fibrillin, fibulins, fibrinogen, fibronectin, laminin, tenascins and thrombospondins. Adv Exp Med Biol. 2014;802:31-47.
Theocharis AD, Manou D, Karamanos NK. The extracellular matrix as a multitasking player in disease. Febs j. 2019;286(15):2830-69.
Kadler KE, Baldock C, Bella J, Boot-Handford RP. Collagens at a glance. J Cell Sci. 2007;120(Pt 12):1955-8.
Arseni L, Lombardi A, Orioli D. From Structure to Phenotype: Impact of Collagen Alterations on Human Health. Int J Mol Sci. 2018;19(5).
Ouyang Z, Dong L, Yao F, Wang K, Chen Y, Li S, et al. Cartilage-Related Collagens in Osteoarthritis and Rheumatoid Arthritis: From Pathogenesis to Therapeutics. Int J Mol Sci. 2023;24(12).
Henriksen K, Karsdal M. Type I collagen. Biochemistry of collagens, laminins and elastin: Elsevier; 2024. p. 1-11.
Chubb SP. Measurement of C-terminal telopeptide of type I collagen (CTX) in serum. Clinical biochemistry. 2012;45(12):928-35.
Szulc P, Naylor K, Hoyle NR, Eastell R, Leary ET. Use of CTX-I and PINP as bone turnover markers: National Bone Health Alliance recommendations to standardize sample handling and patient preparation to reduce pre-analytical variability. Osteoporos Int. 2017;28(9):2541-56.
Nagy EE, Nagy-Finna C, Popoviciu H, Kovács B. Soluble Biomarkers of Osteoporosis and Osteoarthritis, from Pathway Mapping to Clinical Trials: An Update. Clin Interv Aging. 2020;15:501-18.
Vallet S, Hoyle NR, Kyle RA, Podar K, Pecherstorfer M. A role for bone turnover markers β-CrossLaps (CTX) and amino-terminal propeptide of type I collagen (PINP) as potential indicators for disease progression from MGUS to multiple myeloma. Leuk Lymphoma. 2018;59(10):2431-8.
Sophia Fox AJ, Bedi A, Rodeo SA. The basic science of articular cartilage: structure, composition, and function. Sports Health. 2009;1(6):461-8.
Nguyen LT, Sharma AR, Chakraborty C, Saibaba B, Ahn ME, Lee SS. Review of Prospects of Biological Fluid Biomarkers in Osteoarthritis. Int J Mol Sci. 2017;18(3).
Bancroft JD, Layton C. Connective and other mesenchymal tissues with their stains. Bancroft’s theory and practice of histological techniques. 2018:153-75.
Singh D, Rai V, Agrawal DK. Regulation of Collagen I and Collagen III in Tissue Injury and Regeneration. Cardiol Cardiovasc Med. 2023;7(1):5-16.
Berry SD, Ramachandran VS, Cawthon PM, Gona P, McLean RR, Cupples LA, et al. Procollagen type III N-terminal peptide (P3NP) and lean mass: a cross-sectional study. J Frailty Aging. 2013;2(3):129-34.
Schaefer L, Schaefer RM. Proteoglycans: from structural compounds to signaling molecules. Cell Tissue Res. 2010;339(1):237-46.
Hurysz B, Bottini N. Emerging proteoglycans and proteoglycan-targeted therapies in rheumatoid arthritis. Am J Physiol Cell Physiol. 2022;322(6):C1061-c7.
Kiani C, Chen L, Wu YJ, Yee AJ, Yang BB. Structure and function of aggrecan. Cell Research. 2002;12(1):19-32.
Roughley PJ, Mort JS. The role of aggrecan in normal and osteoarthritic cartilage. J Exp Orthop. 2014;1(1):8.
Robinson KA, Sun M, Barnum CE, Weiss SN, Huegel J, Shetye SS, et al. Decorin and biglycan are necessary for maintaining collagen fibril structure, fiber realignment, and mechanical properties of mature tendons. Matrix Biol. 2017;64:81-93.
Farach-Carson MC, Carson DD. Perlecan--a multifunctional extracellular proteoglycan scaffold. Glycobiology. 2007;17(9):897-905.
Gracey E, Burssens A, Cambré I, Schett G, Lories R, McInnes IB, et al. Tendon and ligament mechanical loading in the pathogenesis of inflammatory arthritis. Nat Rev Rheumatol. 2020;16(4):193-207.
Pomin VH, Mulloy B. Glycosaminoglycans and Proteoglycans. Pharmaceuticals. 2018;11(1):27.
Sodhi H, Panitch A. Glycosaminoglycans in Tissue Engineering: A Review. Biomolecules. 2020;11(1).
Marinho A, Nunes C, Reis S. Hyaluronic Acid: A Key Ingredient in the Therapy of Inflammation. Biomolecules. 2021;11(10).
Migliore A, Procopio S. Effectiveness and utility of hyaluronic acid in osteoarthritis. Clin Cases Miner Bone Metab. 2015;12(1):31-3.
Jerosch J. Effects of Glucosamine and Chondroitin Sulfate on Cartilage Metabolism in OA: Outlook on Other Nutrient Partners Especially Omega-3 Fatty Acids. Int J Rheumatol. 2011;2011:969012.
Trowbridge JM, Gallo RL. Dermatan sulfate: new functions from an old glycosaminoglycan. Glycobiology. 2002;12(9):117r-25r.
Caterson B, Melrose J. Keratan sulfate, a complex glycosaminoglycan with unique functional capability. Glycobiology. 2018;28(4):182-206.
Sarrazin S, Lamanna WC, Esko JD. Heparan sulfate proteoglycans. Cold Spring Harb Perspect Biol. 2011;3(7).
Matsuzaka Y, Yashiro R. Classification and Molecular Functions of Heparan Sulfate Proteoglycans and Their Molecular Mechanisms with the Receptor. Biologics. 2024;4(2):105-29.
Varki A, Cummings R, Esko J, Freeze H, Hart G, Marth J. Proteoglycans and glycosaminoglycans. Essentials of glycobiology: Cold Spring Harbor Laboratory Press; 1999.
Kjaer M. Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol Rev. 2004;84(2):649-98.
Anborgh PH, Mutrie JC, Tuck AB, Chambers AF. Role of the metastasis-promoting protein osteopontin in the tumour microenvironment. J Cell Mol Med. 2010;14(8):2037-44.
Rangaswami H, Bulbule A, Kundu GC. Osteopontin: role in cell signaling and cancer progression. Trends Cell Biol. 2006;16(2):79-87.
Bai RJ, Li YS, Zhang FJ. Osteopontin, a bridge links osteoarthritis and osteoporosis. Front Endocrinol (Lausanne). 2022;13:1012508.
Gravallese EM. Osteopontin: a bridge between bone and the immune system. J Clin Invest. 2003;112(2):147-9.
Dakin SG, Buckley CD, Al-Mossawi MH, Hedley R, Martinez FO, Wheway K, et al. Persistent stromal fibroblast activation is present in chronic tendinopathy. Arthritis Res Ther. 2017;19(1):16.
Du Y, Mao L, Wang Z, Yan K, Zhang L, Zou J. Osteopontin - The stirring multifunctional regulatory factor in multisystem aging. Front Endocrinol (Lausanne). 2022;13:1014853.
Lee HJ, Tomasini-Johansson BR, Gupta N, Kwon GS. Fibronectin-targeted FUD and PEGylated FUD peptides for fibrotic diseases. J Control Release. 2023;360:69-81.
Pérez-García S, Carrión M, Gutiérrez-Cañas I, Villanueva-Romero R, Castro D, Martínez C, et al. Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin. Cells. 2019;9(1).
Przybysz M, Borysewicz K, Szechinski J, Katnik-Prastowska I. Synovial fibronectin fragmentation and domain expressions in relation to rheumatoid arthritis progression. Rheumatology (Oxford). 2007;46(7):1071-5.
Iacobini C, Fantauzzi CB, Pugliese G, Menini S. Role of Galectin-3 in Bone Cell Differentiation, Bone Pathophysiology and Vascular Osteogenesis. Int J Mol Sci. 2017;18(11).
Pugliese G, Iacobini C, Pesce CM, Menini S. Galectin-3: an emerging all-out player in metabolic disorders and their complications. Glycobiology. 2015;25(2):136-50.
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