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Home / Equine Research Bank / Bone Rep / Role of cartilage and bone matrix regulation in early equine...
Bone reports2023; 18; 101653; doi: 10.1016/j.bonr.2023.101653

Role of cartilage and bone matrix regulation in early equine osteochondrosis.

Abstract: The objective of this study is to better understand the pathogenesis of early equine osteochondrosis (OC) by identifying differences in gene and protein expression of extracellular matrix components and regulators in normal and diseased cartilage and bone, focusing on the osteochondral junction and cells surrounding the cartilage canals. We expected to find an upregulation of matrix metalloproteinases and a decrease in extracellular matrix constituent expression along the osteochondral junction and cells surrounding the cartilage canals in OC samples. Paraffin-embedded osteochondral samples (6 OC-affected, 8 normal controls) and cDNA from chondrocytes captured with laser capture microdissection from frozen sections (4 OC-affected, 5 normal controls) were used in this study. Quantitative real-time polymerase chain reaction was performed on 16 target genes. Immunohistochemistry was performed on osteochondral samples for Sox-9, lubricin, osteocalcin, and collagen type IIB. In OC-affected samples, there was significantly ( ≤ 0.05) decreased gene expression of collagen type IIB, aggrecan, and SOX-9 in chondrocytes surrounding the cartilage canals and decreased gene expression of PRG4 (Lubricin) and collagen type IIB in chondrocytes along the osteochondral junction. We found significantly lower collagen type IIB total matrix percentages in the middle and deep cartilage layers, lower lubricin total cellular percentage in the superficial layer, and higher Sox-9 total cellular percentage in bone of OC samples. No significant differences were found in matrix degradation molecules or HSCORE protein expression at any locations between normal and OC-affected samples in our study.
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Publication Date: 2023-01-05 PubMed ID: 36632355PubMed Central: PMC9827356DOI: 10.1016/j.bonr.2023.101653Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research sought to understand the progression of early equine osteochondrosis, a joint condition affecting horses, by studying genetic differences and protein expression in healthy and diseased cartilage and bone. The study expected to find increased levels of matrix metalloproteinases, enzymes instrumental in joint degradation, and reduced expression of extracellular matrix constituents in disease samples.

Research Methodology

  • The researchers utilized paraffin-embedded osteochondral samples from both horses affected by osteochondrosis and healthy horses. They also used cDNA gathered from chondrocytes (the cells that produce and maintain the cartilage matrix). These were obtained using laser capture microdissection from frozen sections.
  • 16 target genes were tested using quantitative real-time polymerase chain reaction, a lab technique used to detect, measure and compare gene expression levels.
  • Immunohistochemistry, a method used to visualize and identify the presence, abundance, and localisation of specific proteins, was performed on osteochondral samples using Sox-9 (a transcription factor, or protein that controls the rate of transcription of DNA to RNA), lubricin (a protein essential for joint lubrication), osteocalcin (a protein found in bone and dentin), and collagen type IIB (a particular type of collagen).

Key Findings

  • The study observed significant decreases in the gene expression of collagen type IIB, aggrecan (a component of cartilage), and SOX-9 in chondrocytes around the cartilage canals in samples affected by osteochondrosis.
  • Similarly, a decrease in gene expression of PRG4 (lubricin) and collagen type IIB was found in chondrocytes along the osteochondral junction. These junctions are areas of bone transition into cartilage.
  • They also observed lower collagen type IIB total matrix percentages in the middle and deep cartilage layers. Simultaneously, there was lower lubricin total cellular percentage in the superficial layer, and an increased Sox-9 total cellular percentage in bone of samples affected by osteochondrosis.
  • Conversely, the study did not find any significant differences in the presence or levels of matrix degradation molecules or HSCORE protein expression between normal and osteochondrosis-affected samples. HSCORE is a semi-quantitative method to measure protein expression.

Conclusion

  • This study highlighted a decrease in certain gene expressions and protein levels in cartilage and bone samples affected by early equine osteochondrosis. These findings indicate potential biomarkers for this disease and provide a deeper understanding of osteochondrosis’s genetic and cellular pathology in horses.

Cite This Article

APA
Grissom SK, Semevolos SA, Duesterdieck-Zellmer K. (2023). Role of cartilage and bone matrix regulation in early equine osteochondrosis. Bone Rep, 18, 101653. https://doi.org/10.1016/j.bonr.2023.101653

Publication

Bone reports
ISSN: 2352-1872
NlmUniqueID: 101646176
Country: United States
Language: English
Volume: 18
Pages: 101653
PII: 101653

Researcher Affiliations

Grissom, S K
  • Department of Clinical Sciences, Carlson College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331, United States of America.
Semevolos, S A
  • Department of Clinical Sciences, Carlson College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331, United States of America.
Duesterdieck-Zellmer, K
  • Department of Clinical Sciences, Carlson College of Veterinary Medicine, Oregon State University, Corvallis, OR 97331, United States of America.

Conflict of Interest Statement

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

References

This article includes 24 references
  1. Brun JL, Cortez A, Lesieur B, Uzan S, Rouzier R, Daraï E. Expression of MMP-2, -7, -9, MT1-MMP and TIMP-1 and -2 has no prognostic relevance in patients with advanced epithelial ovarian cancer.. Oncol Rep 2012 Apr;27(4):1049-57.
    pmc: PMC3583568pubmed: 22200690doi: 10.3892/or.2011.1608google scholar: lookup
  2. Carlson CS, Cullins LD, Meuten DJ. Osteochondrosis of the articular-epiphyseal cartilage complex in young horses: evidence for a defect in cartilage canal blood supply.. Vet Pathol 1995 Nov;32(6):641-7.
    pubmed: 8592799doi: 10.1177/030098589503200605google scholar: lookup
  3. Donabédian M, van Weeren PR, Perona G, Fleurance G, Robert C, Léger S, Bergero D, Lepage O, Martin-Rosset W. Early changes in biomarkers of skeletal metabolism and their association to the occurrence of osteochondrosis (OC) in the horse.. Equine Vet J 2008 May;40(3):253-9.
    pubmed: 18267892doi: 10.2746/042516408x273657google scholar: lookup
  4. van den Hoogen BM, van de Lest CH, van Weeren PR, van Golde LM, Barneveld A. Changes in proteoglycan metabolism in osteochondrotic articular cartilage of growing foals.. Equine Vet J Suppl 1999 Nov;(31):38-44.
    pubmed: 10999659doi: 10.1111/j.2042-3306.1999.tb05312.xgoogle scholar: lookup
  5. Ikeda T, Kawaguchi H, Kamekura S, Ogata N, Mori Y, Nakamura K, Ikegawa S, Chung UI. Distinct roles of Sox5, Sox6, and Sox9 in different stages of chondrogenic differentiation.. J Bone Miner Metab 2005;23(5):337-40.
    pubmed: 16133682doi: 10.1007/s00774-005-0610-ygoogle scholar: lookup
  6. Kinsley MA, Semevolos SA, Duesterdieck-Zellmer KF. Wnt/β-catenin signaling of cartilage canal and osteochondral junction chondrocytes and full thickness cartilage in early equine osteochondrosis.. J Orthop Res 2015 Oct;33(10):1433-8.
    pubmed: 25676127doi: 10.1002/jor.22846google scholar: lookup
  7. Laverty S, Girard C. Pathogenesis of epiphyseal osteochondrosis.. Vet J 2013 Jul;197(1):3-12.
    pubmed: 23647656doi: 10.1016/j.tvjl.2013.03.035google scholar: lookup
  8. Laverty S, Okouneff S, Ionescu M, Reiner A, Pidoux I, Webber C, Rossier Y, Billinghurst RC, Poole AR. Excessive degradation of type II collagen in articular cartilage in equine osteochondrosis.. J Orthop Res 2002 Nov;20(6):1282-9.
    pubmed: 12472241doi: 10.1016/s0736-0266(02)00053-0google scholar: lookup
  9. Lefebvre V, Behringer RR, de Crombrugghe B. L-Sox5, Sox6 and Sox9 control essential steps of the chondrocyte differentiation pathway.. Osteoarthritis Cartilage 2001;9 Suppl A:S69-75.
    pubmed: 11680692doi: 10.1053/joca.2001.0447google scholar: lookup
  10. Olstad K, Ytrehus B, Ekman S, Carlson CS, Dolvik NI. Epiphyseal cartilage canal blood supply to the distal femur of foals.. Equine Vet J 2008 Jul;40(5):433-9.
    pubmed: 18487109doi: 10.2746/042516408x300269google scholar: lookup
  11. Olstad K, Ytrehus B, Ekman S, Carlson CS, Dolvik NI. Early lesions of articular osteochondrosis in the distal femur of foals.. Vet Pathol 2011 Nov;48(6):1165-75.
    pubmed: 21321104doi: 10.1177/0300985811398250google scholar: lookup
  12. Olstad K, Hendrickson EH, Carlson CS, Ekman S, Dolvik NI. Transection of vessels in epiphyseal cartilage canals leads to osteochondrosis and osteochondrosis dissecans in the femoro-patellar joint of foals; a potential model of juvenile osteochondritis dissecans.. Osteoarthritis Cartilage 2013 May;21(5):730-8.
    pubmed: 23428601doi: 10.1016/j.joca.2013.02.005google scholar: lookup
  13. Pool RR. Difficulties in definition of equine osteochondrosis; differentiation of developmental and acquired lesions.. Equine Vet. J. 1993;25:5–12.
  14. Reesink HL, Watts AE, Mohammed HO, Jay GD, Nixon AJ. Lubricin/proteoglycan 4 increases in both experimental and naturally occurring equine osteoarthritis.. Osteoarthritis Cartilage 2017 Jan;25(1):128-137.
    doi: 10.1016/j.joca.2016.07.021pmc: PMC5489058pubmed: 27498214google scholar: lookup
  15. Riddick TL, Duesterdieck-Zellmer K, Semevolos SA. Gene and protein expression of cartilage canal and osteochondral junction chondrocytes and full-thickness cartilage in early equine osteochondrosis.. Vet J 2012 Dec;194(3):319-25.
    pubmed: 22627046doi: 10.1016/j.tvjl.2012.04.023google scholar: lookup
  16. Schatz F, Kayisli UA, Vatandaslar E, Ocak N, Guller S, Abrahams VM, Krikun G, Lockwood CJ. Toll-like receptor 4 expression in decidual cells and interstitial trophoblasts across human pregnancy.. Am J Reprod Immunol 2012 Aug;68(2):146-53.
    pmc: PMC3395732pubmed: 22564191doi: 10.1111/j.1600-0897.2012.01148.xgoogle scholar: lookup
  17. Semevolos SA. Osteochondritis Dissecans Development.. Vet Clin North Am Equine Pract 2017 Aug;33(2):367-378.
    pubmed: 28551287doi: 10.1016/j.cveq.2017.03.009google scholar: lookup
  18. Semevolos SA, Duesterdieck-Zellmer KF, Larson M, Kinsley MA. Expression of pro-apoptotic markers is increased along the osteochondral junction in naturally occurring osteochondrosis.. Bone Rep 2018 Dec;9:19-26.
    pmc: PMC6038796pubmed: 29998174doi: 10.1016/j.bonr.2018.06.003google scholar: lookup
  19. Statham P, Jones E, Jennings LM, Fermor HL. Reproducing the Biomechanical Environment of the Chondrocyte for Cartilage Tissue Engineering.. Tissue Eng Part B Rev 2022 Apr;28(2):405-420.
    doi: 10.1089/ten.TEB.2020.0373pubmed: 33726527google scholar: lookup
  20. Teeple E, Elsaid KA, Jay GD, Zhang L, Badger GJ, Akelman M, Bliss TF, Fleming BC. Effects of supplemental intra-articular lubricin and hyaluronic acid on the progression of posttraumatic arthritis in the anterior cruciate ligament-deficient rat knee.. Am J Sports Med 2011 Jan;39(1):164-72.
    pmc: PMC3010331pubmed: 20855557doi: 10.1177/0363546510378088google scholar: lookup
  21. van de Lest CH, Brama PA, van El B, DeGroot J, van Weeren PR. Extracellular matrix changes in early osteochondrotic defects in foals: a key role for collagen?. Biochim Biophys Acta 2004 Sep 6;1690(1):54-62.
    pubmed: 15337170doi: 10.1016/j.bbadis.2004.05.002google scholar: lookup
  22. van Weeren PR, Barneveld A. The effect of exercise on the distribution and manifestation of osteochondrotic lesions in the Warmblood foal.. Equine Vet J Suppl 1999 Nov;(31):16-25.
    pubmed: 10999656doi: 10.1111/j.2042-3306.1999.tb05309.xgoogle scholar: lookup
  23. Waller KA, Chin KE, Jay GD, Zhang LX, Teeple E, McAllister S, Badger GJ, Schmidt TA, Fleming BC. Intra-articular Recombinant Human Proteoglycan 4 Mitigates Cartilage Damage After Destabilization of the Medial Meniscus in the Yucatan Minipig.. Am J Sports Med 2017 Jun;45(7):1512-1521.
    doi: 10.1177/0363546516686965pmc: PMC5453820pubmed: 28129516google scholar: lookup
  24. Wardale RJ, Duance VC. Characterisation of articular and growth plate cartilage collagens in porcine osteochondrosis.. J Cell Sci 1994 Jan;107 ( Pt 1):47-59.
    pubmed: 8175922doi: 10.1242/jcs.107.1.47google scholar: lookup

Citations

This article has been cited 2 times.
  1. Aparicio Rojas GM, Andrade LJ. Thermal and compositional characterization of chicken, beef, and pork cartilage to establish its lifetime. Heliyon 2023 Apr;9(4):e14853.
    doi: 10.1016/j.heliyon.2023.e14853pubmed: 37064450google scholar: lookup
  2. Yu XF, Teng B, Li JF, Zhang JV, Su Z, Ren PG. Novel Function of Osteocalcin in Chondrocyte Differentiation and Endochondral Ossification Revealed on a CRISPR/Cas9 bglap-bglap2 Deficiency Mouse Model. Int J Mol Sci 2024 Sep 15;25(18).
    doi: 10.3390/ijms25189945pubmed: 39337434google scholar: lookup
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