Ultrastructural immunolocalization of cartilage oligomeric matrix protein (COMP) in relation to collagen fibrils in the equine tendon.
Abstract: The structure and organisation of the extracellular matrix, and in particular the axial alignment of type I collagen fibrils, are essential for the tensile strength of tendons. The resident tenocytes synthesize and maintain the composition of the extracellular matrix, which changes with age and maturation. Other components of the extracellular matrix include less abundant collagen types II, III, V, VI, XII, proteoglycans and glycoproteins. Cartilage oligomeric matrix protein (COMP) is an abundant non-collagenous pentameric glycoprotein in the tendon, which can bind to collagen types I and II. The function of COMP in the tendon is not clear, but it may act as a catalyst in fibrillogenesis. Its concentration changes with age, maturation and load. The present study delineates the ultrastructural distribution of COMP and its correlation to collagen fibril thickness in different compartments in two flexor tendons from horses of different ages (foetus, 8 months, 3 years, 12 years). The immunolabeling for COMP was higher in the superficial digital flexor tendon compared with the deep digital flexor tendon and it increased with the age of the animal, with the highest concentration in the 3-year-olds. Fibril diameter differed between age groups and a more homogenous fibril population was found in the fetal tendons. A positive correlation between high COMP immunolabeling and the percentage of small fibrils (<60 nm) were present in the SDFT. COMP immunolabeling was enriched at the gap region of the collagen fibril. In situ hybridization revealed the strongest expression in tendons from the 3-year-old horses whereas there was no expression in foetal tendon.
Publication Date: 2005-07-12 PubMed ID: 16005620DOI: 10.1016/j.matbio.2005.06.003Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
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.
The research examined the distribution and role of cartilage oligomeric matrix protein (COMP) and collagen in the tendons of horses of various ages, finding that the presence of COMP changes with age and location in the tendon, correlating positively with smaller collagen fibrils.
Background of the Study
- The extracellular matrix, a component that provides structural support to cells, plays a pivotal role in maintaining the strength of tendons. A key element of this matrix is Type I collagen fibrils, which align axially.
- Tenocytes, the cells within tendons, synthesize and manage the composition of the extracellular matrix, which evolves over time as the organism matures and ages.
- One of the abundant non-collagenous glycoproteins in the tendons is Cartilage oligomeric matrix protein (COMP). It interacts with types I and II collagen, but the specific role of COMP within tendons remains unclear. Its concentration varies with age, maturation, and load.
Study Approach and Findings
- The research investigated the ultrastructural distribution of COMP, its relationship to collagen fibril thickness, and its variations in different compartments within two types of horse tendons—superficial digital flexor tendon and deep digital flexor tendon—across four age groups: fetus, 8 months, 3 years, and 12 years.
- Findings reveal that COMP distribution differed in terms of location and age. For instance, the superficial digital flexor tendon showed higher levels of immunolabeling for COMP than the deep digital flexor tendon.
- COMP concentration increased with age, peaking in the tendons of 3-year-old horses. However, there was no expression of COMP in the fetus’s tendons, as shown by in situ hybridization.
- Researchers also found variances in fibril diameter across different age groups, with a more uniform population of fibrils found in fetal tendons, and a positive correlation between high COMP immunolabeling and the presence of small fibrils (less than 60 nm).
- Fascinatingly, COMP immunolabeling was enriched at the gap region of the collagen fibril, suggesting a potential link between COMP and the structural organization of the tendon.
Implications and Conclusion
- This study deepens the understanding of the role and distribution of COMP in tendons. By showing its correlation with the size of collagen fibrils and age, the study hints at its potential importance in the maturation and functional development of the tendon.
- The changing presence of COMP in accordance with age and position in the tendon provides new insights for future studies targeting tendon therapeutics and regeneration.
Cite This Article
APA
Södersten F, Ekman S, Eloranta ML, Heinegård D, Dudhia J, Hultenby K.
(2005).
Ultrastructural immunolocalization of cartilage oligomeric matrix protein (COMP) in relation to collagen fibrils in the equine tendon.
Matrix Biol, 24(5), 376-385.
https://doi.org/10.1016/j.matbio.2005.06.003 Publication
Researcher Affiliations
- Department of Biomedicine and Veterinary Public Health, SLU, S-75007 Uppsala, Sweden. fredrik.sodersten@bvf.slu.se
MeSH Terms
- Aging
- Animals
- Collagen Type I / chemistry
- Collagen Type I / immunology
- Collagen Type I / ultrastructure
- Extracellular Matrix Proteins / analysis
- Extracellular Matrix Proteins / genetics
- Extracellular Matrix Proteins / immunology
- Extracellular Matrix Proteins / ultrastructure
- Glycoproteins / analysis
- Glycoproteins / genetics
- Glycoproteins / immunology
- Glycoproteins / ultrastructure
- Horses
- Immunochemistry
- In Situ Hybridization
- Matrilin Proteins
- Microscopy, Electron
- Tendons / cytology
- Tendons / metabolism
- Tendons / ultrastructure
Citations
This article has been cited 18 times.- Wu T, Jin Y, Chen F, Xuan X, Cao J, Liang Y, Wang Y, Zhan J, Zhao M, Huang C. Identification and characterization of bone/cartilage-associated signatures in common fibrotic skin diseases.. Front Genet 2023;14:1121728.
- Eisner LE, Rosario R, Andarawis-Puri N, Arruda EM. The Role of the Non-Collagenous Extracellular Matrix in Tendon and Ligament Mechanical Behavior: A Review.. J Biomech Eng 2022 May 1;144(5).
- Li Y, Wu T, Liu S. Identification and Distinction of Tenocytes and Tendon-Derived Stem Cells.. Front Cell Dev Biol 2021;9:629515.
- Chen H, Wang J, Xie L, Shen YL, Wang HM, Zheng KL, Zhang Q. Correlation between serum cartilage oligomeric matrix protein and major adverse cardiovascular events within 30 days in patients with acute coronary syndrome.. Ann Transl Med 2021 Feb;9(4):353.
- Taye N, Karoulias SZ, Hubmacher D. The "other" 15-40%: The Role of Non-Collagenous Extracellular Matrix Proteins and Minor Collagens in Tendon.. J Orthop Res 2020 Jan;38(1):23-35.
- Posey KL, Coustry F, Hecht JT. Cartilage oligomeric matrix protein: COMPopathies and beyond.. Matrix Biol 2018 Oct;71-72:161-173.
- Coustry F, Posey KL, Maerz T, Baker K, Abraham AM, Ambrose CG, Nobakhti S, Shefelbine SJ, Bi X, Newton M, Gawronski K, Remer L, Veerisetty AC, Hossain MG, Chiu F, Hecht JT. Mutant cartilage oligomeric matrix protein (COMP) compromises bone integrity, joint function and the balance between adipogenesis and osteogenesis.. Matrix Biol 2018 Apr;67:75-89.
- Bastiaansen-Jenniskens YM, de Bart AC, Koevoet W, Jansen KM, Verhaar JA, van Osch GJ, DeGroot J. Elevated Levels of Cartilage Oligomeric Matrix Protein during In Vitro Cartilage Matrix Generation Decrease Collagen Fibril Diameter.. Cartilage 2010 Jul;1(3):200-10.
- Kim DJ, Christofidou ED, Keene DR, Hassan Milde M, Adams JC. Intermolecular interactions of thrombospondins drive their accumulation in extracellular matrix.. Mol Biol Cell 2015 Jul 15;26(14):2640-54.
- Piróg KA, Katakura Y, Mironov A, Briggs MD. Mild myopathy is associated with COMP but not MATN3 mutations in mouse models of genetic skeletal diseases.. PLoS One 2013;8(11):e82412.
- Thorpe CT, Birch HL, Clegg PD, Screen HR. The role of the non-collagenous matrix in tendon function.. Int J Exp Pathol 2013 Aug;94(4):248-59.
- Södersten F, Hultenby K, Heinegård D, Johnston C, Ekman S. Immunolocalization of collagens (I and III) and cartilage oligomeric matrix protein in the normal and injured equine superficial digital flexor tendon.. Connect Tissue Res 2013;54(1):62-9.
- Agarwal P, Zwolanek D, Keene DR, Schulz JN, Blumbach K, Heinegård D, Zaucke F, Paulsson M, Krieg T, Koch M, Eckes B. Collagen XII and XIV, new partners of cartilage oligomeric matrix protein in the skin extracellular matrix suprastructure.. J Biol Chem 2012 Jun 29;287(27):22549-59.
- Crovace A, Lacitignola L, Rossi G, Francioso E. Histological and immunohistochemical evaluation of autologous cultured bone marrow mesenchymal stem cells and bone marrow mononucleated cells in collagenase-induced tendinitis of equine superficial digital flexor tendon.. Vet Med Int 2010;2010:250978.
- Hansson Petersen CA, Alikhani N, Behbahani H, Wiehager B, Pavlov PF, Alafuzoff I, Leinonen V, Ito A, Winblad B, Glaser E, Ankarcrona M. The amyloid beta-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae.. Proc Natl Acad Sci U S A 2008 Sep 2;105(35):13145-50.
- Würgler-Hauri CC, Dourte LM, Baradet TC, Williams GR, Soslowsky LJ. Temporal expression of 8 growth factors in tendon-to-bone healing in a rat supraspinatus model.. J Shoulder Elbow Surg 2007 Sep-Oct;16(5 Suppl):S198-203.
- Piróg-Garcia KA, Meadows RS, Knowles L, Heinegård D, Thornton DJ, Kadler KE, Boot-Handford RP, Briggs MD. Reduced cell proliferation and increased apoptosis are significant pathological mechanisms in a murine model of mild pseudoachondroplasia resulting from a mutation in the C-terminal domain of COMP.. Hum Mol Genet 2007 Sep 1;16(17):2072-88.
- Milz S, Aktas T, Putz R, Benjamin M. Expression of extracellular matrix molecules typical of articular cartilage in the human scapholunate interosseous ligament.. J Anat 2006 Jun;208(6):671-9.
Use Nutrition Calculator
Check if your horse's diet meets their nutrition requirements with our easy-to-use tool Check your horse's diet with our easy-to-use tool
Talk to a Nutritionist
Discuss your horse's feeding plan with our experts over a free phone consultation Discuss your horse's diet over a phone consultation
Submit Diet Evaluation
Get a customized feeding plan for your horse formulated by our equine nutritionists Get a custom feeding plan formulated by our nutritionists
