Immunolocalization of collagens (I and III) and cartilage oligomeric matrix protein in the normal and injured equine superficial digital flexor tendon.
Abstract: This is a descriptive study of tendon pathology with different structural appearances of repair tissue correlated to immunolocalization of cartilage oligomeric matrix protein (COMP) and type I and III collagens and expression of COMP mRNA. The material consists of nine tendons from seven horses (5-25 years old; mean age of 10 years) with clinical tendinopathy and three normal tendons from horses (3, 3, and 13 years old) euthanized for non-orthopedic reasons. The injured tendons displayed different repair-tissue appearances with organized and disorganized fibroblastic regions as well as areas of necrosis. The normal tendons presented distinct immunoreactivity for COMP and expression of COMP mRNA and type I collagen in the normal aligned fiber structures, but no immunolabeling of type III collagen. However, immunoreactivity for type III collagen was present in the endotenon surrounding the fiber bundles, where no expression of COMP could be seen. Immunostaining for type I and III collagens was present in all of the pathologic regions indicating repair tissue. Interestingly, the granulation tissues showed immunostaining for COMP and expression of COMP mRNA, indicating a role for COMP in repair and remodeling of the tendon after fiber degeneration and rupture. The present results suggest that not only type III collagen but also COMP is involved in the repair and remodeling processes of the tendon.
Publication Date: 2012-12-03 PubMed ID: 23020676PubMed Central: PMC3545546DOI: 10.3109/03008207.2012.734879Google 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
- Research Support
- Non-U.S. Gov't
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 looks at the structural changes in the tendons of horses with tendinopathy, a type of tendon injury, by analyzing the location and expression levels of certain proteins and collagens. The findings suggest that cartilage oligomeric matrix protein (COMP) and type I and III collagens play important roles in tendon repair and remodeling processes.
Research Context
- The focus of this study is on equine superficial digital flexor tendon, which is a common site for tendon injuries in horses. These injuries often lead to tendinopathy – a condition resulting in pain, swelling, and impaired function.
- The researchers looked into the spatial distribution (immunolocalization) of cartilage oligomeric matrix protein (COMP) and type I and III collagens in the equine tendons.
- The study utilized tendons from ten horses; seven with clinical tendinopathy and three healthy horses. This provided a comparison between normal and injured tendon tissue.
Findings of the Study
- The injured tendons showed areas of organized and disorganized fibroblastic activity and even areas of necrosis (cell death).
- In the normal tendons, COMP and type I collagen were present in healthy fiber structures, but type III collagen was absent. However, type III collagen was found in the endotenon – a sheath surrounding the bundles of tendon muscle fibers.
- Interestingly, both type I and III collagens were present in all pathological regions of the tendon, suggesting their role in the repair process.
- Notably, the granulation tissues – new connective tissues that form on the surfaces of wounds during the healing process – showed COMP and COMP mRNA expression. This finding suggests that COMP also has a role in tendon repair and remodeling after an injury.
Implications of the Study
- The findings provide insight into the possible mechanisms of tendon repair in horses, which may be utilized for developing more effective treatments for tendinopathy.
- The study suggested that type I and III collagens, as well as COMP, are involved in tendon repair and remodeling after damage. This challenges the earlier perception that only type III collagen is involved in tendon repair.
- With further research, these findings could eventually be translated to human medicine, as tendinopathies are common injuries in many sports and occupations.
Cite This Article
APA
Södersten F, Hultenby K, Heinegård D, Johnston C, Ekman S.
(2012).
Immunolocalization of collagens (I and III) and cartilage oligomeric matrix protein in the normal and injured equine superficial digital flexor tendon.
Connect Tissue Res, 54(1), 62-69.
https://doi.org/10.3109/03008207.2012.734879 Publication
Researcher Affiliations
- Division of Pathology, Pharmacology and Toxicology, Department of Biomedicine & Veterinary Public Health, Swedish University of Agricultural Sciences (SLU), Uppsala, Sweden. fredrik.sodersten@slu.se
MeSH Terms
- Animals
- Collagen Type I / analysis
- Collagen Type I / genetics
- Collagen Type I / metabolism
- Collagen Type II / analysis
- Collagen Type II / genetics
- Collagen Type II / metabolism
- Extracellular Matrix Proteins / analysis
- Extracellular Matrix Proteins / metabolism
- Gene Expression
- Glycoproteins / analysis
- Glycoproteins / metabolism
- Horse Diseases / metabolism
- Horse Diseases / pathology
- Horses
- Matrilin Proteins
- RNA, Messenger / metabolism
- Tendon Injuries / metabolism
- Tendon Injuries / pathology
- Tendon Injuries / veterinary
- Tendons / metabolism
References
This article includes 48 references
- Williams R.B., Harkins L.S., Hammond C.J., Wood J.L.. Racehorse injuries, clinical problems and fatalities recorded on British racecourses from flat racing and National Hunt racing during 1996, 1997 and 1998.. Equine Vet. J. 2001;33:478–486.
- Nyyssonen T., Luthje P.. Achilles tendon ruptures in South-East Finland between 1986–1996, with special reference to epidemiology, complications of surgery and hospital costs.. Ann. Chir. Gynaecol. 2000;89:53–57.
- Thorpe C.T., Clegg P.D., Birch H.L.. A review of tendon injury: Why is the equine superficial digital flexor tendon most at risk?. Equine Vet. J. 2010;42:174–180.
- Dyson S.J.. Medical management of superficial digital flexor tendonitis: A comparative study in 219 horses (1992–2000.. Equine Vet. J. 2004;36:415–419.
- Benjamin M., Ralphs J.R.. Tendon and ligaments—An overview.. Histol. Histopathol. 1997;12:1135–1144.
- Lapiere C.M., Nusgens B., Pierard G.E.. Interaction between collagen type I and type III in conditioning bundles organization.. Connective Tissue Res. 1977;5:21–29.
- Wang J.H.-C.. Mechanobiology of tendon—Review.. J. Biomechanics. 2006;39:1563–1582.
- Zhang G., Young B.B., Ezura Y., Favata M., Soslowsky L.J., Chakravarti S., Birk D.E.. Development of tendon structure and function: Regulation of collagen fibrillogenesis.. J. Musculoskelet. Neuronal. Interact. 2005;5:5–21.
- Birk D.E., Mayne R.. Localization of collagen types I, III and V during tendon development. Changes in collagen types I and III are correlated with changes in fibril diameter.. Eur. J. Cell Biol. 1997;72:352–361.
- Abrahamsson S.O.. Matrix metabolism and healing in the flexor tendon—Review.. Scand. J. Plast. Reconstr. Surg. Handsurg. 1991;23(Suppl.):1–51.
- Vogel K.G., Sandy J.D., Pogány G., Robbins J.R.. Aggrecan in bovine tendon.. Matrix Biol. 1994;14:171–179.
- Svensson L., Aszódi A., Reinholt F.P., Fässler R., Heinegård D., Oldberg Å.. Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon.. J. Biol. Chem. 1999;274:9636–9647.
- Graham H.K., Holmes D.F., Watson R.B., Kadler K.E.. Identification of Collagen fibril fusion during vertebrate tendon morphogenesis. The process relies on unipolar fibrils and is regulated by collagen-proteoglycan interaction.. J. Mol. Biol. 1999;295:891–902.
- Hedbom E., Antonsson P., Hjerpe A., Aeschlimann D., Paulsson M., Rosa-Pimentel E., Sommarin Y., Wendel M., Oldberg Å., Heinegård D.. Cartilage matrix proteins. An acidic oligomeric protein (COMP) detected only in cartilage.. J. Biol. Chem. 1992;267:6132–6136.
- Di Cesare P., Hauser N., Lehman D., Pasumarti S., Paulsson M.. Cartilage oligomeric matrix protein (COMP) is an abundant component of tendon.. FEBS Lett. 1994;354:237–240.
- Mörgelin M., Heinegård D., Engel J., Electron P.M.. Microscopy of native cartilage oligomeric matrix protein purified from the swarm rat chondrosarcoma reveals a five-armed structure.. J. Biol. Chem. 1992;267:6137–6141.
- Oldberg A., Antonsson P., Lindblom K., Heinegård D.. COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins.. J. Biol. Chem. 1992;267:22346–22350.
- Holden P., Meadows R.S., Chapman K.L., Grant M.E., Kadler K.E., Briggs M.D.. Cartilage oligomeric matrix protein interacts with type IX collagen, and disruptions to these interactions identify a pathogenetic mechanism in a bone dysplasia family.. J. Biol. Chem. 2001;276:6046–6055.
- Rosenberg K., Olsson H., Mörgelin M., Heinegård D.. Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen.. J. Biol. Chem. 1998;273:20397–20403.
- Halász K., Kassner A., Mörgelin M., Heinegård D.. COMP acts as a catalyst in collagen fibrillogenesis.. J. Biol. Chem. 2007;282:31166–31173.
- Smith R.K.W., Zunino L., Webbon P.M., Heinegård D.. The distribution of cartilage oligomeric matrix protein (COMP) in tendon and its variation with tendon site, age and load.. Matrix Biol. 1997;16:255–271.
- Södersten F., Ekman S., Eloranta M.-L., Heinegård D., Dudhia J., Hultenby K.. Ultrastructural immunolocalization of cartilage oligomeric matris protein (COMP) in relation to collagen fibrils in the equine tendon.. Matrix Biol. 2005;24:376–385.
- Kasashima Y., Takahashi T., Birch H.L., Smith R.K.W., Goodship A.E.. Can exercise modulate the maturation of functionally different immature tendons in the horse?. J. Appl. Physiol. 2008;104:416–422.
- Smith M.R.W., Wright I.M., Minshall G.J., Verheyen K., Heinegård D., Smith R.K.W.. Increased cartilage oligomeric matrix protein concentrations in equine digital flexor tendon sheath synovial fluid predicts intrathecal tendon damage.. Vet. Surg. 2011;40:54–58.
- Goodship A.E., Birch H.L., Wilson A.M.. The pathobiology and repair of tendon and ligament injury.. Vet Clin. North Am. Equine Pract. 1994;10:323–349.
- Cetti R., Junge J., Vyberg M.. Spontaneous rupture of the Achilles tendon is preceded by widespread and bilateral tendon damage and ipsilateral inflammation: A clinical and histopathologic study of 60 patients.. Acta Orthop. Scand. 2003;74:78–84.
- Riley G.. Tendinopathy – From basic science to treatment.. Rheumatology. 2008;4:82–89.
- Wilson A.M., Goodship A.E.. Exercise-induced hyperthermia as a possible mechanism for tendon degeneration.. J. Biomechanics. 1994;27:899–905.
- Smith R.K.W., Birch H.L., Goodman S., Heinegård D., Goodship A.E.. The influence of ageing and exercise on tendon growth and degeneration—Hypotheses for the initiation and prevention of strain-induced tendinopathies.. Comp. Biochem. Physiol. A Mol. Intergr. Physiol. 2002;133:1039–1050.
- Jones A.J., Bee J.A.. Age- and position-related heterogeneity of equine tendon extracellular matrix composition.. Res. Vet. Sci. 1990;48:357–364.
- Birch H.L., Bailey A.J., Goodship A.E.. Macroscopic ‘degeneration’ of equine superficial digital flexor tendon is accompanied by a change in extracellular matrix composition.. Equine Vet. J. 1998;30:534–539.
- Birch H.L., Bailey J.V.B., Bailey A.J., Goodship A.E.. Age-related changes to the molecular and cellular components of equine flexor tendons.. Equine Vet. J. 1999;31:391–396.
- Cherdchutham W., Becker C., Smith R.K.W., Barneveld A., van Weeren P.R.. Age-related changes and effect of exercise on the molecular composition of immature equine superficial digital flexor tendons.. Equine Vet. J. 1999;31(Suppl.):86–94.
- Cherdchutham W., Becker C.K., Spek E.R., Voorhout W.F., van Weeren P.R.. Effects of exercise on the diameter of collagen fibrils in the central core and periphery of the superficial digital flexor tendon in foals.. Am. J. Vet. Res. 2001;62:1563–1570.
- Dahlgren L.A., Brower-Toland B.D., Nixon A.J.. Cloning and expression of type III collagen in normal and injured tendons of horses.. Am. J. Vet. Res. 2005;66:266–271.
- Williams I.F., McCullagh K.G., Silver I.A.. The distribution of types I and III collagen and fibronectin in the healing equine tendon.. Connective Tissue Res. 1984;12:211–227.
- Watkins J.P., Auer J.A., Gay S., Morgan S.J.. Healing of surgically created defects in the equine superficial digital flexor tendon: Collagen-type transformation and tissue morphologic reorganization.. Am. J. Vet. Res. 1985;46:2091–2096.
- Nixon A.J., Dahlgren L.A., Haupt J.L., Yeager A.E., Ward D.L.. Effect of adipose-derived nucleated cell fractions on tendon repair in horses with collagenase-induced tendinitis.. Am. J. Vet. Res. 2008;69:928–937.
- Williams I.F., McCullagh K.G., Goodship A.E., Silver I.A.. Studies on the pathogenesis of equine tendonitis following collagenase injury.. Res. Vet. Sci. 1984;36:326–338.
- Watts A.E., Nixon A.J., Yeager A.E., Mohammed H.O.. A collagenase gel/physical defect model for controlled induction of superficial digital flexor tendonitis.. Equine Vet. J. 2012;44:576–386.
- Eriksen H.A., Pajala A., Leppilahti J., Risteli J.. Increased content of type III collagen at the rupture site of human Achilles tendon.. J. Orthop. Res. 2002;20:1352–1357.
- Jozsa L., Kannus P.. Histopathological findings in spontaneous tendon ruptures.. Scand. J. Med. Sci. Sports. 1997;7:113–118.
- Dahlgren L.A., Mohammad H.M., Nixon A.J.. Temporal expression of growth factors and matrix molecules in healing tendon lesions.. J. Orthop. Res. 2005;23:84–92.
- Crovace A., Lacitignola L., Francioso E., Rossi G.. Histology and immunohistochemistry study of ovine tendon grafted with cBMSCs and BMMNCs after collagenase-induced tendinitis.. Vet. Comp. Orthop. Traumatol. 2008;21:329–336.
- Maffulli N., Ewen S.W., Waterston S.W., Reaper J., Barrass V.. Tenocytes from ruptured and tendinopathic achilles tendons produce greater quantities of type III collagen than tenocytes from normal achilles tendons. An in vitro model of human tendon healing.. Am. J. Sports Med. 2000;28:499–505.
- Farina G., Lemaire R., Korn J.H., Widom R.L.. Cartilage oligomeric matrix protein is over expressed by scleroderma dermal fibroblasts.. Matrix Biol. 2006;25:213–222.
- Hesselstrand R., Kassner A., Heinegård D., Saxne T.. COMP: A candidate molecule in the pathogenesis of systemic sclerosis with a potential as a disease marker.. Ann. Rhem. Dis. 2008;67:1242–1248.
- Dart A.J., Dart C.M., Dudhia J., Perkins N., Canfield P., Smith R.K.. A preliminary study on the effect of wounding on transforming growth factor-β1 and cartilage oligomeric matrix protein concentrations in the skin of horses.. Vet. Surg. 2011;40:59–65.
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