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Research Article

Immunolocalization of Collagens (I and III) and Cartilage Oligomeric Matrix Protein in the Normal and Injured Equine Superficial Digital Flexor Tendon

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Pages 62-69 | Received 02 Feb 2012, Accepted 25 Sep 2012, Published online: 03 Dec 2012

References

  • Williams, R.B., Harkins, L.S., Hammond, C.J., and Wood, J.L. (2001). 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. 33:478–486.
  • Nyyssonen, T., and Luthje, P. (2000). Achilles tendon ruptures in South-East Finland between 1986–1996, with special reference to epidemiology, complications of surgery and hospital costs. Ann. Chir. Gynaecol. 89:53–57.
  • Thorpe, C.T., Clegg, P.D., and Birch, H.L. (2010). A review of tendon injury: Why is the equine superficial digital flexor tendon most at risk? Equine Vet. J. 42:174–180.
  • Dyson, S.J. (2004). Medical management of superficial digital flexor tendonitis: A comparative study in 219 horses (1992–2000). Equine Vet. J. 36:415–419.
  • Benjamin, M., and Ralphs, J.R. (1997). Tendon and ligaments—An overview. Histol. Histopathol. 12:1135–1144.
  • Lapiere, C.M., Nusgens, B., and Pierard, G.E. (1977). Interaction between collagen type I and type III in conditioning bundles organization. Connective Tissue Res. 5:21–29.
  • Wang, J.H.-C. (2006). Mechanobiology of tendon—Review. J. Biomechanics. 39:1563–1582.
  • Zhang, G., Young, B.B., Ezura, Y., Favata, M., Soslowsky, L.J., Chakravarti, S., and Birk, D.E. (2005). Development of tendon structure and function: Regulation of collagen fibrillogenesis. J. Musculoskelet. Neuronal. Interact. 5:5–21.
  • Birk, D.E., and Mayne, R. (1997). 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. 72:352–361.
  • Abrahamsson, S.O. (1991). Matrix metabolism and healing in the flexor tendon—Review. Scand. J. Plast. Reconstr. Surg. Handsurg. 23(Suppl.):1–51.
  • Vogel, K.G., Sandy, J.D., Pogány, G., and Robbins, J.R. (1994). Aggrecan in bovine tendon. Matrix Biol. 14:171–179.
  • Svensson, L., Aszódi, A., Reinholt, F.P., Fässler, R., Heinegård, D., and Oldberg, Å. (1999). Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. J. Biol. Chem. 274:9636–9647.
  • Graham, H.K., Holmes, D.F., Watson, R.B., and Kadler, K.E. (1999). 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. 295:891–902.
  • Hedbom, E., Antonsson, P., Hjerpe, A., Aeschlimann, D., Paulsson, M., Rosa-Pimentel, E., Sommarin, Y., Wendel, M., Oldberg, Å., and Heinegård, D. (1992). Cartilage matrix proteins. An acidic oligomeric protein (COMP) detected only in cartilage. J. Biol. Chem. 267:6132–6136.
  • Di Cesare, P., Hauser, N., Lehman, D., Pasumarti, S., and Paulsson, M. (1994). Cartilage oligomeric matrix protein (COMP) is an abundant component of tendon. FEBS Lett. 354:237–240.
  • Mörgelin, M., Heinegård, D., Engel, J., and Electron, P.M. (1992). Microscopy of native cartilage oligomeric matrix protein purified from the swarm rat chondrosarcoma reveals a five-armed structure. J. Biol. Chem. 267:6137–6141.
  • Oldberg, A., Antonsson, P., Lindblom, K., and Heinegård, D. (1992). COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins. J. Biol. Chem. 267:22346–22350.
  • Holden, P., Meadows, R.S., Chapman, K.L., Grant, M.E., Kadler, K.E., and Briggs, M.D. (2001). 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. 276:6046–6055.
  • Rosenberg, K., Olsson, H., Mörgelin, M., and Heinegård, D. (1998).Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen. J. Biol. Chem. 273:20397–20403.
  • Halász, K., Kassner, A., Mörgelin, M., and Heinegård, D. (2007).COMP acts as a catalyst in collagen fibrillogenesis. J. Biol. Chem. 282:31166–31173.
  • Smith, R.K.W., Zunino, L., Webbon, P.M., and Heinegård, D. (1997). The distribution of cartilage oligomeric matrix protein (COMP) in tendon and its variation with tendon site, age and load. Matrix Biol. 16:255–271.
  • Södersten, F., Ekman, S., Eloranta, M.-L., Heinegård, D., Dudhia, J., and Hultenby, K. (2005). Ultrastructural immunolocalization of cartilage oligomeric matris protein (COMP) in relation to collagen fibrils in the equine tendon. Matrix Biol. 24:376–385.
  • Kasashima, Y., Takahashi, T., Birch, H.L., Smith, R.K.W., and Goodship, A.E. (2008).Can exercise modulate the maturation of functionally different immature tendons in the horse? J. Appl. Physiol. 104:416–422.
  • Smith, M.R.W., Wright, I.M., Minshall, G.J., Verheyen, K., Heinegård, D., and Smith, R.K.W. (2011). Increased cartilage oligomeric matrix protein concentrations in equine digital flexor tendon sheath synovial fluid predicts intrathecal tendon damage. Vet. Surg. 40:54–58.
  • Goodship, A.E., Birch, H.L., and Wilson, A.M. (1994). The pathobiology and repair of tendon and ligament injury. Vet Clin. North Am. Equine Pract. 10:323–349.
  • Cetti, R., Junge, J., and Vyberg, M. (2003). 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. 74:78–84.
  • Riley, G. (2008). Tendinopathy – From basic science to treatment. Rheumatology 4:82–89.
  • Wilson, A.M., and Goodship, A.E. (1994). Exercise-induced hyperthermia as a possible mechanism for tendon degeneration. J. Biomechanics. 27:899–905.
  • Smith, R.K.W., Birch, H.L., Goodman, S., Heinegård, D., and Goodship, A.E. (2002). 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. 133:1039–1050.
  • Jones, A.J., and Bee, J.A. (1990). Age- and position-related heterogeneity of equine tendon extracellular matrix composition. Res. Vet. Sci. 48:357–364.
  • Birch, H.L., Bailey, A.J., and Goodship, A.E. (1998). Macroscopic ‘degeneration’ of equine superficial digital flexor tendon is accompanied by a change in extracellular matrix composition. Equine Vet. J. 30:534–539.
  • Birch, H.L., Bailey, J.V.B., Bailey, A.J., and Goodship, A.E. (1999). Age-related changes to the molecular and cellular components of equine flexor tendons. Equine Vet. J. 31:391–396.
  • Cherdchutham, W., Becker, C., Smith, R.K.W., Barneveld, A., and van Weeren, P.R. (1999). Age-related changes and effect of exercise on the molecular composition of immature equine superficial digital flexor tendons. Equine Vet. J. 31(Suppl.):86–94.
  • Cherdchutham, W., Becker, C.K., Spek, E.R., Voorhout, W.F., and van Weeren, P.R. (2001). 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. 62:1563–1570.
  • Dahlgren, L.A., Brower-Toland, B.D., and Nixon, A.J. (2005). Cloning and expression of type III collagen in normal and injured tendons of horses. Am. J. Vet. Res. 66:266–271.
  • Williams, I.F., McCullagh, K.G., and Silver, I.A. (1984). The distribution of types I and III collagen and fibronectin in the healing equine tendon. Connective Tissue Res. 12:211–227.
  • Watkins, J.P., Auer, J.A., Gay, S., and Morgan, S.J. (1985). Healing of surgically created defects in the equine superficial digital flexor tendon: Collagen-type transformation and tissue morphologic reorganization. Am. J. Vet. Res. 46:2091–2096.
  • Nixon, A.J., Dahlgren, L.A., Haupt, J.L., Yeager, A.E., and Ward, D.L. (2008). Effect of adipose-derived nucleated cell fractions on tendon repair in horses with collagenase-induced tendinitis. Am. J. Vet. Res. 69:928–937.
  • Williams, I.F., McCullagh, K.G., Goodship, A.E., and Silver, I.A. (1984). Studies on the pathogenesis of equine tendonitis following collagenase injury. Res. Vet. Sci. 36:326–338.
  • Watts, A.E., Nixon, A.J., Yeager, A.E., and Mohammed, H.O. (2012). A collagenase gel/physical defect model for controlled induction of superficial digital flexor tendonitis. Equine Vet. J. 44:576–386. doi: 10.1111/j.2042-3306.2011.00471.x.
  • Eriksen, H.A., Pajala, A., Leppilahti, J., and Risteli, J. (2002). Increased content of type III collagen at the rupture site of human Achilles tendon. J. Orthop. Res. 20:1352–1357.
  • Jozsa, L., and Kannus, P. (1997). Histopathological findings in spontaneous tendon ruptures. Scand. J. Med. Sci. Sports. 7:113–118.
  • Dahlgren, L.A., Mohammad, H.M., and Nixon, A.J. (2005). Temporal expression of growth factors and matrix molecules in healing tendon lesions. J. Orthop. Res. 23:84–92.
  • Crovace, A., Lacitignola, L., Francioso, E., and Rossi, G. (2008). Histology and immunohistochemistry study of ovine tendon grafted with cBMSCs and BMMNCs after collagenase-induced tendinitis. Vet. Comp. Orthop. Traumatol. 21:329–336.
  • Maffulli, N., Ewen, S.W., Waterston, S.W., Reaper, J., and Barrass, V. (2000). 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. 28:499–505.
  • Farina, G., Lemaire, R., Korn, J.H., and Widom, R.L. (2006). Cartilage oligomeric matrix protein is over expressed by scleroderma dermal fibroblasts. Matrix Biol. 25:213–222.
  • Hesselstrand, R., Kassner, A., Heinegård, D., and Saxne, T. (2008). COMP: A candidate molecule in the pathogenesis of systemic sclerosis with a potential as a disease marker. Ann. Rhem. Dis. 67:1242–1248.
  • Dart, A.J., Dart, C.M., Dudhia, J., Perkins, N., Canfield, P., and Smith, R.K. (2011). 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. 40:59–65.