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Cartilage oligomeric matrix protein (COMP), thrombospondin-4 (TSP-4) and type I and III collagens in tendon

an immunohistochemical and biochemical study

Södersten, Fredrik (2006). Cartilage oligomeric matrix protein (COMP), thrombospondin-4 (TSP-4) and type I and III collagens in tendon. Diss. (sammanfattning/summary) Uppsala : Sveriges lantbruksuniv., Acta Universitatis agriculturae Sueciae, 1652-6880 ; 2006:94
ISBN 91-576-7143-5
[Doctoral thesis]

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Abstract

Injury to digital flexor tendons leading to partial or total rupture is a common cause of lameness in athletic horses. Degeneration to the tendon extracellular matrix (ECM) often precedes rupture and a high cyclic load is most likely an important factor explaining its high incidence in racing horses. Tendon is composed of tenocytes that produce and support an abundant ECM responsible for the physical properties of the tendon. Type I collagen, the most abundant protein in the ECM, forms long fibrils and is oriented along the tensional axis of the tendon. Other matrix molecules include type III collagen, proteoglycans, glycoproteins (COMP and TSP-4). These molecules contribute to the strength of the tendon and are involved in regulating extracellular growth of the collagen fibrils. The ultrastructural distributions of COMP were delineated with high immunolabeling in healthy three-year-old horses. In the same material, collagen fibril size and the relative distribution of thin, medium and thick fibrils were examined and the highest levels of thin fibrils were found in the three-year-old horses. Achilles tendons from rats were analysed and an active-related decrease in COMP immunolabelling was found. The immunolocalization of TSP-4 was clearly elevated in the pericellular compartment. In injured equine tendons, immunolabelling of COMP and type III collagen was present in all repair structures, described as organized and disorganized fibroblastic. TSP-4 was purified from equine tendon and a heterooligomer between COMP and TSP-4 was displayed. This Thesis shows that COMP increases in equine tendons during skeletal maturation and is related to greater amounts of thin fibrils. Furthermore, COMP is present in tendon repair tissue and. these findings indicate a role during repair/remodelling where the fibrils are newly synthesised. The decrease in COMP found in active rat tendons can be caused by activity-induced degradation. The heterooligomers of COMP and TSP-4 and the immunolocalization of TSP-4 indicate a function as an adhesion and/or signal molecule between the cell membrane and the extracellular matrix. These results indicate that COMP is involved in activity and aging processes, in repair processes in combination with type III collagen, and in heterooligomer formation with TSP-4 in equine tendon.

Authors/Creators:Södersten, Fredrik
Title:Cartilage oligomeric matrix protein (COMP), thrombospondin-4 (TSP-4) and type I and III collagens in tendon
Subtitle:an immunohistochemical and biochemical study
Year of publishing :October 2006
Volume:2006:94
Number of Pages:42
Papers/manuscripts:
NumberReferences
ALLI. Södersten, F., Ekman, S., Eloranta, M-L., 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 Biology 24, 376-385 II. Södersten, F., Ekman, S., Schmitz, M., Paulsson, M., Zaucke, F. (2006) Thrombosponding-4 and cartilage oligomeric matrix protein form heterooligomers in equine tendon. Connective Tissue Research 47, 85-91 III. Södersten, F., Ekman, S., Niehoff, A., Zaucke, F., Heinegård, D., Hultenby, K. Ultrastrcutural immunolocalization of Cartilage oligomeric matrix protein (COMP), Thrombospondin-4 (TSP-4) and collagen fibril size in the rodent Achilles tendon in relation to exercise. In manuscript. IV. Södersten, F., Hultenby, K., Heinegård, D., Johnston C., Ekman, S. Immunolocalization of collagens (I and III), and cartilage oligomeric matrix protein (COMP) in normal and injured superficial digital flexor tendon. In manuscript.
Place of Publication:Uppsala
Publisher:Dept of Biomedical Sciences and Veterinary Public Health, Swedish University of Agricultural Sciences
Associated Programs and Other Stakeholders:SLU - Research Areas for the Future > Future Animal Health and Welfare
ISBN for printed version:91-576-7143-5
ISSN:1652-6880
Language:English
Publication Type:Doctoral thesis
Full Text Status:Public
Agrovoc terms:racehorses, rats, tendons, cartilage, collagen, aging, disorders, physical activity, analytical methods, animal morphology
Keywords:Tendon, extracellular matrix, COMP, TSP-4, equine, activity, ageing, type I and III collagen.
URN:NBN:urn:nbn:se:slu:epsilon-1254
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-1254
ID Code:1241
Faculty:VH - Faculty of Veterinary Medicine and Animal Science
Department:(VH) > Dept. of Biomedical Sciences and Veterinary Public Health
Deposited By: Fredrik Södersten
Deposited On:25 Oct 2006 00:00
Metadata Last Modified:02 Dec 2014 10:10

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