Research article - Peer-reviewed, 2005
Ultrastructural immunolocalization of cartilage oligomeric matrix protein (COMP) in relation to collagen fibrils in the equine tendon
Sodersten F, Ekman S, Eloranta ML, Heinegard D, Dudhia J, Hultenby KAbstract
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. (C) 2005 Elsevier B.V./International Society of Matrix Biology. All rights reservedKeywords
Tendon; Equine; COMP; Collagen; UltrastructurePublished in
Matrix Biology2005, volume: 24, number: 5, pages: 376-385
Publisher: ELSEVIER SCIENCE BV
Authors' information
Swedish University of Agricultural Sciences, Department of Biomedical Science and Veterinary Public Health
Swedish University of Agricultural Sciences, Department of Biomedical Science and Veterinary Public Health
Eloranta, Maija-Leena
Swedish University of Agricultural Sciences, Department of Molecular Biosciences
Dudhia, J.
Heinegård, D.
Hultenby, K.
SLU - Swedish University of Agricultural Sciences
UKÄ Subject classification
Animal and Dairy Science
Veterinary Science
Publication Identifiers
DOI: https://doi.org/10.1016/j.matbio.2005.06.003
URI (permanent link to this page)
https://res.slu.se/id/publ/7581