Collagen structure of tendon relates to function.
A tendon is a tough band of fibrous connective tissue that connects muscle to bone, designed to transmit forces and withstand tension during muscle contraction. Tendon may be surrounded by different structures: 1) fibrous sheaths or retinaculae; 2) reflection pulleys; 3) synovial sheaths; 4) peritendon sheaths; 5) tendon bursae. Tendons contain a) few cells, mostly represented by tenoblasts along with endothelial cells and some chondrocytes; b) proteoglycans (PGs), mainly decorin and hyaluronan, and c) collagen, mostly type I. Tendon is a good example of a high ordered extracellular matrix in which collagen molecules assemble into filamentous collagen fibrils (formed by microfibrils) which aggregate to form collagen fibers, the main structural components. It represents a multihierarchical structure as it contains collagen molecules arranged in fibrils then grouped in fibril bundles, fascicles and fiber bundles that are almost parallel to the long axis of the tendon, named as primary, secondary and tertiary bundles. Collagen fibrils in tendons show prevalently large diameter, a D-period of about 67 nm and appear built of collagen molecules lying at a slight angle (< 5 degrees). Under polarized light microscopy the collagen fiber bundles appear crimped with alternative dark and light transverse bands. In recent studies tendon crimps observed via SEM and TEM show that the single collagen fibrils suddenly changing their direction contain knots. These knots of collagen fibrils inside each tendon crimp have been termed "fibrillar crimps", and even if they show different aspects they all may fulfil the same functional role. As integral component of musculoskeletal system, the tendon acts to transmit muscle forces to the skeletal system. There is no complete understanding of the mechanisms in transmitting/absorbing tensional forces within the tendon; however it seems likely that a flattening of tendon crimps may occur at a first stage of tendon stretching. Increasing stretching, other transmission mechanisms such as an interfibrillar coupling via PGs linkages and a molecular gliding within the fibrils structure may be involved.
Franchi
Marco
M
Department of Human Anatomical Sciences and Physiopathology of Locomotor Apparatus, University of Bologna, Bologna, Italy. marco.franchi3@unibo.it
Trirè
Alessandra
A
Quaranta
Marilisa
M
Orsini
Ester
E
Ottani
Victoria
V
D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000502:physiology* / Q000648:ultrastructure; D004548:Elasticity; D005109:Extracellular Matrix / Q000737:chemistry* / Q000502:physiology* / Q000648:ultrastructure; D006801:Humans; D013314:Stress, Mechanical; D013329:Structure-Activity Relationship; D013710:Tendons / Q000737:chemistry* / Q000502:physiology* / Q000648:ultrastructure; D013718:Tensile Strength
D003094:Collagen