Vagina Fibrosa

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For other uses, see Tendon (disambiguation) .
The Achilles tendon , one of the tendons in the human body (from Gray's Anatomy , 1 st ed., 1858)
Micrograph of a piece of tendon; H&E stain


^ Dorlands Medical Dictionary, page 602

^ Caldini, E. G.; Caldini, N.; De-Pasquale, V.; Strocchi, R.; Guizzardi, S.; Ruggeri, A.; Montes, G. S. (1990). "Distribution of elastic system fibres in the rat tail tendon and its associated sheaths". Cells Tissues Organs . 139 (4): 341–348. doi : 10.1159/000147022 . PMID 1706129 .

^ Grant, T. M.; Thompson, M. S.; Urban, J.; Yu, J. (2013). "Elastic fibres are broadly distributed in tendon and highly localized around tenocytes" . Journal of Anatomy . 222 (6): 573–579. doi : 10.1111/joa.12048 . PMC 3666236 . PMID 23587025 .

^ Dorlands Medical Dictionary 2012.Page 1382

^ Jump up to: a b c Jozsa, L., and Kannus, P., Human Tendons: Anatomy, Physiology, and Pathology. Human Kinetics: Champaign, IL, 1997.

^ Lin, T. W.; Cardenas, L.; Soslowsky, L. J. (2004). "Biomechanics of tendon injury and repair". Journal of Biomechanics . 37 (6): 865–877. doi : 10.1016/j.jbiomech.2003.11.005 . PMID 15111074 .

^ Kjær, Michael (April 2004). "Role of Extracellular Matrix in Adaptation of Tendon and Skeletal Muscle to Mechanical Loading". Physiological Reviews . 84 (2): 649–698. doi : 10.1152/physrev.00031.2003 . ISSN 0031-9333 . PMID 15044685 .

^ Taye, Nandaraj; Karoulias, Stylianos Z.; Hubmacher, Dirk (January 2020). "The "other" 15–40%: The Role of Non‐Collagenous Extracellular Matrix Proteins and Minor Collagens in Tendon" . Journal of Orthopaedic Research . 38 (1): 23–35. doi : 10.1002/jor.24440 . ISSN 0736-0266 . PMC 6917864 . PMID 31410892 .

^ Fukuta, S.; Oyama, M.; Kavalkovich, K.; Fu, F. H.; Niyibizi, C. (1998). "Identification of types II, IX and X collagens at the insertion site of the bovine achilles tendon". Matrix Biology . 17 (1): 65–73. doi : 10.1016/S0945-053X(98)90125-1 . PMID 9628253 .

^ Fratzl, P. (2009). "Cellulose and collagen: from fibres to tissues". Current Opinion in Colloid & Interface Science . 8 (1): 32–39. doi : 10.1016/S1359-0294(03)00011-6 .

^ Zhang, G. E., Y.; Chervoneva, I.; Robinson, P. S.; Beason, D. P.; Carine, E. T.; Soslowsky, L. J.; Iozzo, R. V.; Birk, D. E. (2006). "Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development". Journal of Cellular Biochemistry . 98 (6): 1436–1449. doi : 10.1002/jcb.20776 . PMID 16518859 . S2CID 39384363 . CS1 maint: multiple names: authors list ( link )

^ Raspanti, M.; Congiu, T.; Guizzardi, S. (2002). "Structural Aspects of the Extracellular Matrix of the Tendon : An Atomic Force and Scanning Electron Microscopy Study" . Archives of Histology and Cytology . 65 (1): 37–43. doi : 10.1679/aohc.65.37 . PMID 12002609 .

^ Scott, J. E. O., C. R.; Hughes, E. W. (1981). "Proteoglycan-collagen arrangements in developing rat tail tendon. An electron microscopical and biochemical investigation" . Biochemical Journal . 195 (3): 573–581. doi : 10.1042/bj1950573 . PMC 1162928 . PMID 6459082 . CS1 maint: multiple names: authors list ( link )

^ Scott, J. E. (2003). "Elasticity in extracellular matrix 'shape modules' of tendon, cartilage, etc. A sliding proteoglycan-filament model" . Journal of Physiology . 553 (2): 335–343. doi : 10.1113/jphysiol.2003.050179 . PMC 2343561 . PMID 12923209 .

^ McNeilly, C. M.; Banes, A. J.; Benjamin, M.; Ralphs, J. R. (1996). "Tendon cells in vivo form a three dimensional network of cell processes linked by gap junctions" . Journal of Anatomy . 189 (Pt 3): 593–600. PMC 1167702 . PMID 8982835 .

^ "Having a short Achilles tendon may be an athlete's Achilles heel" . Retrieved 2007-10-26 .

^ Young, Michael. "A Review on Postural Realignment and its Muscular and Neural Components" (PDF) .

^ Thorpe C.T., Birch H.L., Clegg P.D., Screen H.R.C. (2013). The role of the non-collagenous matrix in tendon function. Int J ExpPathol. 94;4: 248-59.

^ Hulmes, D. J. S. (2002). "Building Collagen Molecules, Fibrils, and Suprafibrillar Structures". Journal of Structural Biology . 137 (1–2): 2–10. doi : 10.1006/jsbi.2002.4450 . PMID 12064927 .

^ Silver, F. H.; Freeman, J. W.; Seehra, G. P. (2003). "Collagen self-assembly and the development of tendon mechanical properties". Journal of Biomechanics . 36 (10): 1529–1553. doi : 10.1016/S0021-9290(03)00135-0 . PMID 14499302 .

^ Ker, R. F. (2002). "The implications of the adaptable fatigue quality of tendons for their construction, repair and function". Comparative Biochemistry and Physiology A . 133 (4): 987–1000. doi : 10.1016/S1095-6433(02)00171-X . PMID 12485688 .

^ Cribb, A. M.; Scott, J.E. (1995). In Tendon response to tensile-stress - an ultrastructural investigation of collagen - proteoglycan interactions in stressed tendon,1995; Cambridge Univ Press.pp 423-428.

^ Screen H.R., Lee D.A., Bader D.L., Shelton J.C. (2004). "An investigation into the effects of the hierarchical structure of tendon fascicles on micromechanical properties" . Proc Inst Mech Eng H . 218 (2): 109–119. doi : 10.1243/095441104322984004 . PMID 15116898 . S2CID 46256718 . CS1 maint: multiple names: authors list ( link )

^ Puxkandl, R.; Zizak, I.; Paris, O.; Keckes, J.; Tesch, W.; Bernstorff, S.; Purslow, P.; Fratzl, P. (2002). "Viscoelastic properties of collagen: synchrotron radiation investigations and structural model" . Philosophical Transactions of the Royal Society B . 357 (1418): 191–197. doi : 10.1098/rstb.2001.1033 . PMC 1692933 . PMID 11911776 .

^ Gupta H.S., Seto J., Krauss S., Boesecke P.& Screen H.R.C. (2010). In situ multi-level analysis of viscoelastic deformation mechanisms in tendon collagen. J. Struct. Biol . 169(2):183-191.

^ Thorpe C.T; Udeze C.P; Birch H.L.; Clegg P.D.; Screen H.R.C. (2012). "Specialisation of tendon mechanical properties results from inter-fascicular differences" . Journal of the Royal Society Interface . 9 (76): 3108–3117. doi : 10.1098/rsif.2012.0362 . PMC 3479922 . PMID 22764132 .

^ Thorpe C.T.; Klemt C; Riley G.P.; Birch H.L.; Clegg P.D.; Screen H.R.C. (2013). "Helical sub-structures in energy-storing tendons provide a possible mechanism for efficient energy storage and return". Acta Biomater . 9 (8): 7948–56. doi : 10.1016/j.actbio.2013.05.004 . PMID 23669621 .

^ Gatt R, Vella Wood M, Gatt A, Zarb F, Formosa C, Azzopardi KM, Casha A, Agius TP, Schembri-Wismayer P, Attard L, Chockalingam N, Grima JN (2015). "Negative Poisson's ratios in tendons: An unexpected mechanical response". Acta Biomater . 24 : 201–208. doi : 10.1016/j.actbio.2015.06.018 . PMID 26102335 .

^ Batson EL, Paramour RJ, Smith TJ, Birch HL, Patterson-Kane JC, Goodship AE. (2003). Equine Vet J. |volume=35 |issue=3 |pages=314-8.

Are the material properties and matrix composition of equine flexor and extensor tendons determined by their functions?

^ ScreenH.R.C., Tanner, K.E. (2012). Structure & Biomechanics of Biological Composites. In: Encyclopaedia of Composites 2nd Ed. Nicolais & Borzacchiello.Pub. John Wiley & Sons, Inc. ISBN 978-0-470-12828-2 (pages 2928-39)

^ Nakagawa, Y. (1989). "Effect of disuse on the ultra structure of the Achilles tendon in rats". European Journal of Applied Physiology . 59 (3): 239–242. doi : 10.1007/bf02386194 . PMID 2583169 . S2CID 20626078 .

^ Reeves, N. D. (2005). "Influence of 90-day simulated micro-gravity on human tendon mechanical properties and the effect of restiveness countermeasures" . Journal of Applied Physiology . 98 (6): 2278–2286. doi : 10.1152/japplphysiol.01266.2004 . hdl : 11379/25397 . PMID 15705722 .

^ Jump up to: a b Riley, G. (2004). "The pathogenesis of tendinopathy. A molecular perspective" (PDF) . Rheumatology . 43 (2): 131–142. doi : 10.1093/rheumatology/keg448 . PMID 12867575 .

^ Jump up to: a b c d Sharma, P. M., N. (2006). "Biology of tendon injury: healing, modeling and remodeling". Journal of Musculoskeletal and Neuronal Interactions . 6 (2): 181–190. PMID 16849830 . CS1 maint: multiple names: authors list ( link )

^ Jump up to: a b c d Sharma, P.; Maffulli, N. (2005). "Tendon injury and tendinopathy: Healing and repair" . Journal of Bone and Joint Surgery. American Volume . 87A (1): 187–202. doi : 10.2106/JBJS.D.01850 . PMID 15634833 . S2CID 1111422 .

^ Jump up to: a b c d e f Wang, J. H. C. (2006). "Mechanobiology of tendon". Journal of Biomechanics . 39 (9): 1563–1582. doi : 10.1016/j.jbiomech.2005.05.011 . PMID 16000201 .

^ Riley, G. P.; Curry, V.; DeGroot, J.; van El, B.; Verzijl, N.; Hazleman, B. L.; Bank, R. A. (2002). "Matrix metalloproteinase activities and their relationship with collagen remodelling in tendon pathology". Matrix Biology . 21 (2): 185–195. doi : 10.1016/S0945-053X(01)00196-2 . PMID 11852234 .

^ Moulin, V.; Tam, B. Y. Y.; Castilloux, G.; Auger, F. A.; O'Connor-McCourt, M. D.; Philip, A.; Germain, L. (2001). "Fetal and adult human skin fibroblasts display intrinsic differences in contractile capacity". Journal of Cellular Physiology . 188 (2): 211–222. doi : 10.1002/jcp.1110 . PMID 11424088 . S2CID 22026692 .

^ Boyer, M. I. W., J. T.; Lou, J.; Manske, P. R.; Gelberman, R. H.; Cai, S. R. (2001). "Quantitative variation in vascular endothelial growth factor mRNA expression during early flexor tendon healing: an investigation in a canine model" . Journal of Orthopaedic Research . 19 (5): 869–872. doi : 10.1016/S0736-0266(01)00017-1 . PMID 11562135 . S2CID 20903366 . CS1 maint: multiple names: authors list ( link )

^ Astrom, M.; Rausing, A. (1995). "Chronic Achilles Tendinopathy - A survey of Surgical and Histopathologic findings". Clinical Orthopaedics and Related Research . 316 (316): 151–164. doi : 10.1097/00003086-199507000-00021 . PMID 7634699 . S2CID 25486134 .

^ Berge, James C. Vanden; Storer, Robert W. (1995). "Intratendinous ossification in birds: A review". Journal of Morphology . 226 (1): 47–77. doi : 10.1002/jmor.1052260105 . PMID 29865323 . S2CID 46926646 .

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A tendon or sinew is a tough high-tensile-strength band of dense fibrous connective tissue that connects muscle to bone and is capable of withstanding tension and transmit the mechanical forces of muscle contraction to the skeletal system.

Tendons are similar to ligaments ; both are made of collagen . Ligaments connect one bone to another, while tendons connect muscle to bone.

Histologically , tendons consist of dense regular connective tissue . The main cellular component of tendons are specialized fibroblasts called tendon cells (tenocytes). Tenocytes synthesize the extracellular matrix of tendons, abundant in densely packed collagen fibers . The collagen fibers are parallel to each other and organized into tendon fascicles. Individual fascicles are bound by the endotendineum , which is a delicate loose connective tissue containing thin collagen fibrils [1] [2] and elastic fibres. [3] Groups of fascicles are bounded by the epitenon , which is a sheath of dense irregular connective tissue . The whole tendon is enclosed by a fascia . The space between the fascia and the tendon tissue is filled with the paratenon , a fatty areolar tissue . [4] Normal healthy tendons are anchored to bone by Sharpey's fibres .

The dry mass of normal tendons, which makes up 30-45% of their total mass, is composed of:

While type I collagen makes up most of the collagen in tendon, many minor collagens are present that play vital roles in proper tendon development and function. These include type II collagen in the cartilaginous zones, type III collagen in the reticulin fibres of the vascular walls, type IX collagen, type IV collagen in the basement membranes of the capillaries , type V collagen in the vascular walls, and type X collagen in the mineralized fibrocartilage near the interface with the bone. [5] [9]

Collagen fibres coalesce into macroaggregates . After secretion from the cell, cleaved by procollagen N- and C- proteases , the tropocollagen molecules spontaneously assemble into insoluble fibrils. A collagen molecule is about 300 nm long and 1–2 nm wide, and the diameter of the fibrils that are formed can range from 50–500 nm. In tendons, the fibrils then assemble further to form fascicles, which are about 10 mm in length with a diameter of 50–300 μm, and finally into a tendon fibre with a diameter of 100–500 μm. [10]

The collagen in tendons are held together with proteoglycan (a compound consisting of a protein bonded to glycosaminoglycan groups, present especially in connective tissue) components including decorin and, in compressed regions of tendon, aggrecan , which are capable of binding to the collagen fibrils at specific locations. [11] The proteoglycans are interwoven with the collagen fibrils – their glycosaminoglycan (GAG) side chains have multiple interactions with the surface of the fibrils – showing that the proteoglycans are important structurally in the interconnection of the fibrils. [12] The major GAG components of the tendon are dermatan sulfate and chondroitin sulfate , which associate with collagen and are involved in the fibril assembly process during tendon development. Dermatan sulfate is thought to be responsible for forming associations between fibrils, while chondroitin sulfate is thought to be more involved with occupying volume between the fibrils to keep them separated and help withstand deformation. [13] The dermatan sulfate side chains of decorin aggregate in solution, and this behavior can assist with the assembly of the collagen fibrils. When decorin molecules are bound to a collagen fibril, their dermatan sulfate chains may extend and associate with other dermatan sulfate chains on decorin that is bound to separate fibrils, therefore creating interfibrillar bridges and eventually causing parallel alignment of the fibrils. [14]

The tenocytes produce the collagen molecules, which aggregate end-to-end and side-to-side to produce collagen fibrils. Fibril bundles are organized to form fibres with the elongated tenocytes closely packed between them. There is a three-dimensional network of cell processes associated with collagen in the tendon. The cells communicate with each other through gap junctions , and this signalling gives them the ability to detect and respond to mechanical loading. [15]

Blood vessels may be visualized within the endotendon running parallel to collagen fibres, with occasional branching transverse anastomoses .

The internal tendon bulk is thought to contain no nerve fibres, but the epitenon and paratenon contain nerve endings, while Golgi tendon organs are present at the myotendinous junction between tendon and muscle.

Tendon length varies in all major groups and from person to person. Tendon length is, in practice, the deciding factor regarding actual and potential muscle size. For example, all other relevant biological factors being equal, a man with a shorter tendons and a longer biceps muscle will have greater potential for muscle mass than a man with a longer tendon and a shorter muscle. Successful bodybuilders will generally have shorter tendons. Conversely, in sports requiring athletes to excel in actions such as running or jumping, it is beneficial to have longer than average Achilles tendon and a shorter calf muscle . [16]

Tendon length is determined by genetic predisposition, and has not been shown to either increase or decrease in response to environment, unlike muscles, which can be shortened by trauma, use imbalances and a lack of recovery and stretching. [17] RAT

Traditionally, tendons have been considered to be a mechanism by which muscles connect to bone as well as muscles itself, functioning to transmit forces. This connection allows tendons to passively modulate forces during locomotion, providing additional stability with no active work. However, over the past two decades, much research has focused on the elastic properties of some tendons and their ability to function as springs. Not all tendons are required to perform the same functional role, with some predominantly positioning limbs, such as the fingers when writing (positional tendons) and others acting as springs to make locomotion more efficient (energy storing tendons). [18] Energy storing tendons can store and recover energy at high efficiency. For example, during a human stride, the Achilles tendon stretches as the ankle joint dorsiflexes. During the last portion of the stride, as the foot plantar-flexes (pointing the toes down), the stored elastic energy is released. Furthermore, because the tendon stretches, the muscle is able to function with less or even no change in length , allowing the muscle to generate more force.

The mechanical properties of the tendon are dependent on the collagen fiber diameter and orientation. The collagen fibrils are parallel to each other and closely packed, but show a wave-like appearance due to planar undulations, or crimps, on a scale of several micrometers. [19] In tendons, the collagen fibres have some flexibility due to the absence of hydroxyproline and proline residues at specific locations in the amino acid sequence, which allows the formation of other conformations such as bends or internal loops in the triple helix and results in the development of crimps. [20] The crimps in the collagen fibrils allow the tendons to have some flexibility as well as a low compressive stiffness. In addition, because the tendon is a multi-stranded structure made up of many partially independent fibrils and fascicles, it does not behave as a single rod, and this property also contributes to its flexibility. [21]

The proteoglycan components of tendons also are important to the mechanical properties. While the collagen fibrils allow tendons to resist tensile stress, the proteoglycans allow them to resist compressive stress. These molecules are very hydrophilic, meaning that they can absorb a large amount of water and therefore have a high swelling ratio. Since they are noncovalently bound to the fibrils, they may reversibly associate and disassociate so that the b
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