Tendon

For other uses, see Tendon (disambiguation).

glycans are interwoven with the collagen brils their

glycosaminoglycan (GAG) side chains have multiple interactions with the surface of the brils showing that
the proteoglycans are important structurally in the interconnection of the brils.[10] The major GAG components
of the tendon are dermatan sulfate and chondroitin sulfate, which associate with collagen and are involved in
the bril assembly process during tendon development.
Dermatan sulfate is thought to be responsible for forming associations between brils, while chondroitin sulfate
is thought to be more involved with occupying volume
between the brils to keep them separated and help withstand deformation.[11] The dermatan sulfate side chains of
decorin aggregate in solution, and this behavior can assist
with the assembly of the collagen brils. When decorin
molecules are bound to a collagen bril, their dermatan
sulfate chains may extend and associate with other dermatan sulfate chains on decorin that is bound to separate
brils, therefore creating interbrillar bridges and eventually causing parallel alignment of the brils.[12]

A tendon (or sinew) is a tough band of brous connective

tissue that usually connects muscle to bone and is capable
of withstanding tension. Tendons are similar to ligaments
and fasciae; all three are made of collagen. Ligaments
join one bone to another bone; fasciae connect muscles
to other muscles. Tendons and muscles work together to
move bones.

Structure

Histologically, tendons consist of dense regular connective tissue fascicles encased in dense irregular connective tissue sheaths. Normal healthy tendons are composed
mostly of parallel arrays of collagen bers closely packed
together. The dry mass of normal tendons, which makes
up about 30% of their total mass, is composed of about
86% collagen, 2% elastin, 15% proteoglycans, and 0.2%
inorganic components such as copper, manganese, and
calcium.[1][2] The collagen portion is made up of 9798%
type I collagen, with small amounts of other types of collagen. These include type II collagen in the cartilaginous
zones, type III collagen in the reticulin bres 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 brocartilage near the interface with the bone.[1][3]
Collagen bres coalesce into macroaggregates. After secretion from the cell, the terminal peptides are cleaved
by procollagen N- and C-proteinases, and the tropocollagen molecules spontaneously assemble into insoluble brils. A collagen molecule is about 300 nm long and 12
nm wide, and the diameter of the brils that are formed
can range from 50500 nm. In tendons, the brils then
assemble further to form fascicles, which are about 10
mm in length with a diameter of 50300 m, and nally
into a tendon bre with a diameter of 100500 m.[4]
Fascicles are bound by the endotendineum, which is a
delicate loose connective tissue containing thin collagen
brils.[5][6] and elastic bres.[7] Groups of fascicles are
bounded by the epitenon. Filling the interstitia within
the fascia where the tendon is located is the paratenon a
fatty areolar tissue.[8]

The tenocytes produce the collagen molecules, which aggregate end-to-end and side-to-side to produce collagen
brils. Fibril bundles are organized to form bres 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.[13]
Blood vessels may be visualized within the endotendon running parallel to collagen bres, with occasional
branching transverse anastomoses.
The internal tendon bulk is thought to contain no nerve
bres, but the epitenon and paratenon contain nerve endings, while Golgi tendon organs are present at the 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
The collagen in tendons are held together with proteogly- such as running or jumping, it is benecial to have longer
can components including decorin and, in compressed re- than average Achilles tendon and a shorter calf muscle.[14]
gions of tendon, aggrecan, which are capable of binding
Tendon length is determined by genetic predisposition,
to the collagen brils at specic locations.[9] The proteo1

2 FUNCTIONS

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.[15]

Functions

a bre composite material, built as a series of hierarchical levels. At each level of the hierarchy, the collagen
units are bound together by either collagen crosslinks, or
the proteoglycans, to create a structure highly resistant
to tensile load.[21] The elongation and the strain of the
collagen brils alone have been shown to be much lower
than the total elongation and strain of the entire tendon
under the same amount of stress, demonstrating that the
proteoglycan-rich matrix must also undergo deformation,
and stiening of the matrix occurs at high strain rates.[22]
This deformation of the non-collagenous matrix occurs
at all levels of the tendon hierarchy, and by modulating
the organisation and structure of this matrix, the dierent
mechanical properties required by dierent tendons can
be achieved.[23] Energy storing tendons have been shown
to utilise signicant amounts of sliding between fascicles to enable the high strain characteristics they require,
whilst positional tendons rely more heavily on sliding between collagen bres and brils.[24] However, recent data
suggests that energy storing tendons may also contain fascicles which are twisted, or helical, in nature - an arrangement that would be highly benecial for providing the
spring-like behaviour required in these tendons.[25]

Tendons have been traditionally considered to simply be

a mechanism by which muscles connect to bone, functioning simply 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 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 ngers when writing
(positional tendons) and others acting as springs to make
locomotion more ecient (energy storing tendons).[16]
Energy storing tendons can store and recover energy at
high eciency. For example, during a human stride, the
Achilles tendon stretches as the ankle joint dorsiexes.
During the last portion of the stride, as the foot plantarexes (pointing the toes down), the stored elastic energy 2.1 Mechanics
is released. Furthermore, because the tendon stretches,
the muscle is able to function with less or even no change Main article: Soft tissue
in length, allowing the muscle to generate greater force.
The mechanical properties of the tendon are dependent
on the collagen ber diameter and orientation. The collagen brils 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.[17]
In tendons, the collagen bres have some exibility due
to the absence of hydroxyproline and proline residues at
specic 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.[18] The crimps in the collagen brils
allow the tendons to have some exibility as well as a low
compressive stiness. In addition, because the tendon is a
multi-stranded structure made up of many partially independent brils and fascicles, it does not behave as a single
rod, and this property also contributes to its exibility.[19]

Tendons are viscoelastic structures which means they exhibit both elastic and viscous behaviour. When stretched,
tendons exhibit typical soft tissue behavior. The forceextension, or stress-strain curve starts with a very low
stiness region, as the crimp structure straightens and the
collagen bres align suggesting negative Poissons ratio in
the bres of the tendon. [26][27] More recently, tests carried out in vivo (through MRI) and ex vivo (through mechanical testing of various cadaveric tendon tissue) have
shown that healthy tendons are highly anisotropic and exhibit a negative Poissons ratio (auxetic) in some planes
when stretched up to 2% along their length, i.e. within
their normal range of motion. [28] After this 'toe' region,
the structure becomes signicantly stier, and has a linear stress-strain curve until it begins to fail. The mechanical properties of tendons vary widely, as they are matched
to the functional requirements of the tendon. The energy
storing tendons tend to be more elastic, or less sti, so
they can more easily store energy, whilst the stier positional tendons tend to be a little more viscoelastic, and
less elastic, so they can provide ner control of movement. A typical energy storing tendon will fail at around
12-15% strain, and a stress in the region of 100-150
MPa, although some tendons are notably more extensible
than this, for example the equine (horse) SDFT, which
stretches in excess of 20% when the horse is galloping.[29]
Positional tendons can fail at strains as low as 6-8%, but
can have moduli in the region of 700-1000 MPa.[30]

The proteoglycan components of tendons also are important to the mechanical properties. While the collagen brils 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 brils,
they may reversibly associate and disassociate so that the
bridges between brils can be broken and reformed. This
process may be involved in allowing the bril to elongate
and decrease in diameter under tension.[20] However, the
proteoglycans may also have a role in the tensile properties of tendon. The structure of tendon is eectively Several studies have demonstrated that tendons respond

2.2

Healing

to changes in mechanical loading with growth and remodeling processes, much like bones. In particular, a study
showed that disuse of the Achilles tendon in rats resulted
in a decrease in the average thickness of the collagen
ber bundles comprising the tendon.[31] In humans, an experiment in which people were subjected to a simulated
micro-gravity environment found that tendon stiness decreased signicantly, even when subjects were required
to perform restiveness exercises.[32] These eects have
implications in areas ranging from treatment of bedridden patients to the design of more eective exercises for
astronauts.

3
to scar-like.[36]

Matrix metalloproteinases or MMPs have a very important role in the degradation and remodeling of the ECM
during the healing process after a tendon injury. Certain
MMPs including MMP-1, MMP-2, MMP-8, MMP-13,
and MMP-14 have collagenase activity, meaning that, unlike many other enzymes, they are capable of degrading
collagen I brils. The degradation of the collagen brils
by MMP-1 along with the presence of denatured collagen
are factors that are believed to cause weakening of the
tendon ECM and an increase in the potential for another
rupture to occur.[37] In response to repeated mechanical
loading or injury, cytokines may be released by tenocytes
and can induce the release of MMPs, causing degradation
2.2 Healing
of the ECM and leading to recurring injury and chronic
[35]
The tendons in the foot are highly complex and intricate. tendinopathies.
Therefore, the healing process for a broken tendon is long A variety of other molecules are involved in tendon reand painful. Most people who do not receive medical at- pair and regeneration. There are ve growth factors
tention within the rst 48 hours of the injury will suer that have been shown to be signicantly upregulated and
from severe swelling, pain, and a burning sensation where active during tendon healing: insulin-like growth facthe injury occurred.
tor 1 (IGF-I), platelet-derived growth factor (PDGF),
It was believed previously that tendons could not undergo vascular endothelial growth factor (VEGF), basic brob(bFGF), and transforming growth facmatrix turnover and that tenocytes were not capable of last growth factor[36]
tor
beta
(TGF-).
These growth factors all have dierrepair. However, it has been shown more recently that,
ent
roles
during
the
healing
process. IGF-1 increases colthroughout the lifetime of a person, tenocytes in the tenlagen
and
proteoglycan
production
during the rst stage
don actively synthesize ECM components as well as enof
inammation,
and
PDGF
is
also
present during the
zymes such as matrix metalloproteinases (MMPs) can de[33]
early
stages
after
injury
and
promotes
the synthesis of
grade the matrix. Tendons are capable of healing and
other
growth
factors
along
with
the
synthesis
of DNA
recovering from injuries in a process that is controlled by
[36]
and
the
proliferation
of
tendon
cells.
The
three
isothe tenocytes and their surrounding extracellular matrix.
forms of TGF- (TGF-1, TGF-2, TGF-3) are known
The three main stages of tendon healing are inamma- to play a role in wound healing and scar formation.[38]
tion, repair or proliferation, and remodeling, which can VEGF is well known to promote angiogenesis and to
be further divided into consolidation and maturation. induce endothelial cell proliferation and migration, and
These stages can overlap with each other. In the rst VEGF mRNA has been shown to be expressed at the site
stage, inammatory cells such as neutrophils are recruited of tendon injuries along with collagen I mRNA.[39] Bone
to the injury site, along with erythrocytes. Monocytes and morphogenetic proteins (BMPs) are a subgroup of TGF-
macrophages are recruited within the rst 24 hours, and superfamily that can induce bone and cartilage formation
phagocytosis of necrotic materials at the injury site oc- as well as tissue dierentiation, and BMP-12 specically
curs. After the release of vasoactive and chemotactic fac- has been shown to inuence formation and dierentiation
tors, angiogenesis and the proliferation of tenocytes are of tendon tissue and to promote brogenesis.
initiated. Tenocytes then move into the site and start to
synthesize collagen III.[34][35] After a few days, the repair
or proliferation stage begins. In this stage, the tenocytes 2.2.1 Eects of activity on healing
are involved in the synthesis of large amounts of collagen and proteoglycans at the site of injury, and the levels In animal models, extensive studies have been conducted
of GAG and water are high.[36] After about six weeks, to investigate the eects of mechanical strain in the form
the remodeling stage begins. The rst part of this stage of activity level on tendon injury and healing. While
is consolidation, which lasts from about six to ten weeks stretching can disrupt healing during the initial inammaafter the injury. During this time, the synthesis of col- tory phase, it has been shown that controlled movement
lagen and GAGs is decreased, and the cellularity is also of the tendons after about one week following an acute
decreased as the tissue becomes more brous as a result of injury can help to promote the synthesis of collagen by
increased production of collagen I and the brils become the tenocytes, leading to increased tensile strength and
aligned in the direction of mechanical stress.[35] The nal diameter of the healed tendons and fewer adhesions than
maturation stage occurs after ten weeks, and during this tendons that are immobilized. In chronic tendon injuries,
time there is an increase in crosslinking of the collagen mechanical loading has also been shown to stimulate brils, which causes the tissue to become stier. Gradu- broblast proliferation and collagen synthesis along with
ally, over about one year, the tissue will turn from brous collagen realignment, all of which promote repair and

OTHER ANIMALS

remodeling.[36] To further support the theory that move- which the tendon is marinated in garlic. It is also somement and activity assist in tendon healing, it has been times found in the Vietnamese noodle dish ph.
shown that immobilization of the tendons after injury often has a negative eect on healing. In rabbits, collagen fascicles that are immobilized have shown decreased
4 Clinical signicance
tensile strength, and immobilization also results in lower
amounts of water, proteoglycans, and collagen crosslinks
4.1 Injury
in the tendons.[34]
Several mechanotransduction mechanisms have been
proposed as reasons for the response of tenocytes to mechanical force that enable them to alter their gene expression, protein synthesis, and cell phenotype, and eventually
cause changes in tendon structure. A major factor is mechanical deformation of the extracellular matrix, which
can aect the actin cytoskeleton and therefore aect cell
shape, motility, and function. Mechanical forces can be
transmitted by focal adhesion sites, integrins, and cell-cell
junctions. Changes in the actin cytoskeleton can activate
integrins, which mediate outside-in and inside-out
signaling between the cell and the matrix. G-proteins,
which induce intracellular signaling cascades, may also
be important, and ion channels are activated by stretching to allow ions such as calcium, sodium, or potassium
to enter the cell.[36]

Society and culture

Sinew was widely used throughout pre-industrial eras as

a tough, durable ber. Some specic uses include using
sinew as thread for sewing, attaching feathers to arrows
(see etch), lashing tool blades to shafts, etc. It is also
recommended in survival guides as a material from which
strong cordage can be made for items like traps or living structures. Tendon must be treated in specic ways
to function usefully for these purposes. Inuit and other
circumpolar people utilized sinew as the only cordage for
all domestic purposes due to the lack of other suitable
ber sources in their ecological habitats. The elastic properties of particular sinews were also used in composite
recurved bows favoured by the steppe nomads of Eurasia. The rst stone throwing artillery also used the elastic
properties of sinew.
Sinew makes for an excellent cordage material for three
reasons: It is extremely strong, it contains natural glues,
and it shrinks as it dries, doing away with the need for
knots.

Tendons are subject to many types of injuries. There are

various forms of tendinopathies or tendon injuries due to
overuse. These types of injuries generally result in inammation and degeneration or weakening of the tendons, which may eventually lead to tendon rupture.[34]
Tendinopathies can be caused by a number of factors relating to the tendon extracellular matrix (ECM), and their
classication has been dicult because their symptoms
and histopathology often are similar.
The rst category of tendinopathy is paratenonitis, which
refers to inammation of the paratenon, or paratendinous sheet located between the tendon and its sheath.
Tendinosis refers to non-inammatory injury to the tendon at the cellular level. The degradation is caused by
damage to collagen, cells, and the vascular components
of the tendon, and is known to lead to rupture.[40] Observations of tendons that have undergone spontaneous
rupture have shown the presence of collagen brils that
are not in the correct parallel orientation or are not uniform in length or diameter, along with rounded tenocytes, other cell abnormalities, and the ingrowth of blood
vessels.[34] Other forms of tendinosis that have not led
to rupture have also shown the degeneration, disorientation, and thinning of the collagen brils, along with an
increase in the amount of glycosaminoglycans between
the brils.[35] The third is paratenonitis with tendinosis, in
which combinations of paratenon inammation and tendon degeneration are both present. The last is tendinitis,
which refers to degeneration with inammation of the
tendon as well as vascular disruption.[1]
Tendinopathies may be caused by several intrinsic factors
including age, body weight, and nutrition. The extrinsic
factors are often related to sports and include excessive
forces or loading, poor training techniques, and environmental conditions.[33]

5 Other animals

In some organisms, notable ones being birds[41] and

ornithischian dinosaurs,[42] portions of the tendon can be3.1 Culinary uses
come ossied. In this process, osteocytes inltrate the
tendon and lay down bone as they would in sesamoid bone
Main article: Tendon (meal)
such as the patella. In birds, tendon ossication primarily
occurs in the hindlimb, while in ornithischian dinosaurs,
Tendon (in particular, beef tendon) is used as a food in ossied axial muscle tendons form a latticework along the
some Asian cuisines (often served at yum cha or dim sum neural and haemal spines on the tail, presumably for suprestaurants). One popular dish is suan bao niu jin, in port.

[8] Dorlands Medical Dictionary 2012.Page 1382

[9] 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
brils and acquisition of biomechanical properties during tendon development.. Journal of Cellular Biochemistry 98 (6): 14361449. doi:10.1002/jcb.20776. PMID
16518859.

Ossied tendon from an Edmontosaurus bone bed in Wyoming

(Lance Formation)

See also

This article uses anatomical terminology;

overview, see Anatomical terminology.

for an

Aponeurosis
Cartilage
Chordae tendineae
List of muscles of the human body
Tendon sheath

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Tendon Source: https://en.wikipedia.org/wiki/Tendon?oldid=702833124 Contributors: Alex.tan, Heron, Olivier, Stevertigo, Ixfd64,

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