Elastic fiber | |
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![]() Subcutaneous tissue from a young rabbit. Highly magnified. (Elastic fibers labeled at right) | |
Identifiers | |
FMA | 63868 |
Anatomical terminology |
Elastic fibers (or yellow fibers) are an essential component of the extracellular matrix composed of bundles of proteins (elastin) which are produced by a number of different cell types including fibroblasts, endothelial, smooth muscle, and airway epithelial cells. [1] These fibers are able to stretch many times their length, and snap back to their original length when relaxed without loss of energy. Elastic fibers include elastin, elaunin and oxytalan.
Elastic fibers are formed via elastogenesis, [2] [3] a highly complex process involving several key proteins including fibulin-4, fibulin-5, latent transforming growth factor β binding protein 4, and microfibril associated protein 4. [4] [5] [6] [7] In this process tropoelastin, the soluble monomeric precursor to elastic fibers is produced by elastogenic cells and chaperoned to the cell surface. Following excretion from the cell, tropoelastin self associates into ~200 nm particles by coacervation, an entropically driven process involving interactions between tropoelastin's hydrophobic domains, which is mediated by glycosaminoglycans, heparan, and other molecules. [8] [9] [10] These particles then fuse to give rise to 1-2 micron spherules which continue to grow as they move down from the cells surface before being deposited onto fibrillin microfibrillar scaffolds. [1]
Following deposition onto microfibrils tropoelastin is insolubilized via extensive crosslinking by members of the lysyl oxidase and lysyl oxidase like family of copper-dependent amine oxidases into amorphous elastin, a highly resilient, insoluble polymer that is metabolically stable over a human lifespan. [1] These two families of enzymes react with the many lysine residues present in tropoelastin to form reactive aldehydes and allysine via oxidative deamination. [11]
These reactive aldehydes and allysines can react with other lysine and allysine residues to form desmosine, isodesmosine, and a number of other polyfunctional crosslinks that join surrounding molecules of tropoelastin into an extensively crosslinked elastin matrix. This process creates a diverse array of intramolecular and intermolecular crosslinks [12] These unique crosslinks are responsible for elastin's durability and persistence. Maintenance of crosslinked elastin is carried out by a number of proteins including lysyl oxidase-like 1 protein. [13]
Mature elastic fibers consist of an amorphous elastin core surrounded by a glycosaminoglycans, heparan sulphate, [14] and number of other proteins such as microfibrillar-associated glycoproteins, fibrillin, fibullin, and the elastin receptor.
Elastic fibers are found in the skin, lungs, arteries, veins, connective tissue proper, elastic cartilage, periodontal ligament, fetal tissue and other tissues which must undergo mechanical stretching. [1] In the lung there are thick and thin elastic fibers. [3]
Elastic fibers are absent from scarring, keloids and dermatofibromas and they are decreased greatly, or are absent in anetodermas. [15]
Elastic fibers stain well with aldehyde fuchsin, orcein, [16] and Weigert's elastic stain in histological sections.
The permanganate-bisulfite-toluidine blue reaction is a highly selective and sensitive method for demonstrating elastic fibers under polarizing optics. The induced birefringence demonstrates the highly ordered molecular structure of the elastin molecules in the elastic fiber. This is not readily apparent under normal optics.
There is evidence to believe that certain defects of any components of the elastic matrix may impair and alter the structural appearance of elastic and collagen fibers.
Cutis laxa and Williams syndrome have elastic matrix defects that have been directly associated with alterations in the elastin gene.
Alpha-1 antitrypsin deficiency is a genetic disorder where elastin is excessively degraded by elastase, a degrading protein released by neutrophils during the inflammatory response. This leads most often to emphysema and liver disease in affected individuals.
Buschke-Ollendorff syndrome, Menkes disease, pseudoxanthoma elasticum, and Marfan's syndrome have been associated with defects in copper metabolism and lysyl oxidase or defects in the microfibril (defects in fibrillin, or fibullin for example).
Hurler disease, a lysosomal storage disease, is associated with an altered elastic matrix.
Hypertension and some congenital heart defects are associated with alterations in the great arteries, arteries, and arterioles with alterations in the elastic matrix.
Elastosis is the buildup of elastic fibers in tissues, and is a form of degenerative disease. [17] There are a multitude of causes, but the most commons cause is actinic elastosis of the skin, also known as solar elastosis, which is caused by prolonged and excessive sun exposure, a process known as photoaging. Uncommon causes of skin elastosis include elastosis perforans serpiginosa, perforating calcific elastosis and linear focal elastosis. [17]
Condition | Distinctive features | Histopathology |
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Actinic elastosis (most common, also called solar elastosis) | Elastin replacing collagen fibers of the papillary dermis and reticular dermis | ![]() |
Elastosis perforans serpiginosa | Degenerated elastic fibers and transepidermal perforating canals (arrow in image points at one of them) [18] | ![]() |
Perforating calcific elastosis | Clumping of short elastic fibers in the dermis. [18] | ![]() |
Linear focal elastosis | Accumulation of fragmented elastotic material within the papillary dermis and transcutaneous elimination of elastotic fibers. [18] | ![]() |
Collagen is the main structural protein in the extracellular matrix found in the body's various connective tissues. As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen consists of amino acids bound together to form a triple helix of elongated fibril known as a collagen helix. It is mostly found in connective tissue such as cartilage, bones, tendons, ligaments, and skin. Collagen makes up 30% of the protein found in the human body. Vitamin E improves the production of collagen.
Elastin is a protein that in humans is encoded by the ELN gene. Elastin is a key component of the extracellular matrix in gnathostomes. It is highly elastic and present in connective tissue allowing many tissues in the body to resume their shape after stretching or contracting. Elastin helps skin to return to its original position when it is poked or pinched. Elastin is also an important load-bearing tissue in the bodies of vertebrates and used in places where mechanical energy is required to be stored.
Elastic cartilage, fibroelastic cartilage or yellow fibrocartilage is a type of cartilage present in the pinnae (auricles) of the ear giving it shape, provides shape for the lateral region of the external auditory meatus, medial part of the auditory canal Eustachian tube, corniculate and cuneiform laryneal cartilages, and the epiglottis. It contains elastic fiber networks and collagen type II fibers. The principal protein is elastin.
The basement membrane, also known as base membrane is a thin, pliable sheet-like type of extracellular matrix that provides cell and tissue support and acts as a platform for complex signalling. The basement membrane sits between epithelial tissues including mesothelium and endothelium, and the underlying connective tissue.
Fibrillin is a glycoprotein, which is essential for the formation of elastic fibers found in connective tissue. Fibrillin is secreted into the extracellular matrix by fibroblasts and becomes incorporated into the insoluble microfibrils, which appear to provide a scaffold for deposition of elastin.
Fibrils are structural biological materials found in nearly all living organisms. Not to be confused with fibers or filaments, fibrils tend to have diameters ranging from 10–100 nanometers. Fibrils are not usually found alone but rather are parts of greater hierarchical structures commonly found in biological systems. Due to the prevalence of fibrils in biological systems, their study is of great importance in the fields of microbiology, biomechanics, and materials science.
A microfibril is a very fine fibril, or fiber-like strand, consisting of glycoproteins and cellulose. It is usually, but not always, used as a general term in describing the structure of protein fiber, e.g. hair and sperm tail. Its most frequently observed structural pattern is the 9+2 pattern in which two central protofibrils are surrounded by nine other pairs. Cellulose inside plants is one of the examples of non-protein compounds that are using this term with the same purpose. Cellulose microfibrils are laid down in the inner surface of the primary cell wall. As the cell absorbs water, its volume increases and the existing microfibrils separate and new ones are formed to help increase cell strength.
Ground substance is an amorphous gel-like substance in the extracellular space of animals that contains all components of the extracellular matrix (ECM) except for fibrous materials such as collagen and elastin. Ground substance is active in the development, movement, and proliferation of tissues, as well as their metabolism. Additionally, cells use it for support, water storage, binding, and a medium for intercellular exchange. Ground substance provides lubrication for collagen fibers.
Lysyl oxidase (LOX), also known as protein-lysine 6-oxidase, is an enzyme that, in humans, is encoded by the LOX gene. It catalyzes the conversion of lysine residues into its aldehyde derivative allysine. Allysine form cross-links in extracellular matrix proteins. Inhibition of lysyl oxidase can cause osteolathyrism, but, at the same time, its upregulation by tumor cells may promote metastasis of the existing tumor, causing it to become malignant and cancerous.
Isodesmosine is a lysine derivative found in elastin. Isodesmosine is an isomeric pyridinium-based amino acid resulting from the condensation of four lysine residues between elastin proteins by lysyl-oxidase. These represent ideal biomarkers for monitoring elastin turnover because these special cross-links are only found in mature elastin in mammals.
Fibrillin-1 is a protein that in humans is encoded by the FBN1 gene, located on chromosome 15. It is a large, extracellular matrix glycoprotein that serves as a structural component of 10-12 nm calcium-binding microfibrils. These microfibrils provide force bearing structural support in elastic and nonelastic connective tissue throughout the body. Mutations altering the protein can result in a variety of phenotypic effects differing widely in their severity, including fetal death, developmental problems, Marfan syndrome or in some cases Weill-Marchesani syndrome.
Fibulin-5 is a protein that in humans is encoded by the FBLN5 gene.
Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.
Microfibrillar-associated protein 2 is a protein that in humans is encoded by the MFAP2 gene.
Lysyl oxidase homolog 1, also known as LOXL1, is an enzyme which in humans is encoded by the LOXL1 gene.
Lysyl oxidase homolog 4 is an enzyme that in humans is encoded by the LOXL4 gene.
Lysyl oxidase homolog 3 is an enzyme that in humans is encoded by the LOXL3 gene.
Histology is the study of the minute structure, composition, and function of tissues. Mature human vocal cords are composed of layered structures which are quite different at the histological level.
Wrinkly skin syndrome(WSS) is a rare genetic condition characterized by sagging, wrinkled skin, low skin elasticity, and delayed fontanelle (soft spot) closure, along with a range of other symptoms. The disorder exhibits an autosomal recessive inheritance pattern with mutations in the ATP6V0A2 gene, leading to abnormal glycosylation events. There are only about 30 known cases of WSS as of 2010. Given its rarity and symptom overlap with other dermatological conditions, reaching an accurate diagnosis is difficult and requires specialized dermatological testing. Limited treatment options are available but long-term prognosis is variable from patient to patient, based on individual case studies. Some skin symptoms recede with increasing age, while progressive neurological advancement of the disorder causes seizures and mental deterioration later in life for some patients.
MFAP4 is an extracellular matrix protein encoded by the MFAP4 gene. It is part of the MFAP family of proteoglycans, which are involved in cell adhesion, intercellular interactions and the assembly and/or maintenance of elastic fibres.
Elastic fibers are absent from scarring processes such as scars, keloids, and dermatofibromas