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Elastic Cartilage
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. Structure Elastic cartilage is histologically similar to hyaline cartilage but contains many yellow elastic fibers lying in a solid matrix. These fibers form bundles that appear dark under a microscope. The elastic fibers require special staining since when it is stained using haematoxylin and eosin (H&E) stain it appears the same as hyaline cartilage. Verhoeff van Geison stains are used (giving the elastic fibers a black color), but aldehyde fuchsin stains, Weigert's elastic stains, and orcein stains also work. These fibers give elastic carti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Auricle (anatomy)
The auricle or auricula is the visible part of the ear that is outside the head. It is also called the pinna ( Latin for " wing" or "fin", plural pinnae), a term that is used more in zoology. Structure The diagram shows the shape and location of most of these components: * ''antihelix'' forms a 'Y' shape where the upper parts are: ** ''Superior crus'' (to the left of the ''fossa triangularis'' in the diagram) ** ''Inferior crus'' (to the right of the ''fossa triangularis'' in the diagram) * ''Antitragus'' is below the ''tragus'' * ''Aperture'' is the entrance to the ear canal * ''Auricular sulcus'' is the depression behind the ear next to the head * ''Concha'' is the hollow next to the ear canal * Conchal angle is the angle that the back of the ''concha'' makes with the side of the head * ''Crus'' of the helix is just above the ''tragus'' * ''Cymba conchae'' is the narrowest end of the ''concha'' * External auditory meatus is the ear canal * ''Fossa triangularis'' is the de ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Perichondrium
The perichondrium (from Greek el, περί, peri, around, label=none and el, χόνδρος, chondros, cartilage, label=none) is a layer of dense irregular connective tissue that surrounds the cartilage of developing bone. It consists of two separate layers: an outer fibrous layer and inner chondrogenic layer. The fibrous layer contains fibroblasts, which produce collagenous fibres. The chondrogenic layer remains undifferentiated and can form chondroblasts. Perichondrium can be found around the perimeter of elastic cartilage 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 audit ... and hyaline cartilage. Perichondrium is a type of irregular collagenous ordinary connective tissue, and also functions in the growth and repair of cartilage. Perichondrium contains type I collagen and t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Tension (physics)
In physics, tension is described as the pulling force transmitted axially by the means of a string, a rope, chain, or similar object, or by each end of a rod, truss member, or similar three-dimensional object; tension might also be described as the action-reaction pair of forces acting at each end of said elements. Tension could be the opposite of compression. At the atomic level, when atoms or molecules are pulled apart from each other and gain potential energy with a restoring force still existing, the restoring force might create what is also called tension. Each end of a string or rod under such tension could pull on the object it is attached to, in order to restore the string/rod to its relaxed length. Tension (as a transmitted force, as an action-reaction pair of forces, or as a restoring force) is measured in newtons in the International System of Units (or pounds-force in Imperial units). The ends of a string or other object transmitting tension will exert forces on ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Copolymerization
In polymer chemistry, a copolymer is a polymer derived from more than one species of monomer. The polymerization of monomers into copolymers is called copolymerization. Copolymers obtained from the copolymerization of two monomer species are sometimes called ''bipolymers''. Those obtained from three and four monomers are called ''terpolymers'' and ''quaterpolymers'', respectively. Copolymers can be characterized by a variety of techniques such as NMR spectroscopy and size-exclusion chromatography to determine the molecular size, weight, properties, and composition of the material. Commercial copolymers include acrylonitrile butadiene styrene (ABS), styrene/butadiene co-polymer (SBR), nitrile rubber, styrene-acrylonitrile, styrene-isoprene-styrene (SIS) and ethylene-vinyl acetate, all of which are formed by chain-growth polymerization. Another production mechanism is step-growth polymerization, which is used to produce the nylon-12/6/66 copolymer of nylon 12, nylon 6 and nylo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chondroblast
Chondroblasts, or perichondrial cells, is the name given to mesenchymal progenitor cells in situ which, from endochondral ossification, will form chondrocytes in the growing cartilage matrix. Another name for them is subchondral cortico-spongious progenitors. They have euchromatic nuclei and stain by basic dyes. These cells are extremely important in chondrogenesis due to their role in forming both the chondrocytes and cartilage matrix which will eventually form cartilage. Use of the term is technically inaccurate since mesenchymal progenitors can also technically differentiate into osteoblasts or fat. Chondroblasts are called chondrocytes when they embed themselves in the cartilage matrix, consisting of proteoglycan and collagen fibers, until they lie in the matrix lacunae. Once they embed themselves into the cartilage matrix, they grow the cartilage matrix by growing more cartilage extracellular matrix rather than by dividing further. Structure Within adults and developing ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aggrecan
Aggrecan (ACAN), also known as cartilage-specific proteoglycan core protein (CSPCP) or chondroitin sulfate proteoglycan 1, is a protein that in humans is encoded by the ''ACAN'' gene. This gene is a member of the lectican (chondroitin sulfate proteoglycan) family. The encoded protein is an integral part of the extracellular matrix in cartilagenous tissue and it withstands compression in cartilage. Aggrecan is a proteoglycan, or a protein modified with large carbohydrates; the human form of the protein is 2316 amino acids long and can be expressed in multiple isoforms due to alternative splicing. Aggrecan was named for its ability to form large aggregates in the cartilage tissue (a large aggregating proteoglycan). Structure Aggrecan is a high molecular weight (1x106 < M < 3x106) proteoglycan. It exhibits a bottlebrush structure, in which |
Proteoglycan
Proteoglycans are proteins that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate-GlcA- Gal-Gal- Xyl-PROTEIN). The Ser residue is generally in the sequence -Ser- Gly-X-Gly- (where X can be any amino acid residue but proline), although not every protein with this sequence has an attached glycosaminoglycan. The chains are long, linear carbohydrate polymers that are negatively charged under physiological conditions due to the occurrence of sulfate and uronic acid groups. Proteoglycans occur in connective tissue. Types Proteoglycans are categorized by their relative size (large and small) and the nature of their glycosaminoglycan chains. Types include: Certain members are considered members of the "small leucine-rich proteogly ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Type II Collagen
Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage. Type II collagen is organised into fibrils. This fibrillar network of collagen allows the cartilage to entrap the proteoglycan aggregate, as well as providing tensile strength to the tissue. Oral administration of native type II collagen induces oral tolerance to pathological immune responses and may be useful in arthritis. See also * Type I collagen Type I collagen is the most abundant collagen of the human body. It forms large, eosinophilic fibers known as collagen fibers. It is present in scar tissue, the end product when tissue heals by repair, as well as tendons, ligaments, the endomy ... * Collagen, type III, alpha 1 References External links * Collagens {{gene-12-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Collagen
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. Depending upon the degree of mineralization, collagen tissues may be rigid (bone) or compliant (tendon) or have a gradient from rigid to compliant (cartilage). Collagen is also abundant in corneas, blood vessels, the gut, intervertebral discs, and the dentin in teeth. In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue and accounts for 6% of the weight of the skeletal muscle tissue. The fibroblast is the most common ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycoprotein
Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated. In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important integral membrane proteins, where they play a role in cell–cell interactions. It is important to distinguish endoplasmic reticulum-based glycosylation of the secretory system from reversible cytosolic-nuclear glycosylation. Glycoproteins of the cytosol and nucleus can be modified through the reversible addition of a single GlcNAc residue that is considered reciprocal to phosphorylation and the functions of these are likely to be an additional regulatory mechanism that controls phosphorylation-based signalling. In contra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibrillin
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. Clinical aspects Marfan syndrome is a genetic disorder of the connective tissue caused by defected FBN1 gene. Mutations in FBN1 and FBN2 are also sometimes associated with adolescent idiopathic scoliosis. Types Fibrillin-1 Fibrillin-1 is a major component of the microfibrils that form a sheath surrounding the amorphous elastin. It is believed that the microfibrils are composed of end-to-end polymers of fibrillin. To date, 3 forms of fibrillin have been described. The fibrillin-1 protein was isolated by Engvall in 1986, and mutations in the FBN1 gene cause Marfan syndrome. This protein is found in humans, and its gene is found on chromosome 15. At present more than 1500 different ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Elastin
Elastin is a protein that in humans is encoded by the ''ELN'' gene. Elastin is a key component of the extracellular matrix in gnathostomes (jawed vertebrates). 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. Function The ''ELN'' gene encodes a protein that is one of the two components of elastic fibers. The encoded protein is rich in hydrophobic amino acids such as glycine and proline, which form mobile hydrophobic regions bounded by crosslinks between lysine residues. Multiple transcript variants encoding different isoforms have been found for this gene. Elastin's soluble precursor is tropoelastin. The characterization of disorder is consistent with an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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