Beruflich Dokumente
Kultur Dokumente
Está formada por una cadena de aminoácidos con dos regiones: una hidrofóbica
constituida por los aminoácidos apolares valina, prolina y glicina, y una hidrofílica con
los aminoácidos lisina y alanina, formando estructuras de tipo hélice alfa. Esta última
región es la que confiere la elasticidad característica a la elastina.
[editar] Síntesis
Su biosíntesis sigue la misma ruta que el colágeno; va desde el retículo endoplasmático,
se dirige al aparato de Golgi y de ahí hasta las vesículas secretoras. No sufre tantas
modificaciones postraduccionales como el colágeno, sin embargo, en la matriz
extracelular se da un cambio importante. Allí es captada por las microfibrillas
(constituidas por fibrilina 1 y fibrilina 2 básicamente) que se encuentran asociadas a la
lisil-oxidasa. Esta enzima se encargara de hidroxilar la lisina a alisina (utilizando
vitamina C como co-sustrato) permitiendo así el enlace entre los dominios alfa de la
proteína (un proceso similar al entrecruzamiento del colágeno). Las redes de fibras de
elastina se encuentran inicialmente en un estado "caótico". La tendencia a aumentar la
entropía hará que, al aplicar fuerza sobre ellas, se de un ordenamiento de dichas fibras
alcanzando una buen grado de compactación.
1. ↑ Sage EH & Gray WR 1977 Evolution of elastin and elastin structure, p 291. in;
Advances in Experimental Medicine and Biology, vol. 79 LB Sandberg & C
Franzblaw, eds) Plenum Press, NY & London
2. ↑ enlaceAdvances in protein chemistry,2005, 70;437
3. ↑ Prog. Polym. Sci. 2005, 30 (11), 1119-1145
4. he elastin protein is composed largely of two types of short segments that
alternate along the polypeptide chain: hydrophobic segments, which are
responsible for the elastic properties of the molecule; and alanine- and lysine-
rich α-helical segments, which form cross-links between adjacent molecules.
Each segment is encoded by a separate exon. There is still controversy, however,
concerning the conformation of elastin molecules in elastic fibers and how the
structure of these fibers accounts for their rubberlike properties. In one view, the
elastin polypeptide chain, like the polymer chains in ordinary rubber, adopts a
loose “random coil” conformation, and it is the random coil structure of the
component molecules cross-linked into the elastic fiber network that allows the
network to stretch and recoil like a rubber band (Figure 19-52
).
5. Elastin is the dominant extracellular matrix protein in arteries, comprising 50%
of the dry weight of the largest artery—the aorta. Mutations in the elastin gene
causing a deficiency of the protein in mice or humans result in narrowing of the
aorta or other arteries as a result of excessive proliferation of smooth muscle
cells in the arterial wall. Apparently, the normal elasticity of an artery is required
to restrain the proliferation of these cells.
6. Elastic fibers are not composed solely of elastin. The elastin core is covered with
a sheath of microfibrils, each of which has a diameter of about 10 nm.
Microfibrils are composed of a number of distinct glycoproteins, including the
large glycoprotein fibrillin, which binds to elastin and is essential for the
integrity of elastic fibers. Mutations in the fibrillin gene result in Marfan's
syndrome, a relatively common human genetic disease affecting connective
tissues that are rich in elastic fibers; in the most severely affected individuals,
the aorta is prone to rupture. Microfibrils are thought to be important in the
assembly of elastic fibers. They appear before elastin in developing tissues and
seem to form a scaffold on which the secreted elastin molecules are deposited.
As the elastin is deposited, the microfibrils become displaced to the periphery of
the growing fiber.
7. Many vertebrate tissues, such as skin, blood vessels, and lungs, need to be both
strong and elastic in order to function. A network of elastic fibers in the
extracellular matrix of these tissues gives them the required resilience so that
they can recoil after transient stretch (Figure 19-51
).
Elastic fibers are at least five times more extensible than a rubber band of the
same cross-sectional area. Long, inelastic collagen fibrils are interwoven with
the elastic fibers to limit the extent of stretching and prevent the tissue from
tearing.
8. The main component of elastic fibers is elastin, a highly hydrophobic protein
(about 750 amino acids long), which, like collagen, is unusually rich in proline
and glycine but, unlike collagen, is not glycosylated and contains some hydroxy-
proline but no hydroxylysine. Soluble tropoelastin (the biosynthetic precursor of
elastin) is secreted into the extracellular space and assembled into elastic fibers
close to the plasma membrane, generally in cell-surface infoldings. After
secretion, the tropoelastin molecules become highly cross-linked to one another,
generating an extensive network of elastin fibers and sheets. The cross-links are
formed between lysines by a mechanism similar to the one discussed earlier that
operates in cross-linking collagen molecules.
(A)Collagen is a triple helix formed by three extended protein chains that wrap
around one another (bottom). Many rodlike collagen molecules are cross-linked
together in the extracellular space to form unextendable collagen fibrils (top)
that have the tensile strength of steel. The striping on the collagen fibril is
caused by the regular repeating arrangement of the collagen molecules within
the fibril. (B) Elastin polypeptide chains are cross-linked together to form
rubberlike, elastic fibers. Each elastin molecule uncoils into a more extended
conformation when the fiber is stretched and recoils spontaneously as soon as
the stretching force is relaxed.
(B) Molecular Biology of the Cell, 4th edition
(C) Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts,
and Peter Walter
(D) New York: Garland Science; 2002.
(E) ISBN: 0-8153-3218-1
(F) ISBN: 0-8153-4072-9
(G)
A dense network of elastin and collagen fibers form the extracellular matrix
of elastic cartilage. These fibers of the ECM are intimately connected to the
plasma membrane of a chondrocyte. The membrane is supported by the
network of filaments from the actin cytoskeleton. [Courtesy of R. Mecham
and J. Heuser, Washington University School of Medicine.]
illiams Syndrome
[Williams-Beuren Syndrome]
PMID: 20301427
cam@unr.edu williams
Summary
Disease characteristics. Williams syndrome (WS) is characterized by cardiovascular
disease (elastin arteriopathy, peripheral pulmonary stenosis, supravalvular aortic
stenosis, hypertension), distinctive facies, connective tissue abnormalities, mental
retardation (usually mild), a specific cognitive profile, unique personality
characteristics, growth abnormalities, and endocrine abnormalities (hypercalcemia,
hypercalciuria, hypothyroidism, and early puberty). Feeding difficulties often lead to
failure to thrive in infancy. Hypotonia and hyperextensible joints can result in delayed
attainment of motor milestones.
http://www.ncbi.nlm.nih.gov/sites/entrez
Elastina Forma parte de las fibras elásticas. Las fibras elásticas permiten
que los tejidos recuperen su forma orginal tras una distensión mecánica.
El colágeno es una molécula proteica que forma fibras, las fibras colágenas.
Estas se encuentran en todos los organismos pluricelulares. Son secretadas
por las células del tejido conjuntivo como los fibroblastos, así como por otros
tipos celulares. Es el componente más abundante de la piel y de los huesos,
cubriendo un 25% de la masa total de proteínas en los mamíferos.
Características físico-químicas(daniel)
Las fibras colágenas son flexibles, pero ofrecen gran resistencia a la
tracción. El punto de ruptura de las fibras colágenas de los tendones
humanos se alcanza con una fuerza de varios cientos de kilogramos por
centímetro cuadrado. A esta tensión solamente se han alargado un pequeño
porcentaje de su longitud original.
Cuando el colágeno se desnaturaliza por ebullición y se deja enfriar,
manteniéndolo en una solución acuosa, se convierte en una sustancia bien
conocida, la gelatina
ELASTINA