Elastin
Section snippets
Elastic Fiber
The extracellular matrix imparts structural integrity on the tissues and organs of the body. It also acts as a dynamic modulator of a variety of biological processes. An important component of the extracellular matrix is the elastic fiber. Elastic fibers confer the properties of elastic recoil and resilience on all vertebrate elastic tissues, with the exception of lower vertebrates such as the lamprey (Debelle and Tamburro, 1999). Such properties are critical to the long-term function of these
Elastogenesis
In vivo elastin fiber formation requires the coordination of a number of important processes. These include the control of intracellular transcription and translation of tropoelastin, intracellular processing of the protein, secretion of the protein into the extracellular space, delivery of tropoelastin monomers to sites of elastogenesis, alignment of the monomers with previously accreted tropoelastin through associating microfibrillar proteins, and finally, the conversion to the insoluble
Physical Properties
Purified elastin is pale yellow and has a characteristic blue fluorescence in ultraviolet light (Partridge, 1962). When dry, it is a hard, brittle glassy solid. On wetting, it becomes flexible and elastic. The water content of elastin is affected by temperature; a large increase is seen in the swollen volume of elastin with decreasing temperature (Lillie and Gosline, 2002). At 36 °C, purified bovine ligamentum nuchae (which is primarily composed of elastin) contains 0.46 g water⧸g protein; at
Mechanism of Elasticity
The fundamental driving force behind the remarkable elastic properties of the elastin polymer is believed to be entropic, where stretching decreases the entropy of the system and elastic recoil is driven by a spontaneous return to maximum entropy. The precise molecular basis for elasticity has not been fully elucidated and a number of models exist. Two main categories of structure-function models have been proposed: those in which elastin is considered to be isotropic and devoid of structure,
Biomaterials
In healthy individuals, the mature elastin molecule is a stable, insoluble protein. Degradation of elastin is extremely slow due to the extensive crosslinking of tropoelastin within the elastic fiber. However, with aging, injury, or the onset of a variety of acquired diseases, the degradation and excessive or aberrant remodeling of elastic fibers becomes apparent in arteries, lung, skin, and ligament (Osakabe et al., 2001). The correct assembly of the elastin polymer is critical for proper
Acknowledgements
ASW is a recipient of grants from the Australian Research Council and the University of Sydney Vice Chancellor's Development Fund.
References (152)
- et al.
Characterization of the complete human elastin gene. Delineation of unusual features in the 5′-flanking region
J. Biol. Chem.
(1989) - et al.
New bioactivation mode for vascular prostheses made of Dacron polyester
Biomaterials
(1995) - et al.
Relevance of aggregation properties of tropoelastin to the assembly and structure of elastic fibers
J. Ultrastruct. Molec. Struct. Res.
(1986) - et al.
Identification of an elastin cross-linking domain that joins three peptide chains. Possible role in nucleated assembly
J. Biol. Chem.
(1995) - et al.
In-situ self-assembling protein polymer gel systems for administration, delivery, and release of drugs
J. Control. Release
(1998) - et al.
Targeted drug delivery by thermally responsive polymers
Adv. Drug Deliver. Rev.
(2002) - et al.
Insulin-like growth factor-I regulates transcription of the elastin gene through a putative retinoblastoma control element. A role for Sp3 acting as a repressor of elastin gene transcription
J. Biol. Chem.
(1996) - et al.
Fibrillin immunoreactive fibers constitute a unique network in the human dermis: Immunohistochemical comparison of the distributions of fibrillin, vitronectin, amyloid P component, and orcein stainable structures in normal skin and elastosis
J. Invest. Dermatol.
(1990) - et al.
Bovine elastin and kappa-elastin secondary structure determination by optical spectroscopies
J. Biol. Chem.
(1995) - et al.
Elastin: Molecular description and function
Int. J. Biochem. Cell Biol.
(1999)
The role of NF-1 factors in regulation of elastin gene transcription
Matrix Biol.
Elastin-derived protein coating onto poly(ethylene terephthalate). Technical, microstructural and biological studies
Biomaterials
Function-structure relationship of elastic arteries in evolution: From microfibrils to elastin and elastic fibers
Pathol. Biol.
Tissue engineering: A 21st century solution to surgical reconstruction
Ann. Thor. Surg.
The major antigen of elastin-associated microfibrils is a 31-kDa glycoprotein
J. Biol. Chem.
The physical properties of elastic tissue
Int. Rev. Connect. Tissue Res.
The ultrastructural organization of elastin
J. Ultrastruct. Res.
In vitro processing of tropoelastin: Investigation of a possible transport function associated with the carboxy-terminal domain
Biochem. Biophys. Res. Comm.
Alternative splicing of rat tropoelastin mRNA is tissue-specific and developmentally regulated
Matrix
Recycling of the 67-kDa elastin binding protein in arterial myocytes is imperative for secretion of tropoelastin
Exp. Cell Res.
Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks
J. Biol. Chem.
Production of recombinant human tropoelastin: Characterization and demonstration of immunologic and chemotactic activity
Arch. Biochem. Biophys.
Extracellular matrix remodeling in the vascular wall
Pathol. Biol.
Domain 26 of tropoelastin plays a dominant role in association by coacervation
J. Biol. Chem.
Lysyl oxidase: Preparation and role in elastin biosynthesis
Methods Enzymol.
Isolation of active site peptides of lysyl oxidase
Methods Enzymol.
Tumor necrosis factor-alpha down-regulates human elastin gene expression. Evidence for the role of AP-1 in the suppression of promoter activity
J. Biol. Chem.
Deposition of tropoelastin into the extracellular matrix requires a competent elastic fiber scaffold but not live cells
Matrix Biol.
The effect of elastin damage on the mechanics of the aortic valve
J. Biomech.
The elastogenic effect of recombinant transforming growth factor-beta on porcine aortic smooth muscle cells
Biochem. Biophys. Res. Comm.
Highly swelling hydrogels from ordered galactose-based polyacrylates
Biomaterials
Total synthesis and expression in Escherichia coli of a gene encoding human tropoelastin
Gene.
Human recombinant interleukin-1 beta up-regulates elastin gene expression in dermal fibroblasts. Evidence for transcriptional regulation in vitro and in vivo
J. Biol. Chem.
Genetic disorders of the elastic fiber system
Matrix Biol.
Synthetic elastin hydrogels derived from massive elastic assemblies of self-organized human protein monomers
Biomaterials
Biomolecule-sensitive hydrogels
Adv. Drug Deliv. Rev.
Self-assembly and supramolecular organization of EMILIN
J. Biol. Chem.
Structural changes and facilitated association of tropoelastin
Archi. Biochem. Biophys.
Lysyl oxidase-like and lysyl oxidase are present in the dermis and epidermis of a skin equivalent and in human skin and are associated to elastic fibers
J. Invest. Dermatol.
The ultrastructure of elastin revealed by freeze-fracture electron microscopy
Micron.
Genomic organization of mouse and human 65 kDa FK506-binding protein genes and evolution of the FKBP multigene family
Genomics
Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-like properties
Biopolymers
Characterization of a genetically engineered elastin-like polypeptide for cartilaginous tissue repair
Biomacromolecules
Stretch affects phenotype and proliferation of vascular smooth muscle cells
Mol. Cell. Biochem.
Spectroscopic evidence revealing polyproline II structure in hydrophobic, putatively elastomeric sequences encoded by specific exons of human tropoelastin
Biopolymers
Emilin, a component of elastic fibers preferentially located at the elastin-microfibrils interface
J. Cell Biol.
Functional domains on elastin and MAGP involved in elastic fiber assembly
Biochem. J.
Heparan sulfate depletion within pulmonary fibroblasts: Implications for elastogenesis and repair
J. Cell. Physiol.
Basic fibroblast growth factor decreases elastin gene transcription in aortic smooth muscle cells
J. Cell. Biochem.
Microfibril-associated glycoprotein-1 binding to tropoelastin: Multiple binding sites and the role of divalent cations
Eur. J. Biochem.
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