[37] Production and isolation of soluble elastin from copper-deficient swine

Sandberg, Lawrence B.; Wolt, Terril B.

doi:10.1016/0076-6879(82)82094-6

Cited by 16 publications

(18 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Tropoelastin can be produced by two methods; either by isolation from copper-defi cient animals [115,116] or by molecular biological techniques [121]. The latter is preferred since isolation from copper-defi cient animals is an animal-unfriendly method with low yield.…”

Section: Tropoelastinmentioning

confidence: 99%

Elastin as a biomaterial for tissue engineering

et al. 2007

View full text Add to dashboard Cite

Section: Tropoelastinmentioning

confidence: 99%

Elastin as a biomaterial for tissue engineering

et al. 2007

View full text Add to dashboard Cite

“…Traditionally, this has been accomplished by inhibiting lysyl oxidase through feeding animals (mostly newborn pigs and chickens) a diet deficient in copper (a critical cofactor for lysyl oxidase activity) [55,56] or a diet containing the lysyl oxidase inhibitors β-aminopropionitrile (BAPN) or α-aminoacetonitrile (AAN) [57,58]. Tropoelastin is then extracted using either neutral salt [56,57] or acidic [55] buffers. Because whole animal approaches have been largely superseded by in vitro methods or recombinant expression techniques, the interested reader is referred to the primary literature cited above.…”

Section: Purification Of Tropoelastin From Animal Tissuesmentioning

confidence: 99%

“…Following overnight stirring at 4°C, insoluble material is removed by centrifugation at 16,000 × g for 30 min at 4°C and discarded. Tropoelastin is extracted from the supernatant by the drop-wise addition (on ice) of 1.5 volumes of n-propanol and 2.5 volumes of n-butanol to the stirred solution [55,56]. The precipitate that forms during this step is removed by centrifugation and the supernatant is flash evaporated to dryness on a rotary evaporator at 40°C.…”

Section: In Vitro Technique For Isolating Tropoelastin From Viable Anmentioning

confidence: 99%

Methods in elastic tissue biology: Elastin isolation and purification

Mecham

2008

Methods

View full text Add to dashboard Cite

Elastin provides recoil to tissues subjected to repeated stretch, such as blood vessels and the lung. It is encoded by a single gene in mammals and is secreted as a 60-70 kDa monomer call tropoelastin. The functional form of the protein is that of a large, highly crosslinked polymer that organizes as sheets or fibers in the extracellular matrix. Purification of mature, crosslinked elastin is problematic because its insolubility precludes its isolation using standard wet-chemistry techniques. Instead, relatively harsh experimental approaches designed to remove non-elastin 'contaminates' are employed to generate an insoluble product that has the amino acid composition expected of elastin. Although soluble, tropoelastin also presents problems for isolation and purification. The protein's extreme stickiness and susceptibility to proteolysis requires careful attention during purification and in tropoelastin-based assays. This article describes the most common approaches for purification of insoluble elastin and tropoelastin. It also addresses key aspects of studying tropoelastin production in cultured cells, where elastin expression is highly dependent upon cell type, culture conditions, and passage number.

show abstract

“…In general, the results from gravimetric methods for quantifying elastin are most easily interpreted when One of the precursors to the elastin component of elastic fibers has been designated as tropoelastin (5,10,40). Tropoelastin appears to be secreted from cells in the form of a 72,000 molecular weight protein (5,10,11,15,41).…”

Section: Components Of Elastic Fiber: Isolation and Composition Of Elmentioning

confidence: 99%

Elastin metabolism and chemistry: potential roles in lung development and structure.

Rucker¹,

Dubick²

1984

Environ Health Perspect

View full text Add to dashboard Cite

Elastic fibers are important for elasticity and extensibility of lung tissue. In the developing lung, elastic fibers appear in greatest numbers during the process or period of alveolarization. A variety of mesenchymal cells in lung appear responsible for elastin synthesis. Elastin is a novel protein both from the standpoint of its processing into elastic fibers and chemical properties. For example, elastin undergoes posttranslational modification before its assembly into fibers. These steps include limited proteolysis, hydroxylation of prolyl residues and the oxidative deamination of lysyl residues prior to their incorporation into the crosslinks that covalently bond together polypeptide chains of elastin. The crosslinking amino acids include lysinonorleucine, merodesmosine and desmosine isomers. A key enzyme that controls this process is lysyl oxidase. Lysyl oxidase is a copper metalloprotein whose activity is responsive to and modulated by environmental insults, nutrition deficiencies and the administration of various pharmacological agents. Regarding chemical properties, elastin is one of the most apolar proteins secreted by mammalian cells. Moreover, elastin is one of the most long-lived proteins secreted into the extracellular matrix. In relationship to its processing into elastic fibers and chemical properties, details related to major aspects of elastin metabolism as well as speculation on its potential as a factor in lung development and disease are discussed.

show abstract

[37] Production and isolation of soluble elastin from copper-deficient swine

Cited by 16 publications

References 6 publications

Elastin as a biomaterial for tissue engineering

Elastin as a biomaterial for tissue engineering

Methods in elastic tissue biology: Elastin isolation and purification

Elastin metabolism and chemistry: potential roles in lung development and structure.

Contact Info

Product

Resources

About