Chemical compositions of elastins isolated from aortas and pulmonary tissues of humans of different ages

John, Rhys; Thomas, J. D. R.

doi:10.1042/bj1270261

Cited by 137 publications

(39 citation statements)

References 20 publications

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“…The composition of pulmonary alveolar septal elastin at term resembles that of the adult ewe. The same pattern also appears to be true for the human as well in which the process may continue for as long as 7 years after birth (6,25,26,54,73,(101)(102)(103).…”

Section: Mammalian Lungmentioning

confidence: 61%

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

Rucker¹,

Dubick²

1984

Environ Health Perspect

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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.

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Section: Mammalian Lungmentioning

confidence: 61%

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

Rucker¹,

Dubick²

1984

Environ Health Perspect

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“…The AA content of elastin protein cultured in the presence of elastogenic cues and in their absence was dominated by the nonpolar AAs, glycine, alanine, proline, and valine (65% vs. 63.5%, respectively), similar to that described in literature (*71%). 36,37 Desmosine (Des) and isodesmosine (Ide), vital but minor constituents of crosslinked elastin protein, 38 were barely resolved in the present analysis, while hydroxyproline (OH-Pro), which is present in elastin protein as a minor constituent (<3%), was sparingly detected (0.5%) as expected.…”

Section: Aa Analysis Of Elastinmentioning

confidence: 67%

Transforming Growth Factor Beta 1 and Hyaluronan Oligomers Synergistically Enhance Elastin Matrix Regeneration by Vascular Smooth Muscle Cells

Kothapalli

Taylor

Smolenski

et al. 2009

Tissue Engineering Part A

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Elastin is a vital structural and regulatory matrix protein that plays an important role in conferring elasticity to blood vessel wall. Previous tissue engineering approaches to regenerate elastin in situ or within tissue engineering constructs are curtailed by innate poor elastin synthesis potential by adult vascular smooth muscle cells (SMCs). Currently, we seek to develop cellular cues to enhance tropoelastin synthesis and improve elastin matrix yield, stability, and ultrastructure. Our earlier studies attest to the elastogenic utility of hyaluronan (HA)-based cellular cues, though their effects are fragment size dependent and dose dependent, with HA oligomers deemed most elastogenic. We presently show transforming growth factor beta 1 (TGF-b1) and HA oligomers, when provided concurrently, to synergistically and dramatically improve elastin matrix regeneration by adult vascular SMCs. Together, these cues suppress SMC proliferation, enhance synthesis of tropoelastin (8-fold) and matrix elastin protein (5.5-fold), and also improve matrix elastin yield (45% of total elastin vs. 10% for nonadditive controls), possibly by more efficient recruitment of tropoelastin for crosslinking. The density of desmosine crosslinks within the elastin matrix was itself attenuated, although the cues together modestly increased production and activity of the elastin crosslinking enzyme, lysyl oxidase. TGF-b1 and HA oligomers together induced much greater assembly of mature elastin fibers than they did separately, and did not induce matrix calcification. The present outcomes might be great utility to therapeutic regeneration of elastin matrix networks in situ within elastin-compromised vessels, and within tissue-engineered vascular graft replacements.

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“…More than 10 different procedures have been published for purifying elastin (e.g. see [11][12][13][14][15][16][17][18][19][20][21] and all have their relative advantages and disadvantages. Other than the hot alkali and autoclaving protocols, all other procedures employ chaotropic agents, buffers with reducing agents, and protease treatment to remove unwanted contaminants.…”

Section: Purification Of Insoluble Elastinmentioning

confidence: 99%

Methods in elastic tissue biology: Elastin isolation and purification

Mecham

2008

Methods

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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.

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Chemical compositions of elastins isolated from aortas and pulmonary tissues of humans of different ages

Cited by 137 publications

References 20 publications

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

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

Transforming Growth Factor Beta 1 and Hyaluronan Oligomers Synergistically Enhance Elastin Matrix Regeneration by Vascular Smooth Muscle Cells

Methods in elastic tissue biology: Elastin isolation and purification

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