Elastin Gene Expression

Foster, Jeffrey S.; Rich, Celeste B.; Karr, Stephen R.

doi:10.1016/b978-0-12-363710-9.50008-3

Cited by 15 publications

(5 citation statements)

References 47 publications

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“…It is expressed during a tightly controlled developmental window occurring from the late fetal period to early postnatal life (42)(43)(44). Inadequate deposition of elastin during this critical period cannot be compensated by later expression and individuals with elastin insufficiency are consequently at risk for significant pathology in their vascular and other elastic tissues.…”

Section: Discussionmentioning

confidence: 99%

Genetic Modifiers of Cardiovascular Phenotype Caused by Elastin Haploinsufficiency Act by Extrinsic Noncomplementation

Kozel

Knutsen

et al. 2011

Journal of Biological Chemistry

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Background: Variability in vascular pathology is associated with elastin loss-of-function mutations. Results: Quantitative trait loci and several candidate genes that modify vessel pathology were identified in a mouse model of elastin insufficiency. Conclusion: The effects of elastin insufficiency are determined by interactions between the primary elastin defect and unrelated secondary modifiers. Significance: Identification of modifier genes enhances our understanding of disease mechanisms associated with elastin mutations.

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Section: Discussionmentioning

confidence: 99%

Genetic Modifiers of Cardiovascular Phenotype Caused by Elastin Haploinsufficiency Act by Extrinsic Noncomplementation

Kozel

Knutsen

et al. 2011

Journal of Biological Chemistry

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“…It is generally accepted that tropoelastin represents the soluble precursor of insoluble elastin, and cell-free translation studies with elastin mRNA have demonstrated that the primary translation products are two polypeptides designated tropoelastin a and tropoelastin b, of M, approx. 73000 and 70000 respectively (for review see Foster et al, 1983). Much is known about the structure of tropoelastin and the extracellular modifications leading to the formation of the very hydrophobic, highly insoluble, cross-linked extracellular elastic fibre.…”

mentioning

confidence: 99%

Elastin biosynthesis in chick-embryo arteries. Studies on the intracellular site of synthesis of tropoelastin

Saunders¹,

Grant²

1984

Biochemical Journal

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Electrophoretic analyses of the products of cell-free translation of elastin mRNA isolated from 17-day chick-embryo thoracic arteries have demonstrated that the elastin mRNA codes for polypeptides that are slightly larger than the cellular tropoelastin polypeptides synthesized and secreted by matrix-free artery cells. Pulse-chase experiments with cells labelled with [3H]proline established that newly synthesized tropoelastin polypeptides were associated solely with membrane-bound particulate fractions. Cell-free translation of membrane-bound and free polyribosomes isolated from artery cells revealed that the tropoelastin mRNA was associated predominantly with the membrane-bound fraction. When rough-microsomal fractions, isolated from cells labelled with [3H]proline for 10 min, were treated with proteinases in the presence and in the absence of detergent, the nascent tropoelastin polypeptides were shown to be susceptible to proteolysis only when the integrity of the membranes was destroyed by detergent treatment. In similar experiments tropoelastin polypeptides synthesized by membrane-bound polyribosomes in the nuclease-treated reticulocyte lysate were also resistant to the proteolytic-enzyme treatment. The results suggest that tropoelastin polypeptides are synthesized on membrane-bound polyribosomes and discharged into the lumen of the endoplasmic reticulum with co-translational removal of a signal peptide.

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“…Elastin is important to the elasticity of blood vessels, ligaments, skin and lung (Sandberg et al, 1981;Foster et al, 1983;Rucker & Dubick, 1984). Despite the biological importance ofelastin, knowledge of the factors responsible for regulation of elastin expression is incomplete.…”

Section: Introductionmentioning

confidence: 99%

Tropoelastin production and tropoelastin messenger RNA activity. Relationship to copper and elastin cross-linking in chick aorta

Tinker

Geller

Romero

et al. 1986

Biochemical Journal

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The elastin content of the chick thoracic aorta increases 2--3-fold during the first 3 weeks post-hatching. The deposition of elastin requires the covalent cross-linking of tropoelastin by means of lysine-derived cross-links. This process is sensitive to dietary copper intake, since copper serves as cofactor for lysyl oxidase, the enzyme that catalyses the oxidative deamination of the lysine residues involved in cross-link formation. Disruption of cross-linking alters tissue concentrations of both elastin and tropoelastin and results in a net decrease in aortic elastin content. Autoregulation of tropoelastin synthesis by changes in the pool sizes of elastin or tropoelastin has been suggested as a possible mechanism for the diminished aortic elastin content. Consequently, dietary copper deficiency was induced to study the effect of impaired elastin cross-link formation on tropoelastin synthesis. Elastin in aortae from copper-deficient chicks was only two-thirds to one-half the amount measured in copper-supplemented chicks, whereas copper-deficient concentrations of tropoelastin in aorta were at least 5-fold higher than normal. In spite of these changes, however, increased amounts of tropoelastin, copper deficiency and decreased amounts of elastin did not influence the amounts of functional elastin mRNA in aorta. Likewise, the production of tropoelastin in aorta explants was the same whether the explants were taken from copper-sufficient or -deficient birds. The lower accumulation of elastin in aorta from copper-deficient chicks appeared to be due to extracellular proteolysis, rather than to a decrease in the rate of synthesis. Electrophoresis of aorta extracts, followed by immunological detection of tropoelastin-derived products, indicated degradation products in aortae from copper-deficient birds. In extracts of aortae from copper-sufficient chicks, tropoelastin was not degraded and appeared to be incorporated into elastin without further proteolytic processing.

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Elastin Gene Expression

Cited by 15 publications

References 47 publications

Genetic Modifiers of Cardiovascular Phenotype Caused by Elastin Haploinsufficiency Act by Extrinsic Noncomplementation

Genetic Modifiers of Cardiovascular Phenotype Caused by Elastin Haploinsufficiency Act by Extrinsic Noncomplementation

Elastin biosynthesis in chick-embryo arteries. Studies on the intracellular site of synthesis of tropoelastin

Tropoelastin production and tropoelastin messenger RNA activity. Relationship to copper and elastin cross-linking in chick aorta

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