Electrospun elastin and collagen nanofibers and their application as biomaterials
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Biomedicine
Electrospinning
Biomimetics
Matrix (chemical analysis)
Fibrillin
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The earliest scientific journals on biomedicine began publication in the 50s and their authors addressed the application of biology to medicine. More recently, biochemistry and biomedical engineering questions have figured more prominently. This trend is discussed in a survey of the topics appearing in the Journal of Applied Biomedicine. Pharmacological and toxicological articles have been popular over the long term and the neurosciences, chronomedicine, molecular and cell biomedicine have also been very important. The role of computational biomedicine and nanomedicine has received increasing attention as has the part which applied biomedicine can play in the enhancement of the general economy.
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ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTElastin mRNA levels and insoluble elastin accumulation in neonatal rat smooth muscle cell culturesLeesa M. Barone, B. Leslie Wolfe, Barbara Faris, and Carl FranzblauCite this: Biochemistry 1988, 27, 9, 3175–3182Publication Date (Print):May 3, 1988Publication History Published online1 May 2002Published inissue 3 May 1988https://pubs.acs.org/doi/10.1021/bi00409a008https://doi.org/10.1021/bi00409a008research-articleACS PublicationsRequest reuse permissionsArticle Views59Altmetric-Citations18LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
Tropoelastin
Northern blot
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Thoracic aorta
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It is generally accepted that, once laid down in the extracellular matrix, elastin turns over only very slowly if at all. However, much of the evidence for minimal turnover of elastin comes from aortic tissue. In this study we have compared the relative synthesis rates of elastin and collagen with their relative accumulation rates in segments of aorta (AO), pulmonary artery (PA), and pulmonary vein (PV) of young, growing pigs. While rates of elastin synthesis are comparable in the AO and PA, the PA accumulates only 33% of the elastin deposited in the AO. Similarly, while the rate of elastin synthesis in the PV is 60% of that in the AO, accumulation of elastin is only 20% of that in the AO. Similar discrepancies between collagen synthesis and accumulation were seen among these three vessels. These data suggest that, at least in growing animals, the efficiency of permanent incorporation of elastin and collagen into the extracellular matrix may be an important factor in determining the final contents of these connective tissue proteins in vascular tissues.
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Abstract —The elastin content in the thoracic aorta of male Brown-Norway (BN) rats is 31.4±1.2% (dry weight), whereas that of male LOU rats is 37.2±1.0%. A similar difference in the elastin content of the thoracic aorta is also observed in female animals. Furthermore, in the thoracic aorta of young, growing rats as well as in cultured aortic smooth muscle cells, the steady-state level of elastin mRNA is significantly lower in the BN than in the LOU strain. These results suggested that 1 or more genes control the elastin mRNA level and the elastin content in the aortas of BN and LOU rats. A possible relationship between a polymorphism in the elastin gene and the elastin content of the aorta was tested. For this purpose, the aortic elastin content was measured in F 1 and F 2 generations bred from LOU and BN rats and was compared with that of the F 0 (parental) generation. A polymorphic marker located in intron 25 of the elastin gene has been used to genotype the F 2 rats. The degree of genetic determination of aortic elastin content was estimated to be 73% in the F 2 cohort, but the elastin locus accounts for only 3.9% of the total variance in aortic elastin content. Other genes are thus responsible for the major part of the observed interstrain difference by regulating the transcription of the gene, the stability of elastin mRNA, and/or posttranslational events.
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The relative levels of elastin-specific mRNA were used as a measure of tropoelastin expression in uteri from pregnant Sprague-Dawley rats. The levels of elastin-specific mRNA were also correlated with values for net tropoelastin production and net deposition of mature, crosslinked elastin. The total content of uterine elastin increased throughout gestation, reaching maximal levels at Day 19 of gestation, which were three times those of nongravid tissue. Following involution, the elastin content decreased rapidly to near baseline values by 5 days postpartum. The content of soluble elastin, estimated using an enzyme-linked immunosorbent assay, paralleled in part the increase in elastin deposition and elastin mRNA levels. Uterine elastin metabolism appears to be unlike that in other elastic tissues, e.g., lung and large blood vessels. In most elastin containing tissues, the protein is synthesized during discrete developmental periods and is not readily degraded. However, uterine elastin is continuously expressed, and appears to be in a continual cycle of degradation and replacement.
Tropoelastin
Desmosine
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The presence of elastin layers in the aortic walls of twelve human fetuses was confirmed with scanning electron microscope pictures after hot alkali treatment and histochemical examination. In addition, the number of elastin layers in aortic walls of 5 different segments were compared in fetuses of varying ages. Aldehyde fuchsin stained slides of elastin ascending aortas showed a range between 27 and 55 layers of elastin in fetuses of 8 weeks to 32 weeks. However, in the lower abdominal aortas, elastin layers decreased from 28 to only 3 layers for fetuses of the same age. Furthermore, as elastin layers decreased from ascending aorta to abdominal aorta with the progression of fetal life, similar changes in the elastin lamellae were observed. These results suggest that while aortas grow rapidly in length, the medial elastin thickens slowly, perhaps due to slow development of hydrodynamic forces and pressures. Also the adventitial elastin appears to lose out gradually along the length from ascending aorta to abdominal aorta.
Abdominal aorta
Elastic fiber
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Elastin is a key structural protein found in the extracellular matrix (ECM) of all mammals. As the dominant part of the elastic fiber, elastin confers the mechanical properties of resilience and elasticity essential to the function of elastic tissues. Elastin interacts with cells through specific biochemical mechanisms. This chapter considers the (1) mechanical and biochemical roles of elastin in elastic tissues and the subsequent disease phenotypes that result from the degradation and loss of elastin, (2) development and success of current elastin based biomaterials including sources of elastin for tissue engineering and their application, and (3) vascular constructs that our laboratory has developed from recombinant human tropoelastin. These constructs mimic the physical and biochemical properties of native elastin.
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