Elastin
Elastin is a protein encoded by the ELN gene in humans and several other animals. Elastin is a key component in the extracellular matrix of gnathostomes (jawed vertebrates).[5] It is highly elastic and present in connective tissue of the body to resume its shape after stretching or contracting.[6] Elastin helps skin return to its original position whence poked or pinched. Elastin is also in important load-bearing tissue of vertebrates and used in places where storage of mechanical energy is required.[7]
Function
[edit]The ELN gene encodes a protein that is one of the two components of elastic fibers. The encoded protein is rich in hydrophobic amino acids such as glycine and proline, which form mobile hydrophobic regions bounded by crosslinks between lysine residues. Multiple transcript variants encoding different isoforms have been found for this gene.[8] Elastin's soluble precursor is tropoelastin.[9]
Mechanism of elastic recoil
[edit]The characterization of disorder is consistent with an entropy-driven mechanism of elastic recoil. It is concluded that conformational disorder is a constitutive feature of elastin structure and function.[10]
Clinical significance
[edit]Deletions and mutations in this gene are associated with supravalvular aortic stenosis (SVAS) and the autosomal dominant cutis laxa.[8] Other associated defects in elastin include Marfan syndrome, emphysema caused by α1-antitrypsin deficiency, atherosclerosis, Buschke–Ollendorff syndrome, Menkes syndrome, pseudoxanthoma elasticum, and Williams syndrome.[11]
Elastosis
[edit]Elastosis is the buildup of elastin in tissues, and is a form of degenerative disease. There are a multitude of causes, but the most commons cause is actinic elastosis of the skin, also known as solar elastosis, which is caused by prolonged and excessive sun exposure, a process known as photoaging. Uncommon causes of skin elastosis include elastosis perforans serpiginosa, perforating calcific elastosis and linear focal elastosis.[12]
| Condition | Distinctive features | Histopathology |
|---|---|---|
| Actinic elastosis (most common, also called solar elastosis) |
Elastin replacing collagen fibers of the papillary dermis and reticular dermis |  |
| Elastosis perforans serpiginosa | Degenerated elastic fibers and transepidermal perforating canals (arrow in image points at one of them)[13] |  |
| Perforating calcific elastosis | Clumping of short elastic fibers in the dermis.[13] |  |
| Linear focal elastosis | Accumulation of fragmented elastotic material within the papillary dermis and transcutaneous elimination of elastotic fibers.[13] |  |
Composition
[edit]
In the body, elastin is usually associated with other proteins in connective tissues. Elastic fiber in the body is a mixture of amorphous elastin and fibrous fibrillin. Both components are primarily made of smaller amino acids such as glycine, valine, alanine, and proline.[11][14] The total elastin ranges from 58 to 75% of the weight of the dry defatted artery in normal canine arteries.[15] Comparison between fresh and digested tissues shows that, at 35% strain, a minimum of 48% of the arterial load is carried by elastin, and a minimum of 43% of the change in stiffness of arterial tissue is due to the change in elastin stiffness.[16]
Tissue distribution
[edit]Elastin serves an important function in arteries as a medium for pressure wave propagation to help blood flow and is particularly abundant in large elastic blood vessels such as the aorta. Elastin is also very important in the lungs, elastic ligaments, elastic cartilage, the skin, and the bladder. It is present in jawed vertebrates.[17]
Characteristics
[edit]Elastin is a very long-lived protein, with a half-life of over 78 years in humans.[18] However, its long lifespan does not imply that its functional properties remain unchanged throughout life.
In human skin, ageing is associated with changes in the amount, organisation and integrity of dermal elastic fibres. An in vivo multiphoton tomography study reported age-related reductions in the measured elastin and collagen content of the human dermis.[19]
More recent three-dimensional imaging of human dermal elastin has shown that the number of elastic fibres decreases with age and that the remaining network becomes more fragmented and less interconnected. Finite-element modelling based on these structural observations associated age-related changes in elastin-fibre architecture with reduced skin firmness.[20]
Although elastin is exceptionally long-lived, its structure and function can change with aging. In human skin, aging has been associated with reductions and structural alterations in dermal elastin and elastic fibers. Imaging studies have reported age-related changes in the amount and organization of dermal elastin, including fragmentation and reduced connectivity of elastic-fiber networks. These changes may contribute to the decline in skin elasticity and firmness associated with aging.
Clinical research
[edit]The feasibility of using recombinant human tropoelastin to promote elastin-fibre production and improve skin flexibility in wounds and scars has been studied.[22][23] Although new elastin fibres were observed following the administration of recombinant human tropoelastin into fresh wounds, the treatment did not result in significant improvements in scar appearance or flexibility.[22][23]
Another line of research has investigated stimulation of endogenous elastin production in the skin. In an in vitro study, an amino acid–copper mixture increased elastin- and type I collagen-related gene expression and protein production in cultured human dermal fibroblasts compared with copper or the amino acid mixture alone.[24]
A subsequent open-label, single-centre clinical study evaluated a skin-booster formulation containing amino acids, copper sulfate and non-cross-linked hyaluronic acid, marketed as Elastic Lab. Five participants received four facial treatments at one-week intervals, and the outcomes were assessed one week after the final treatment. Instrumentally measured skin elasticity increased by 23.4% from baseline, while skin thickness and density increased by 7.3% and 12.5%, respectively. Improvements in skin hydration and periocular wrinkle depth were also reported.[25] The study did not directly measure newly synthesised or deposited elastin fibres. Its small sample size and uncontrolled design limit the conclusions that can be drawn, and larger controlled studies with direct tissue-based measurements are required to determine whether stimulation of elastin biosynthesis produces sustained improvements in skin elasticity.[25]
A different approach has investigated stimulation of endogenous elastin production in the skin. An in vitro study using cultured human dermal fibroblasts reported that an amino acid–copper mixture increased elastin- and type I collagen-related gene expression and protein production compared with copper or the amino-acid mixture alone. A subsequent open-label, single-center clinical study evaluated a skin-booster formulation containing amino acids, copper sulfate, and non-cross-linked hyaluronic acid (Elastic Lab). In five participants receiving four weekly treatments, the study reported increases in instrumentally measured skin elasticity, as well as skin thickness and density. The study did not directly measure newly deposited elastin fibers, and its small, uncontrolled design limits the conclusions that can be drawn; larger controlled studies are needed to determine whether stimulation of elastin biosynthesis produces sustained improvements in skin elasticity.
Biosynthesis
[edit]The formation of mature elastic fibers, known as elastogenesis, requires the coordinated production and assembly of tropoelastin with a fibrillin-rich microfibrillar scaffold. Tropoelastin is secreted by elastogenic cells, including fibroblasts and vascular smooth-muscle cells, and undergoes coacervation before being deposited onto microfibrils. Proteins including fibulin-4, fibulin-5, and latent transforming growth factor beta-binding protein 4 participate in the organization and stabilization of the developing elastic-fiber matrix.[26][27]
Tropoelastin precursors
[edit]Elastin is made by linking together many small soluble precursor tropoelastin protein molecules (50-70 kDa), to make the final massive, insoluble, durable complex. The unlinked tropoelastin molecules are not normally available in the cell, since they become crosslinked into elastin fibres immediately after their synthesis by the cell and export into the extracellular matrix.[28]
Each tropoelastin consists of a string of 36 small domains, each weighing about 2 kDa in a random coil conformation. The protein consists of alternating hydrophobic and hydrophilic domains, which are encoded by separate exons, so that the domain structure of tropoelastin reflects the exon organization of the gene. The hydrophilic domains contain Lys-Ala (KA) and Lys-Pro (KP) motifs that are involved in crosslinking during the formation of mature elastin. In the KA domains, lysine residues occur as pairs or triplets separated by two or three alanine residues (e.g. AAAKAAKAA) whereas in KP domains the lysine residues are separated mainly by proline residues (e.g. KPLKP). The hydrophobic domains of tropoelastin are enriched in non-polar amino acids, particularly glycine, valine, proline, and alanine, whereas its lysine-rich domains provide sites for enzymatic cross-linking during the formation of mature elastin.[26]
Aggregation
[edit]Tropoelastin aggregates at physiological temperature due to interactions between hydrophobic domains in a process called coacervation. This process is reversible and thermodynamically controlled and does not require protein cleavage. The coacervate is made insoluble by irreversible crosslinking.
Crosslinking
[edit]To make mature elastin fibres, tropoelastin molecules are cross-linked through their lysine residues to form desmosine and isodesmosine cross-links. The enzyme responsible for initiating this cross-linking process is lysyl oxidase, and the resulting cross-links are formed through reactions described as an in vivo Chichibabin pyridine synthesis.[29] Copper is an essential cofactor for lysyl oxidase activity, which contributes to the maturation and cross-linking of both elastin and collagen.[30][27]Based on this biochemical mechanism, some experimental formulations have combined copper with amino acids abundant in tropoelastin, including glycine, valine, alanine, and proline, to investigate their effects on dermal extracellular-matrix protein production.[30] An in vitro study using cultured human dermal fibroblasts found that an amino acid–copper mixture increased elastin- and type I collagen-related gene expression and protein production compared with treatment using copper or the amino-acid mixture alone.[30] This approach was subsequently evaluated in a patented skin-booster formulation containing these amino acids, copper sulfate, and non-cross-linked hyaluronic acid (trade name: Elastic Lab). In a small, uncontrolled, open-label study involving five participants, four weekly treatments were followed by reported increases in instrumentally measured skin elasticity, thickness, and density; however, the study did not directly measure new elastin deposition, and larger controlled studies are required to confirm the findings.[31] Lysyl oxidase requires copper as a cofactor for its activity and is involved in the cross-linking and maturation of elastin and collagen. Experimental studies have therefore investigated whether copper-containing amino acid mixtures can influence extracellular-matrix protein production by dermal fibroblasts. In cultured human dermal fibroblasts, an amino acid–copper mixture increased elastin- and type I collagen-related gene expression and protein production compared with the individual components alone.
Molecular biology
[edit].png)
In mammals, the genome only contains one gene for tropoelastin, called ELN. The human ELN gene is a 45 kb segment on chromosome 7, and has 34 exons interrupted by almost 700 introns, with the first exon being a signal peptide assigning its extracellular localization. The large number of introns suggests that genetic recombination may contribute to the instability of the gene, leading to diseases such as SVAS. The expression of tropoelastin mRNA is highly regulated under at least eight different transcription start sites.
Tissue specific variants of elastin are produced by alternative splicing of the tropoelastin gene. There are at least 11 known human tropoelastin isoforms. These isoforms are under developmental regulation, however there are minimal differences among tissues at the same developmental stage.[11]
See also
[edit]- Cutis laxa
- Elastic fibers
- Elastin receptor
- Resilin: an invertebrate protein
- Williams syndrome
References
[edit]- 1 2 3 GRCh38: Ensembl release 89: ENSG00000049540 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029675 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Mithieux SM, Weiss AS (2005). "Elastin". Advances in Protein Chemistry. 70: 437–461. doi:10.1016/S0065-3233(05)70013-9. ISBN 978-0-12-034270-9. PMID 15837523.
{{cite journal}}: CS1 maint: periodical has ISBN (link) - ↑ Vindin H, Mithieux SM, Weiss AS (November 2019). "Elastin architecture". Matrix Biology. 84: 4–16. doi:10.1016/j.matbio.2019.07.005. PMID 31301399. S2CID 196458819.
- ↑ Curran ME, Atkinson DL, Ewart AK, Morris CA, Leppert MF, Keating MT (April 1993). "The elastin gene is disrupted by a translocation associated with supravalvular aortic stenosis". Cell. 73 (1): 159–168. doi:10.1016/0092-8674(93)90168-P. PMID 8096434. S2CID 8274849.
- 1 2 "Entrez Gene: elastin".
- ↑ "Elastin (ELN)". Archived from the original on 13 March 2017. Retrieved 31 October 2011.
- ↑ Muiznieks LD, Weiss AS, Keeley FW (April 2010). "Structural disorder and dynamics of elastin". Biochemistry and Cell Biology. 88 (2): 239–250. Bibcode:2010BCB....88..161M. doi:10.1139/o09-161. PMID 20453927.
- 1 2 3 Vrhovski B, Weiss AS (November 1998). "Biochemistry of tropoelastin". European Journal of Biochemistry. 258 (1): 1–18. doi:10.1046/j.1432-1327.1998.2580001.x. PMID 9851686.
- ↑ Wright B (26 October 2023). "Elastosis". DermNet NZ.
- 1 2 3 Hosen MJ, Lamoen A, De Paepe A, Vanakker OM (2012). "Histopathology of pseudoxanthoma elasticum and related disorders: histological hallmarks and diagnostic clues". Scientifica. 2012 598262. doi:10.6064/2012/598262. PMC 3820553. PMID 24278718.
-Creative Commons Attribution 3.0 Unported license - ↑ Kielty CM, Sherratt MJ, Shuttleworth CA (July 2002). "Elastic fibres". Journal of Cell Science. 115 (Pt 14): 2817–2828. doi:10.1242/jcs.115.14.2817. PMID 12082143.
- ↑ Fischer GM, Llaurado JG (August 1966). "Collagen and elastin content in canine arteries selected from functionally different vascular beds". Circulation Research. 19 (2): 394–399. doi:10.1161/01.res.19.2.394. PMID 5914851.
- ↑ Lammers SR, Kao PH, Qi HJ, Hunter K, Lanning C, Albietz J, et al. (October 2008). "Changes in the structure-function relationship of elastin and its impact on the proximal pulmonary arterial mechanics of hypertensive calves". American Journal of Physiology. Heart and Circulatory Physiology. 295 (4): H1451–H1459. doi:10.1152/ajpheart.00127.2008. PMC 2593497. PMID 18660454.
- ↑ Sage EH, Gray WR (1977). "Evolution of Elastin Structure". Elastin and Elastic Tissue. Advances in Experimental Medicine and Biology. Vol. 79. pp. 291–312. doi:10.1007/978-1-4684-9093-0_27. ISBN 978-1-4684-9095-4. PMID 868643.
- ↑ Toyama BH, Hetzer MW (January 2013). "Protein homeostasis: live long, won't prosper". Nature Reviews Molecular Cell Biology. 14 (1): 55–61. doi:10.1038/nrm3496. PMC 3570024. PMID 23258296.
- ↑ Pittet, J.C.; Freis, O.; Vazquez-Duchêne, M.D.; Périé, G.; Pauly, G. (2014). "Evaluation of Elastin/Collagen Content in Human Dermis In-Vivo by Multiphoton Tomography—Variation with Depth and Correlation with Aging". Cosmetics. 1 (3): 211–221. doi:10.3390/cosmetics1030211.
- ↑ Jiang, Fei; Tohgasaki, Takeshi; Kami, Mayuko (2025). "Influence of aging on dermal elastin fiber architecture and skin firmness assessed by finite element modeling". Scientific Reports. 15 (1) 28598. Bibcode:2025NatSR..1528598J. doi:10.1038/s41598-025-14393-2. PMC 12325628. PMID 40764373.
- ↑ Pena, A.-M.; Baldeweck, T.; Decencière, E.; Koudoro, S.; Victorin, S.; Raynaud, E.; Ngo, B.; Bastien, P.; Brizion, S.; Tancrède-Bohin, E. (2022). "In vivo multiphoton multiparametric 3D quantification of human skin aging on forearm and face". Scientific Reports. 12 (1) 14863. Bibcode:2022NatSR..1214863P. doi:10.1038/s41598-022-18657-z. PMC 9436993. PMID 36050367.
- 1 2 Souto EB, Ribeiro AF, Ferreira MI, Teixeira MC, Shimojo AA, Soriano JL, et al. (January 2020). "New Nanotechnologies for the Treatment and Repair of Skin Burns Infections". International Journal of Molecular Sciences. 21 (2) 393. doi:10.3390/ijms21020393. PMC 7013843. PMID 31936277.
- 1 2 Xie H, Lucchesi L, Zheng B, Ladich E, Pineda T, Merten R, et al. (1 September 2017). "Treatment of Burn and Surgical Wounds With Recombinant Human Tropoelastin Produces New Elastin Fibers in Scars". Journal of Burn Care & Research. 38 (5): e859–e867. doi:10.1097/BCR.0000000000000507. PMID 28221299. S2CID 39251937.
- ↑ Chung, Ki Wung; Song, Seh Hyon; Kim, Man-seok (2021). "Synergistic effect of copper and amino acid mixtures on the production of extracellular matrix proteins in skin fibroblasts". Molecular Biology Reports. 48 (4): 3277–3284. doi:10.1007/s11033-021-06403-z. PMID 34013449.
- 1 2 Kim, Man-Seok; Chun, Ko-Eun; Lee, Dong-Keun; Song, Seh-Hyon (2022). "Evaluation of the Efficacy of an Elastin-Inducing Composition Containing Amino Acids, Copper, and Hyaluronic Acid: Results of an Open Single-Center Clinical Trial Study". Cosmetics. 9 (3) 51. doi:10.3390/cosmetics9030051.
- 1 2 Wang, K.; Meng, X.; Guo, Z. (2021). "Elastin Structure, Synthesis, Regulatory Mechanism and Relationship With Cardiovascular Diseases". Frontiers in Cell and Developmental Biology. 9 596702. doi:10.3389/fcell.2021.596702. PMC 7974140. PMID 33732663.
- 1 2 Vindin, H.; Mithieux, S.M.; Weiss, A.S. (2019). "Elastin architecture". Matrix Biology. 84: 4–16. doi:10.1016/j.matbio.2019.07.005. PMID 31301399.
- ↑ Valenzuela CD, Wagner WL, Bennett RD, Ysasi AB, Belle JM, Molter K, et al. (September 2017). "Extracellular Assembly of the Elastin Cable Line Element in the Developing Lung". Anatomical Record. 300 (9): 1670–1679. doi:10.1002/ar.23603. PMC 6315300. PMID 28380679.
- ↑ Umeda H, Takeuchi M, Suyama K (April 2001). "Two new elastin cross-links having pyridine skeleton. Implication of ammonia in elastin cross-linking in vivo". The Journal of Biological Chemistry. 276 (16): 12579–12587. doi:10.1074/jbc.M009744200. PMID 11278561.
- 1 2 3 Chung, K.W.; Song, S.H.; Kim, M.S. (2021). "Synergistic effect of copper and amino acid mixtures on the production of extracellular matrix proteins in skin fibroblasts". Molecular Biology Reports. 48 (4): 3277–3284. doi:10.1007/s11033-021-06403-z. PMID 34009566.
- ↑ Kim, M.-S.; Chun, K.-E.; Lee, D.-K.; Song, S.-H. (2022). "Evaluation of the Efficacy of an Elastin-Inducing Composition Containing Amino Acids, Copper, and Hyaluronic Acid: Results of an Open Single-Center Clinical Trial Study". Cosmetics. 9 (3): 51. doi:10.3390/cosmetics9030051.
Further reading
[edit]- Jan SL, Chan SC, Fu YC, Lin SJ (June 2009). "Elastin gene study of infants with isolated congenital ductus arteriosus aneurysm". Acta Cardiologica. 64 (3): 363–369. doi:10.2143/ac.64.3.2038023. PMID 19593948. S2CID 31411296.
- Keeley FW, Bellingham CM, Woodhouse KA (February 2002). "Elastin as a self-organizing biomaterial: use of recombinantly expressed human elastin polypeptides as a model for investigations of structure and self-assembly of elastin". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 357 (1418): 185–189. doi:10.1098/rstb.2001.1027. PMC 1692930. PMID 11911775.
- Choudhury R, McGovern A, Ridley C, Cain SA, Baldwin A, Wang MC, et al. (September 2009). "Differential regulation of elastic fiber formation by fibulin-4 and -5". The Journal of Biological Chemistry. 284 (36): 24553–24567. doi:10.1074/jbc.M109.019364. PMC 2782046. PMID 19570982.
- Hubmacher D, Cirulis JT, Miao M, Keeley FW, Reinhardt DP (January 2010). "Functional consequences of homocysteinylation of the elastic fiber proteins fibrillin-1 and tropoelastin". The Journal of Biological Chemistry. 285 (2): 1188–1198. doi:10.1074/jbc.M109.021246. PMC 2801247. PMID 19889633.
- Coolen NA, Schouten KC, Middelkoop E, Ulrich MM (January 2010). "Comparison between human fetal and adult skin". Archives of Dermatological Research. 302 (1): 47–55. doi:10.1007/s00403-009-0989-8. PMC 2799629. PMID 19701759.
- McGeachie M, Ramoni RL, Mychaleckyj JC, Furie KL, Dreyfuss JM, Liu Y, et al. (December 2009). "Integrative predictive model of coronary artery calcification in atherosclerosis". Circulation. 120 (24): 2448–2454. doi:10.1161/CIRCULATIONAHA.109.865501. PMC 2810344. PMID 19948975.
- Yoshida T, Kato K, Yokoi K, Oguri M, Watanabe S, Metoki N, et al. (August 2009). "Association of genetic variants with chronic kidney disease in individuals with different lipid profiles". International Journal of Molecular Medicine. 24 (2): 233–246. doi:10.3892/ijmm_00000226. PMID 19578796.
- Akima T, Nakanishi K, Suzuki K, Katayama M, Ohsuzu F, Kawai T (November 2009). "Soluble elastin decreases in the progress of atheroma formation in human aorta". Circulation Journal. 73 (11): 2154–2162. doi:10.1253/circj.cj-09-0104. PMID 19755752.
- Chen Q, Zhang T, Roshetsky JF, Ouyang Z, Essers J, Fan C, et al. (September 2009). "Fibulin-4 regulates expression of the tropoelastin gene and consequent elastic-fibre formation by human fibroblasts". The Biochemical Journal. 423 (1): 79–89. doi:10.1042/BJ20090993. PMC 3024593. PMID 19627254.
- Tintar D, Samouillan V, Dandurand J, Lacabanne C, Pepe A, Bochicchio B, Tamburro AM (November 2009). "Human tropoelastin sequence: dynamics of polypeptide coded by exon 6 in solution" (PDF). Biopolymers. 91 (11): 943–952. doi:10.1002/bip.21282. PMID 19603496.
- Dyksterhuis LB, Weiss AS (June 2010). "Homology models for domains 21-23 of human tropoelastin shed light on lysine crosslinking". Biochemical and Biophysical Research Communications. 396 (4): 870–873. Bibcode:2010BBRC..396..870D. doi:10.1016/j.bbrc.2010.05.013. PMID 20457133.
- Romero R, Velez Edwards DR, Kusanovic JP, Hassan SS, Mazaki-Tovi S, Vaisbuch E, et al. (May 2010). "Identification of fetal and maternal single nucleotide polymorphisms in candidate genes that predispose to spontaneous preterm labor with intact membranes". American Journal of Obstetrics and Gynecology. 202 (5): 431.e1–431.34. doi:10.1016/j.ajog.2010.03.026. PMC 3604889. PMID 20452482.
- Fan BJ, Figuieredo Sena DR, Pasquale LR, Grosskreutz CL, Rhee DJ, Chen TC, et al. (September 2010). "Lack of association of polymorphisms in elastin with pseudoexfoliation syndrome and glaucoma". Journal of Glaucoma. 19 (7): 432–436. doi:10.1097/IJG.0b013e3181c4b0fe. PMC 6748032. PMID 20051886.
- Bertram C, Hass R (October 2009). "Cellular senescence of human mammary epithelial cells (HMEC) is associated with an altered MMP-7/HB-EGF signaling and increased formation of elastin-like structures". Mechanisms of Ageing and Development. 130 (10): 657–669. doi:10.1016/j.mad.2009.08.001. PMID 19682489. S2CID 46477586.
- Roberts KE, Kawut SM, Krowka MJ, Brown RS, Trotter JF, Shah V, et al. (July 2010). "Genetic risk factors for hepatopulmonary syndrome in patients with advanced liver disease". Gastroenterology. 139 (1): 130–9.e24. doi:10.1053/j.gastro.2010.03.044. PMC 2908261. PMID 20346360.
- Rosenbloom J (December 1984). "Elastin: relation of protein and gene structure to disease". Laboratory Investigation; A Journal of Technical Methods and Pathology. 51 (6): 605–623. PMID 6150137.
- Bax DV, Rodgers UR, Bilek MM, Weiss AS (October 2009). "Cell adhesion to tropoelastin is mediated via the C-terminal GRKRK motif and integrin alphaVbeta3". The Journal of Biological Chemistry. 284 (42): 28616–28623. doi:10.1074/jbc.M109.017525. PMC 2781405. PMID 19617625.
- Rodriguez-Revenga L, Iranzo P, Badenas C, Puig S, Carrió A, Milà M (September 2004). "A novel elastin gene mutation resulting in an autosomal dominant form of cutis laxa". Archives of Dermatology. 140 (9): 1135–1139. doi:10.1001/archderm.140.9.1135. PMID 15381555.
- Micale L, Turturo MG, Fusco C, Augello B, Jurado LA, Izzi C, et al. (March 2010). "Identification and characterization of seven novel mutations of elastin gene in a cohort of patients affected by supravalvular aortic stenosis". European Journal of Human Genetics. 18 (3): 317–323. doi:10.1038/ejhg.2009.181. PMC 2987220. PMID 19844261.
- Tzaphlidou M (2004). "The role of collagen and elastin in aged skin: an image processing approach". Micron. 35 (3): 173–177. doi:10.1016/j.micron.2003.11.003. PMID 15036271.
External links
[edit]- Elastin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Histology image: 21402loa – Histology Learning System at Boston University
- GeneReviews/NIH/NCBI/UW entry on Williams or Williams-Beuren Syndrome
- The Elastin Protein
- Microfibril
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
