The site of the Media Sphera Publishers contains materials intended solely for healthcare professionals.
By closing this message, you confirm that you are a certified medical professional or a student of a medical educational institution.

Borzykh O.B.

Voyno-Yasenetsky Krasnoyarsk State Medical University (V.F. Voyno-Yasenetsky KrasSMU)

Shnayder N.A.

Bekhterev National Medical Research Center of Psychiatry and Neurology

Petrova M.M.

Voino-Yasenetsky Krasnoyarsk State Medical University

Karpova E.I.

Pirogov Russian National Research Medical University

Demina O.M.

Pirogov Russian National Research Medical University (RNRMU)

Zatolokina M.A.

Kursk state medical university

Regulation of elastin turnover in the skin: Biological and genetic aspects

Authors:

Borzykh O.B., Shnayder N.A., Petrova M.M., Karpova E.I., Demina O.M., Zatolokina M.A.

More about the authors

Read: 7756 times


To cite this article:

Borzykh OB, Shnayder NA, Petrova MM, Karpova EI, Demina OM, Zatolokina MA. Regulation of elastin turnover in the skin: Biological and genetic aspects. Russian Journal of Clinical Dermatology and Venereology. 2022;21(4):435‑441. (In Russ.)
https://doi.org/10.17116/klinderma202221041435

Recommended articles:
Modern methods of correction of age-related changes in the female body. Plastic Surgery and Aesthetic Medi­cine. 2025;(1):90-96

References:

  1. Usansky I, Jaworska P, Asti L, Kenny FN, Hobbs C, Sofra V, Song H, Logan M, Graham A, Shaw TJ. A developmental basis for the anatomical diversity of dermis in homeostasis and wound repair. J Pathol. 2021;253(3): 315-325.  https://doi.org/10.1002/path.5589
  2. Jansen KA, Licup AJ, Sharma A, Rens R, MacKintosh FC, Koenderink GH. The Role of Network Architecture in Collagen Mechanics. Biophys J. 2018;114(11):2665-2678. https://doi.org/10.1016/j.bpj.2018.04.043
  3. Gambichler T, Mamali K, Scheel C. A Brief Literature Update on Mid-dermal Elastolysis with an Emphasis on Pathogenetic and Therapeutic Aspects. J Clin Aesthet Dermatol. 2020;13(9):E53-E58. 
  4. Shin JW, Kwon SH, Choi JY, Na JI, Huh CH, Choi HR, Park KC. Molecular Mechanisms of Dermal Aging and Antiaging Approaches. Int J Mol Sci. 2019;20(9):2126. https://doi.org/10.3390/ijms20092126
  5. Erickson JR, Echeverri K. Learning from regeneration research organisms: the circuitous road to scar free wound healing. Dev Biol. 2018;433(2):144-154. 
  6. Mithieux SM, Weiss AS. Design of an elastin-layered dermal regeneration template. Acta Biomater. 2017;52:33-40. 
  7. Shnayder NA, Dyuzhakova AV, Vaiman EE, Nikitina EI, Borzykh OB, Nasyrova RF. The role of genetic factors of endogenous hyaluronic acid metabolism in maintaining skin homeostasis. Vestnik Dermatologii i Venerologii. 2021;97(3):24-38. (In Russ.). https://doi.org/10.25208/vdv1193
  8. Borzykh OB, Petrova MM, Shnayder NA, Nasyrova RF. Problems of implementation of personalized medicine in medical cosmetology in Russia. Siberian Medical Review. 2021;(2):12-22. (In Russ.). https://doi.org/10.20333/25000136-2021-2-12-22
  9. Uitto J, Li Q, Urban Z. The complexity of elastic fibre biogenesis in the skin — a perspective to the clinical heterogeneity of cutis laxa. Exp Dermatol. 2013;22(2):88-92.  https://doi.org/10.1111/exd.12025
  10. Ozsvar J, Yang C, Cain SA, Baldock C, Tarakanova A, Weiss AS. Tropoelastin and Elastin Assembly. Front Bioeng Biotechnol. 2021;9:643110. https://doi.org/10.3389/fbioe.2021.643110
  11. Gharesouran J, Hosseinzadeh H, Ghafouri-Fard S, Jabbari Moghadam Y, Ahmadian Heris J, Jafari-Rouhi AH, Taheri M, Rezazadeh M. New insight into clinical heterogeneity and inheritance diversity of FBLN5-related cutis laxa. Orphanet J Rare Dis. 2021;16(1):51.  https://doi.org/10.1186/s13023-021-01696-6
  12. Van Damme T, Gardeitchik T, Mohamed M, Guerrero-Castillo S, Freisinger P, Guillemyn B, Kariminejad A, Dalloyaux D, van Kraaij S, Lefeber DJ, Syx D, Steyaert W, De Rycke R, Hoischen A, Kamsteeg EJ, Wong SY, van Scherpenzeel M, Jamali P, Brandt U, Nijtmans L, Korenke GC, Chung BHY, Mak CCY, Hausser I, Kornak U, Fischer-Zirnsak B, Strom TM, Meitinger T, Alanay Y, Utine GE, Leung KCP, Ghaderi-Sohi S, Coucke P, Symoens S, De Paepe A, Thiel C, Haack TB, Malfait F, Morava E, Callewaert B, Wevers RA. Mutations in ATP6V1E1 or ATP6V1A Cause Autosomal-Recessive Cutis Laxa. Am J Hum Genet. 2020 Aug 6;107(2):374.  https://doi.org/10.1016/j.ajhg.2020.07.013
  13. Dhital B, Durlik P, Rathod P, Gul-E-Noor F, Wang Z, Sun C, Chang EJ, Itin B, Boutis GS. Ultraviolet radiation reduces desmosine cross-links in elastin. Biochem Biophys Rep. 2017;10:172-177.  https://doi.org/10.1016/j.bbrep.2017.04.002
  14. Mahajan D, Kancharla S, Kolli P, Sharma AK, Singh S, Kumar S, Mohanty AK, Jena MK. Role of Fibulins in Embryonic Stage Development and Their Involvement in Various Diseases. Biomolecules. 2021;11(5):685.  https://doi.org/10.3390/biom11050685
  15. Vindin H, Mithieux SM, Weiss AS. Elastin architecture. Matrix Biol. 2019; 84:4-16 
  16. Pigatto Filho G, Zeni M, Melchioretto EF, Marques GL, Hota T, Fraga R. Age-dependent histomorphometric evolution of the corpus spongiosum. Acta Cir Bras. 2021;35(12):e351203. https://doi.org/10.1590/ACB351203
  17. Almine JF, Wise SG, Weiss AS. Elastin signaling in wound repair. Birth Defects Res C Embryo Today. 2012;96(3):248-257. 
  18. Bergstrom KG. Beyond tretinoin: cosmeceuticals for aging skin. J. Drugs Dermatol.: JDD. 2009;8:674-677. 
  19. Baumann L, Bernstein EF, Weiss AS, Bates D, Humphrey S, Silberberg M, Daniels R. Clinical Relevance of Elastin in the Structure and Function of Skin. Aesthet Surg J Open Forum. 2021;3(3):ojab019. https://doi.org/10.1093/asjof/ojab019
  20. Cohen BE, Geronemus RG, McDaniel DH, Brauer JA. The role of elastic fibers in scar formation and treatment. Dermatol Surg. 2017;43(1):S19-24. 
  21. Widgerow AD, Napekoski K. New approaches to skin photodamage histology-Differentiating ‘good’ versus ‘bad’ Elastin. J Cosmet Dermatol. 2021; 20(2):526-531.  https://doi.org/10.1111/jocd.13865
  22. Potekaev NN, Borzykh OB, Shnayder NA, Petrova MM, Karpova EI, Demina OM, Nasyrova RF. Genomics of elastic fiber synthesis. Practical significance for cosmetologists and dermatologists. Russian Journal of Clinical Dermatology and Venereology = Klinicheskaya dermatologiya i venerologiya. 2021;20(6):52-59. (In Russ.). https://doi.org/10.17116/klinderma20212006152
  23. Kleiser S, Nyström A. Interplay between Cell-Surface Receptors and Extracellular Matrix in Skin. Biomolecules. 2020 Aug 11;10(8):1170. https://doi.org/10.3390/biom10081170
  24. Philips N, Samuel P, Keller T, Alharbi A, Alshalan S, Shamlan SA. Beneficial Regulation of Cellular Oxidative Stress Effects, and Expression of Inflammatory, Angiogenic, and the Extracellular Matrix Remodeling Proteins by 1α,25-Dihydroxyvitamin D3 in a Melanoma Cell Line. Molecules. 20205; 25(5):1164. https://doi.org/10.3390/molecules25051164
  25. Sproul EP, Argraves WS. A cytokine axis regulates elastin formation and degradation. Matrix Biol. 2013;32(2):86-94.  https://doi.org/10.1016/j.matbio.2012.11.004
  26. Gonzalez de Torre I., Alonso M., Rodriguez-Cabello J.C. Elastin-Based Materials: Promising Candidates for Cardiac Tissue Regeneration. Front Bioeng Biotechnol. 2020;8:657.  https://doi.org/10.3389/fbioe.2020.00657
  27. Godinho MSC, Thorpe CT, Greenwald SE, Screen HRC. Elastin is Localised to the Interfascicular Matrix of Energy Storing Tendons and Becomes Increasingly Disorganised With Ageing. Sci Rep. 2017;7(1):9713. https://doi.org/10.1038/s41598-017-09995-4
  28. Cocciolone AJ, Hawes JZ, Staiculescu MC, Johnson EO, Murshed M, Wagenseil JE. Elastin, arterial mechanics, and cardiovascular disease. Am J Physiol Heart Circ Physiol. 2018;315(2):H189-H205. https://doi.org/10.1152/ajpheart.00087.2018
  29. Bartstra JW, Spiering W, van den Ouweland JMW, Mali WPTM, Janssen R, de Jong PA. Increased Elastin Degradation in Pseudoxanthoma Elasticum Is Associated with Peripheral Arterial Disease Independent of Calcification. J Clin Med. 2020;9(9):2771. https://doi.org/10.3390/jcm9092771
  30. Fazaeli S, Mirahmadi F, Everts V, Smit TH, Koolstra JH, Ghazanfari S. Alteration of structural and mechanical properties of the temporomandibular joint disc following elastase digestion. J Biomed Mater Res B Appl Biomater. 2020;108(8):3228-3240. https://doi.org/10.1002/jbm.b.34660
  31. Van Doren SR. Matrix metalloproteinase interactions with collagen and elastin. Matrix Biol. 2015;44-46:224-231.  https://doi.org/10.1016/j.matbio.2015.01.005
  32. Yadati T, Houben T, Bitorina A, Shiri-Sverdlov R. The Ins and Outs of Cathepsins: Physiological Function and Role in Disease Management. Cells. 2020;9(7):1679. https://doi.org/10.3390/cells9071679
  33. Rawat K, Syeda S., Shrivastava A. Neutrophil-derived granule cargoes: paving the way for tumor growth and progression. Cancer Metastasis Rev. 2021; 40(1):221-244.  https://doi.org/10.1007/s10555-020-09951-1
  34. Novak T, Fortune F, Bergmeier L, Khan I, Hagi-Pavli E. Neutrophil elastase and endogenous inhibitors in Behçet’s disease saliva. Clin Exp Immunol. 2020;202(1):93-105.  https://doi.org/10.1111/cei.13483
  35. Ahmad S, Saleem M, Riaz N, Lee YS, Diri R, Noor A, Almasri D, Bagalagel A, Elsebai MF. The Natural Polypeptides as Significant Elastase Inhibitors. Front Pharmacol. 2020;11:688.  https://doi.org/10.3389/fphar.2020.00688
  36. Varanko A, Saha S, Chilkoti A. Recent trends in protein and peptide-based biomaterials for advanced drug delivery. Adv Drug Deliv Rev. 2020;156: 133-187.  https://doi.org/10.1016/j.addr.2020.08.008
  37. Frugé AD, Smith KS, Bail JR, Rais-Bahrami S, Demark-Wahnefried W. Biomarkers Associated With Tumor Ki67 and Cathepsin L Gene Expression in Prostate Cancer Patients Participating in a Presurgical Weight Loss Trial. Front Oncol. 2020 Sep 17;10:544201. https://doi.org/10.3389/fonc.2020.544201
  38. Cabral-Pacheco GA, Garza-Veloz I, Castruita-De la Rosa C, Ramirez-Acuña JM, Perez-Romero BA, Guerrero-Rodriguez JF, Martinez-Avila N, Martinez-Fierro ML. The Roles of Matrix Metalloproteinases and Their Inhibitors in Human Diseases. Int J Mol Sci. 2020;21(24):9739. https://doi.org/10.3390/ijms21249739
  39. Raeeszadeh-Sarmazdeh M, Do LD, Hritz BG. Metalloproteinases and Their Inhibitors: Potential for the Development of New Therapeutics. Cells. 2020; 9(5):1313. https://doi.org/10.3390/cells9051313
  40. Du X, Chen NL, Wong A, Craik CS, Brömme D. Elastin degradation by cathepsin V requires two exosites. J Biol Chem. 2013;288(48):34871-34881. https://doi.org/10.1074/jbc.M113.510008
  41. García-Onrubia L, Valentín-Bravo FJ, Coco-Martin RM, González-Sarmiento R, Pastor JC, Usategui-Martín R, Pastor-Idoate S. Matrix Metalloproteinases in Age-Related Macular Degeneration (AMD). Int J Mol Sci. 2020;21(16):5934. https://doi.org/10.3390/ijms21165934
  42. Cancemi P, Aiello A, Accardi G, Caldarella R, Candore G, Caruso C, Ciaccio M, Cristaldi L, Di Gaudio F, Siino V, Vasto S. The Role of Matrix Metalloproteinases (MMP-2 and MMP-9) in Ageing and Longevity: Focus on Sicilian Long-Living Individuals (LLIs). Mediators Inflamm. 2020;2020: 8635158. https://doi.org/10.1155/2020/8635158
  43. Zarkovic K, Larroque-Cardoso P, Pucelle M, Salvayre R, Waeg G, Nègre-Salvayre A, Zarkovic N. Elastin aging and lipid oxidation products in human aorta. Redox Biol. 2015;4:109-117.  https://doi.org/10.1016/j.redox.2014.12.008
  44. Henderson MW, Noubouossie DF, Ilich A, Wilson KJ, Pawlinski R, Monroe DM, Key NS. Protease: Serpin complexes to assess contact system and intrinsic pathway activation. Res Pract Thromb Haemost. 2020;4(5):789-798.  https://doi.org/10.1002/rth2.12389
  45. McCabe MC, Hill RC, Calderone K, Cui Y, Yan Y, Quan T, Fisher GJ, Hansen KC. Alterations in extracellular matrix composition during aging and photoaging of the skin. Matrix Biol Plus. 2020;8:100041. https://doi.org/10.1016/j.mbplus.2020.100041
  46. Meinke MC, Nowbary CK, Schanzer S, Vollert H, Lademann J, Darvin ME. Influences of Orally Taken Carotenoid-Rich Curly Kale Extract on Collagen I/Elastin Index of the Skin. Nutrients. 2017;9(7):775.  https://doi.org/10.3390/nu9070775
  47. Tsamis A, Krawiec JT, Vorp DA. Elastin and collagen fibre microstructure of the human aorta in ageing and disease: a review. J R Soc Interface. 2013; 10(83):20121004. https://doi.org/10.1098/rsif.2012.1004
  48. Tsamis A, Krawiec JT, Vorp DA. Elastin and collagen fibre microstructure of the human aorta in ageing and disease: a review. J R Soc Interface. 2013; 10(83):20121004. https://doi.org/10.1098/rsif.2012.1004

Email Confirmation

An email was sent to test@gmail.com with a confirmation link. Follow the link from the letter to complete the registration on the site.

Email Confirmation

We use cооkies to improve the performance of the site. By staying on our site, you agree to the terms of use of cооkies. To view our Privacy and Cookie Policy, please. click here.