THE FEATURES OF THE FACE SKIN CONSTRUCTION THAT INFLUENCE ON THE FORMATION OF CICATRICAL TISSUES DURING SUGICAL INTERVENTIONS
Formation of pathological scars of maxillofacial localization after surgery is a significant and widespread problem of modern surgical stomatology and maxillofacial surgery. A significant percentage of patients who needs planned and urgent surgical interventions cause rapid development of reconstructive-restorative surgery of the maxillofacial region.
The analysis of domestic and foreign literary sources was devoted to the peculiarities of the structure of the skin of the head and neck and the optimization of the skin incisions of this localization.
Functional features of human skin depend on the mechanical properties of the dermis, which provides elasticity and resistance to stretching. Changes in the biomechanics of the dermis occur during aging, excessive insolation, scarring, and fibrosis. In addition, mechanical changes in the extracellular matrix of the skin affect the activity and phenotype of the fibroblasts, which adapt the stiffness of the cytoskeleton. Extracellular matrix stiffness defines and maintains cell identity and influences the proliferation, differentiation, migration and expression of skin cells.
The extracellular matrix has been regarded for a long time as a structure with simple architectonics. But, due to modern research, it is known that this complex formation is highly specialized. The different classes of macromolecules that make up the extracellular matrix determine its biological functions. For example, collagen proteins are responsible for the tensile strength of tissues, proteoglycans and glycosaminoglycan are important for hydration and compression resistance, and glycoproteins such as laminas facilitate cell attachment. The largest structures of the extracellular matrix are elastin fibers, which are mainly localized in tissues subject to high mechanical stress, such as skin, lungs, or arteries. These structures represent a very complex organization whose core consists of elastin surrounded by a mantle of microfibrils.
Collagen proteins in the dermis contain mainly type I collagen (85% - 90%) with smaller amounts of type III collagen (10% - 15%). Skin fibroblasts synthesize individual collagen type I and III polypeptide chains as precursor molecules, called procollagens. During the formation of insoluble collagen fibrils, specific proteases break down the carboxy- and amino-terminal domains, forming pN-collagen (procollagen from which the carboxy-terminal domain propeptide is cleaved) and pC-collagen (procollagen, from which the amino-terminal propeptide is cleaved). Because type I and III procollagen, pN-collagen and pC-collagen are precursors of mature collagen molecules, their level usually reflects the level of collagen biosynthesis.
Collagens and elastin contain highly abundant fibrils, each of which is repeated in a sequence enriched in the conformation of polyproline II, cross-linked, insoluble in assembly and resistant to the most photolytic enzymes. The monomeric block of type I collagen consists of two extended chains α1 and one chain α2, twisted together into a triple helix.
The direction of collagen and elastin fibers, according to biomechanical studies, has a significant effect on the enlargement of the wound on the head skin and the tension when closing its edges. The overwhelming reduction of tension and accordingly the improvement of reparative processes in the skin occur when the incision lines correspond to the so-called "golden spiral".
Conclusion. Thus, the analysis of domestic and foreign literature sources indicates the relevance of the selected topics, the need for further studies on the biomechanical and histological substantiation of incisions, which are due to the peculiarities of the structure of the skin in the head and neck to create optimal conditions for reparative regeneration.
2. Avetíkov DS, Steblovskiy DV, Popovich IYU, Lokes YEP, Boyko IV. Izucheniye biokhimicheskikh svoystv kozhi sostsevidnoy oblasti pri vypolnenii kosmeticheskoy otoplastiki. Klíníchna khírurgíya. 2015;8(876):41–44.
3. Avetikov DS, Lokes KP, Stavickij SO, Yatsenko IV. Optimization of Replacement of Defects and Deformation of Head and Neck by Using of Angiosome Temporal Flap. Intermedical journal. 2016;1:6–10.
4. Achterberg VF, Buscemi L, Diekmann H, Smith-Clerc J, Schwengler H, Meister JJ, Wenck H, Gallinat S, Hinz B. The Nano-Scale Mechanical Properties of the Extracellular Matrix Regulate Dermal Fibroblast Function. J Invest Dermatol. 2014;134(7):1862-1872.
5. Balestrini JL, Chaudhry S, Sarrazy V. The mechanical memory of lung myofibroblasts. Itegr Biol (Camb). 2012;4:410–421.
6. Swift J, Ivanovska IL, Buxboim A. Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation. Science. 2013;341:1240104.
7. Bennasroune A, Romier-Crouzet B, Blaise S, Laffargue M, Efremov RG, Martiny L, Maurice P, Duca L. Elastic fibers and elastin receptor complex: Neuraminidase-1 takes the center stage. Matrix Biol. 2019: S0945-053X(19)30146-5.
8. Langton AK, Graham HK, McConnell JC, Sherratt MJ, Griffiths CEM, Watson REB. Organization of the dermal matrix impacts the biomechanical properties of skin. Br J Dermatol. 2017;177(3):818-827.
9. Annabi N, Mithieux SM, Camci-Unal G, Dokmeci MR, Weiss AS, Khademhosseini A. Elastomeric recombinant protein-based biomaterials. Biochem. Eng. J. 2013;77:110–118.
10. Lescan M, Perl RM, Golombek S, Pilz M, Hann L, Yasmin M, Behring A, Keller T, Nolte A, Gruhn F, Kochba E, Levin Y, Schlensak C, Wendel HP, Avci-Adali M. De Novo Synthesis of Elastin by Exogenous Delivery of Synthetic Modified mRNA into Skin and Elastin-Deficient Cells. Mol Ther Nucleic Acids. 2018;1(11):475-484.
11. Moore J, Thibeault S. Insights into the role of elastin in vocal fold health and disease. J. Voice. 2012;26:269–275.
12. Pober BR. Williams-Beuren syndrome. N. Engl. J. Med. 2010;362: 239–252.
13. Wise SG, Weiss AS. Tropoelastin. Int. J. Biochem. Cell Biol. 2009;41:494–497.
14. Mora Huertas AC, Schmelzer CEH, Luise C, Sippl W, Pietzsch M, Hoehenwarter W, Heinz A. Degradation of tropoelastin and skin elastin by neprilysin. Biochimie. 2018;146:73-78.
15. Horiguchi M, Inoue T, Ohbayashi T, Hirai M, Noda K, Marmorstein LY, Yabe D, Takagi K, Akama TO, Kita T, Kimura T, Nakamura T. Fibulin-4 conducts proper elastogenesis via interaction with cross-linking enzyme lysyl oxidase. Proc Natl Acad Sci U S A. 2009;106(45):19029-19034.
16. Zhao HL, Zhang CP, Zhu H, Jiang YF, Fu XB. Autofluorescence of collagen fibres in scar. Skin Res Technol. 2017;23(4):588-592.
17. Caetano GF, Fronza M, Leite MN, Gomes A, Frade MA. Comparison of collagen content in skin wounds evaluated by biochemical assay and by computer-aided histomorphometric analysis. Pharm Biol. 2016;54(11):2555-2559.
18. Paul SP, Matulich J, Charlton N. A New Skin Tensiometer Device: Computational Analyses To Understand Biodynamic Excisional Skin Tension Lines. Sci Rep. 2016;6:301-317.
19. Paul SP. Biodynamic Excisional Skin Tension Lines for Excisional Surgery of the Lower Limb and the Technique of Using Parallel Relaxing Incisions to Further Reduce Wound Tension. Plast Reconstr Surg Glob Open. 2017;5(12):1614-1618.
20. Paul SP. The Golden Spiral Flap: A New Flap Design that Allows for Closure of Larger Wounds under Reduced Tension – How Studying Nature’s Own Design Led to the Development of a New Surgical Technique. Front Surg. 2016;3:63.
21. Johnson TM, Lowe L, Brown MD, Sullivan MJ, Nelson BR. Histology and physiology of tissue expansion. The Journal of Dermatologic Surgery and Oncology.1993;9(12):1074-1078.
22. Krishnan NM, Brown BJ, Davison SP, Mauskar N, Mino M, Jordan MH, Shupp JW. Reducing Wound Tension with Undermining or Imbrication—Do They Work? Plast Reconstr Surg Glob Open. 2016;4(7):799.
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