2010, Número 2
<< Anterior Siguiente >>
Med Cutan Iber Lat Am 2010; 38 (2)
Romper el proceso del envejecimiento cutáneo: activos dermocosméticos
Prieto L
Idioma: Español
Referencias bibliográficas: 20
Paginas: 95-100
Archivo PDF: 250.82 Kb.
FRAGMENTO
El envejecimiento cutáneo es el conjunto de cambios que ocurren en el organismo, debido a la asociación de múltiples factores. Existen diferentes teorías que permiten explicar este proceso. Actualmente, junto a las teorías genéticas de acortamiento de los telómeros, la “Teoría de la intoxicación por sustancias intrínsecas” es una de las que mejor explica este proceso ineluctable. El acúmulo de sustancias tóxicas generadas por reacciones internas de nuestro organismo da lugar a alteraciones en el funcionamiento de los tejidos. Dentro de este tipo de reacciones endógenas, la glicación y la oxidación son las que más repercuten en el desarrollo y la amplificación del envejecimiento del organismo y, en consecuencia en el proceso del envejecimiento cutáneo.
REFERENCIAS (EN ESTE ARTÍCULO)
Suji G, Sivakami S. Glucose, glycation and aging. Biogerontology 2004; 5: 365-73.
Pageon H, Asselineau D. An in vitro approach to the chronological aging of skin by glyction of the collagen: the biological effect of glycation on the reconstructed skin model. Ann N Y Acads Sci 2005; 1043:529-32.
Uribarri J, Cai W, Peppa M et al. Circulating glycotoxins and dietary advanced glycation end products: two links to inflammatory response, axidative stress, and aging. J Gerontol A Biol Sci Med Sci 2007; 62: 427-33.
Pageon H, Téccher MP, Asselineau D. Reconstructed skin modified by glycation of the dermal equivalent as a model for skin aging and its potential use to evaluate anti-glycation molecules. Exp Gerontol 2008; 43: 584-8.
Hipkiss AR, Michaelis J, Syrris. Non-enzymatic glycosylation of the dipeptide Lcarnosine, a potential anti-protein-crosslinking agent. P FEBS Lett 1995; 371: 81-5.
Howard EW, Benton R, Ahern-Moore J et al. Cellular contraction of collagen lattices is inhibited by nonenzymatic glycation. Exp Cell Res 1996; 228: 132.
Hipkiss AR, Worthington VC, Himsworth DT et al. Protective effects of carnosine against protein modification mediated by malondialdehyde and hy-pochlorite. Biochim Biophys Acta 1998; 1380: 46-54.
Hipkiss AR, Chana H. Carnosine protects proteins against methylglyoxal-mediated modifications. Biochem Biophys Res Commun 1998; 248: 28-32.
Hipkiss AR. On the enigma of carnosine’s anti-ageing action. Exp Gerontol 2009; 44: 237-42.
Morcos M, Du X, Pfisterer F, Hutter H et al. Glyoxalase-1 prevents mitochondrial protein modification and enhances lifespan in Caenorhabditis elegans. Aging Cell 2008; 7: 260-9.
Hipkiss AR, Brownson C, Carrier MJ. Carnosine, the anti-ageing, anti-oxidant dipeptide, may react with protein carbonyl groups. Mech Ageing Dev 2001; 122: 1431-45.
Quinn PJ, Boldyrev AA, Formazuyk VE. Carnosine: its properties, functions and potential therapeutic applications. Mol Aspects Med 1992; 13: 379-444.
Rimbach G, Virgili F, Park YC, Packer L. Effect of procyanidins from Pinus maritima on glutathione levels in endothelial cells challenged by 3-morpholinosydnonimine or activated macrophages. Redox Rep 1999; 4: 171-7.
Brenneisen P, Sies H, Scharffetter-Kochanek K. Ultraviolet-B irradiation and matrix metalloproteinases: from induction via signaling to initial events”. Ann N Y Acad Sci 2002; 973: 31-43.
Rihn B, Saliou C, Bottin MC et al. From ancient remedies to modern therapeutics: pine bark uses in skin disorders revisited. Phytother Res 2001; 15: 76-8.
Halliwell B, Gutteridge JM. The antioxidants of human extracellular fluids. Arch Biochem Biophys 1990; 280: 1-8.
Quevedo WC Jr, Holstein TJ, Dyckman J et al. The responses of the human epidermal melanocyte system to chronic erythemal doses of UVR in skin protected by topical applications of a combination of vitamins C and E. Pigment Cell Res 2000; 3: 190-2.
Kojo S. Vitamin C: basic metabolism and its function as an index of oxidative stress. Curr Med Chem 2004; 11: 1041-64.
Nusgens BV, Humbert P, Rougier A et al. Topically applied vitamin C enhances the mRNA level of collagens I and III, their processing enzymes and tissue inhibitor of matrix metalloproteinase 1 in the human dermis. J Invest Dermatol 2001; 116: 853-9.
Boyce ST, Supp AP, Swope VB et al. Vitamin C regulates keratinocyte viability, epidermal barrier, and basement membrane in vitro, and reduces wound contraction after grafting of cultured skin substitutes. J Invest Dermatol 2002; 118: 565-72.