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dc.contributor.author Añazco, Carolina
dc.contributor.author Riedelsberger, Janin
dc.contributor.author Vega-Montoto, Lorenzo
dc.contributor.author Rojas, Armando
dc.date.accessioned 2024-09-26T00:43:37Z
dc.date.available 2024-09-26T00:43:37Z
dc.date.issued 2023-07-01
dc.identifier.issn 1661-6596
dc.identifier.other ORCID: /0000-0003-1311-9492/work/137952161
dc.identifier.other Mendeley: 57f567c3-94d6-38df-b870-4812b80486ef
dc.identifier.uri https://repositorio.uss.cl/handle/uss/13276
dc.description Publisher Copyright: © 2023 by the authors.
dc.description.abstract Collagen, the most abundant structural protein found in mammals, plays a vital role as a constituent of the extracellular matrix (ECM) that surrounds cells. Collagen fibrils are strengthened through the formation of covalent cross-links, which involve complex enzymatic and non-enzymatic reactions. Lysyl oxidase (LOX) is responsible for catalyzing the oxidative deamination of lysine and hydroxylysine residues, resulting in the production of aldehydes, allysine, and hydroxyallysine. These intermediates undergo spontaneous condensation reactions, leading to the formation of immature cross-links, which are the initial step in the development of mature covalent cross-links. Additionally, non-enzymatic glycation contributes to the formation of abnormal cross-linking in collagen fibrils. During glycation, specific lysine and arginine residues in collagen are modified by reducing sugars, leading to the creation of Advanced Glycation End-products (AGEs). These AGEs have been associated with changes in the mechanical properties of collagen fibers. Interestingly, various studies have reported that plant polyphenols possess amine oxidase-like activity and can act as potent inhibitors of protein glycation. This review article focuses on compiling the literature describing polyphenols with amine oxidase-like activity and antiglycation properties. Specifically, we explore the molecular mechanisms by which specific flavonoids impact or protect the normal collagen cross-linking process. Furthermore, we discuss how these dual activities can be harnessed to generate properly cross-linked collagen molecules, thereby promoting the stabilization of highly organized collagen fibrils. en
dc.language.iso eng
dc.relation.ispartof vol. 24 Issue: no. 10985 Pages: 10985
dc.source International Journal of Molecular Sciences
dc.title Exploring the Interplay between Polyphenols and Lysyl Oxidase Enzymes for Maintaining Extracellular Matrix Homeostasis en
dc.type Artículo de revisión
dc.identifier.doi 10.3390/ijms241310985
dc.publisher.department Facultad de Ciencias para el Cuidado de la Salud


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