Exploring the Interplay between Polyphenols and Lysyl Oxidase Enzymes for Maintaining Extracellular Matrix Homeostasis

Carolina Añazco, Janin Riedelsberger, Lorenzo Vega-Montoto, Armando Rojas

Producción científica: Contribución a una revistaArtículo de revisiónrevisión exhaustiva

7 Citas (Scopus)

Resumen

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.

Idioma originalInglés estadounidense
Número de artículo10985
Páginas (desde-hasta)10985
PublicaciónInternational Journal of Molecular Sciences
Volumen24
N.º10985
DOI
EstadoPublicada - 2023

Nota bibliográfica

Funding Information:
This research was funded by Agencia Nacional de Investigación y Desarrollo: Fondo Nacional de Desarrollo Científico y Tecnológico (FONDECYT 1212026) and Programa de Fortalecimiento al Desarrollo Científico de Centros Regionales 2020 (R20F0001). The APC was funded by Vicerrectoría de Investigación y Doctorados de la Universidad San Sebastian—Fondo VRID_APC23/05 and FONDECYT 1212026.

Publisher Copyright:
© 2023 by the authors.

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