Oxidative modification of collagen by malondialdehyde in porcine skin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F24%3A73627369" target="_blank" >RIV/61989592:15310/24:73627369 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0003986123003491" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0003986123003491</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.abb.2023.109850" target="_blank" >10.1016/j.abb.2023.109850</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Oxidative modification of collagen by malondialdehyde in porcine skin

Popis výsledku v původním jazyce

Human skin is exposed to various physical and chemical stress factors, which commonly cause the oxidation of lipids and proteins. In this study, azo initiator AAPH [2,2′ -azobis(2-methylpropionamidine) dihydrochloride] was employed to initiate lipid peroxidation in porcine skin as an ex vivo model for human skin. We demonstrate that malondialdehyde (MDA), a secondary product of lipid peroxidation, is covalently bound to collagen in the dermis, forming MDA-collagen adducts. The binding of MDA to collagen results in an unfolding of the collagen triple helix, formation of the dimer of α-chains of collagen, and fragmentation of the collagen α-chain. It is proposed here that the MDA is bound to the lysine residues of α-chain collagen, which are involved in electrostatic interaction and hydrogen bonding with the glutamate and aspartate of other α-chains of the triple helix. Our data provide crucial information about the MDA binding topology in the skin, which is necessary to understand better the various types of skin-related diseases and the aging process in the skin under stress.

Název v anglickém jazyce

Oxidative modification of collagen by malondialdehyde in porcine skin

Popis výsledku anglicky

Human skin is exposed to various physical and chemical stress factors, which commonly cause the oxidation of lipids and proteins. In this study, azo initiator AAPH [2,2′ -azobis(2-methylpropionamidine) dihydrochloride] was employed to initiate lipid peroxidation in porcine skin as an ex vivo model for human skin. We demonstrate that malondialdehyde (MDA), a secondary product of lipid peroxidation, is covalently bound to collagen in the dermis, forming MDA-collagen adducts. The binding of MDA to collagen results in an unfolding of the collagen triple helix, formation of the dimer of α-chains of collagen, and fragmentation of the collagen α-chain. It is proposed here that the MDA is bound to the lysine residues of α-chain collagen, which are involved in electrostatic interaction and hydrogen bonding with the glutamate and aspartate of other α-chains of the triple helix. Our data provide crucial information about the MDA binding topology in the skin, which is necessary to understand better the various types of skin-related diseases and the aging process in the skin under stress.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

<a href="/cs/project/EF16_019%2F0000827" target="_blank" >EF16_019/0000827: Rostliny jako prostředek udržitelného globálního rozvoje</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

ISSN

0003-9861

e-ISSN

1096-0384

Svazek periodika

752

Číslo periodika v rámci svazku

FEB

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

"109850-1"-"109850-8"

Kód UT WoS článku

001140242500001

EID výsledku v databázi Scopus

2-s2.0-85180611404