Expanded View of the Pathophysiology of Fabry Disease

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00064165%3A_____%2F25%3A10500352" target="_blank" >RIV/00064165:_____/25:10500352 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11110/25:10500352

Výsledek na webu

<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=UAarN-aFgf" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=UAarN-aFgf</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1159/000546555" target="_blank" >10.1159/000546555</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Expanded View of the Pathophysiology of Fabry Disease

Popis výsledku v původním jazyce

Protein processing and maturation are intricate processes involving distinct intracellular compartments. Cellular quality control systems maintain protein homeostasis by identifying, sequestering, and eliminating damaged or misfolded proteins. Yet misfolded proteins can accumulate and overwhelm the quality control systems. This phenomenon is a hallmark of numerous pathologies, including a variety of genetic disorders. Recently Lacoste et al. showed that a significant proportion of pathogenic human variants (16% of 3,448 pathogenic or likely pathogenic missense variants across 1,269 genes) encode for proteins that are less stable and abnormally distributed across the cellular compartments. In the secretory pathway, the buildup of misfolded proteins triggers endoplasmic reticulum (ER) stress, which activates the unfolded protein response (UPR). The UPR is an adaptive mechanism that alleviates ER stress and restores cellular homeostasis. However, if ER stress is prolonged or severe, the UPR may fail to restore balance, leading to apoptosis and interstitial fibrosis.

Název v anglickém jazyce

Expanded View of the Pathophysiology of Fabry Disease

Popis výsledku anglicky

Protein processing and maturation are intricate processes involving distinct intracellular compartments. Cellular quality control systems maintain protein homeostasis by identifying, sequestering, and eliminating damaged or misfolded proteins. Yet misfolded proteins can accumulate and overwhelm the quality control systems. This phenomenon is a hallmark of numerous pathologies, including a variety of genetic disorders. Recently Lacoste et al. showed that a significant proportion of pathogenic human variants (16% of 3,448 pathogenic or likely pathogenic missense variants across 1,269 genes) encode for proteins that are less stable and abnormally distributed across the cellular compartments. In the secretory pathway, the buildup of misfolded proteins triggers endoplasmic reticulum (ER) stress, which activates the unfolded protein response (UPR). The UPR is an adaptive mechanism that alleviates ER stress and restores cellular homeostasis. However, if ER stress is prolonged or severe, the UPR may fail to restore balance, leading to apoptosis and interstitial fibrosis.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30105 - Physiology (including cytology)

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

V - Vyzkumna aktivita podporovana z jinych verejnych zdroju

Rok uplatnění

2025

Kód důvěrnosti údajů

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

Název periodika

Nephron

ISSN

1660-8151

e-ISSN

2235-3186

Svazek periodika

149

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

4

Strana od-do

620-623

Kód UT WoS článku

001541537600001

EID výsledku v databázi Scopus

2-s2.0-105012396564