Endoplasmatisk retikulum protein 29 er dysreguleret hos ME patienter

Af forrige blog indlæg: 

Dysregulering af Endoplasmatisk Retikulum stress responset hos ME patienter efter motion (1).

fremgik det, at Enoplasmatisk Retikulum protein 29 (ERP29) er dysreguleret i vesikler fra ME patienter efter motion. 

I et preprint af en ny artikel:

Charting the Circulating Proteome in ME/CFS. Cross System Profiling and Mechanistic insights (2).

har man undersøgt protein indholdet i serum fra ME patienter, og her dukker ERP29 også op.

ERP29 er nr 7 på listen over opregulerede proteiner. Dette fremgår af figur 1E på side 31 i artiklen.

Det eneste som vi kan bruge denne observation til lige nu, er at vi skal holde øje med forskning i ERP29. Så nu kommer lidt ERP29 viden.

ERP29 og ER stress

ERP29 er opreguleret under ER stress (ERS). Ved ER stress ophobes misfolde proteiner. Dette udløser det ufoldede protein respons (UPR) (3).

Citat fra artikel 3:
"While it is logical to hypothesize that ERp29 is predominantly upregulated during ERS to facilitate stabilization of its clients for their eventual exit from the ER, there are also data suggesting that ERp29 may play a role in the underlying pathways that regulate and facilitate UPR and ERS."

I figur 3 fra reference 3 er ERP29s mulige rolle i ER stress og UPR anskueliggjort:

https://pmc.ncbi.nlm.nih.gov/articles/PMC7506106/figure/F3/

Mere viden om ERP29

Regulatory role of endoplasmic reticulum resident chaperone protein ERp29 in anti-murine β-coronavirus host cell response

Non-canonical function of DPP4 promotes cognitive impairment through ERp29-associated mitochondrial calcium overload in diabetes

Phenylbutyrate restricts murine β-coronavirus infectivity and limits virus-induced demyelination in vivo

Endoplasmic reticulum protein 29 negatively regulates platelet functions and thrombosis in mice

Identification of endoplasmic reticulum stress genes in human stroke based on bioinformatics and machine learning

ERp29 Attenuates Nicotine-Induced Endoplasmic Reticulum Stress and Inhibits Choroidal Neovascularization

Molecular Chaperone ERp29: A Potential Target for Cellular Protection in Retinal and Neurodegenerative Diseases

Referencer

1) Glass KA, Giloteaux L, Zhang S, Hanson MR. Extracellular vesicle proteomics uncovers energy metabolism, complement system, and endoplasmic reticulum stress response dysregulation postexercise in males with myalgic encephalomyelitis/chronic fatigue syndrome. Clin Transl Med. 2025 May;15(5):e70346. doi: 10.1002/ctm2.70346. PMID: 40465195; PMCID: PMC12135887.
https://pubmed.ncbi.nlm.nih.gov/40465195/

2) Charting the Circulating Proteome in ME/CFS: Cross System Profiling and Mechanistic insights
August Hoel, Fredrik Hoel, Sissel Elisabeth Furesund Dyrstad, Henrique Chapola, Ingrid Gurvin Rekeland, Kristin Risa, Kine Alme, Kari Sørland, Karl Albert Brokstad, Hans-Peter Marti, Olav Mella, Øystein Fluge, Karl Johan Tronstad
medRxiv 2025.05.28.25328245; doi: https://doi.org/10.1101/2025.05.28.25328245
This article is a preprint and has not been peer-reviewed [what does this mean?]. It reports new medical research that has yet to be evaluated and so should not be used to guide clinical practice.

https://www.medrxiv.org/content/10.1101/2025.05.28.25328245v1

3) Brecker M, Khakhina S, Schubert TJ, Thompson Z, Rubenstein RC. The Probable, Possible, and Novel Functions of ERp29. Front Physiol. 2020 Sep 8;11:574339. doi: 10.3389/fphys.2020.574339. PMID: 33013490; PMCID: PMC7506106.

https://www.frontiersin.org/journals/physiology/articles/10.3389/fphys.2020.574339/full