Oxidative stress-mediated aldehyde adduction of GRP78 in a mouse model of alcoholic liver disease: functional independence of ATPase activity and chaperone function
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Pathogenesis in alcoholic liver disease (ALD) is complicated and multifactorial but clearly involves oxidative stress and inflammation. Currently, conflicting reports exist regarding the role of endoplasmic reticulum (ER) stress in the etiology of ALD. The glucose-regulated protein 78 (GRP78) is the ER homolog of HSP70 and plays a critical role in the cellular response to ER stress by serving as a chaperone assisting protein folding and by regulating the signaling of the unfolded protein response (UPR). Comprising three functional domains, an ATPase, a peptide-binding, and a lid domain, GRP78 folds nascent polypeptides via the substrate-binding domain. Earlier work has indicated that the ATPase function of GRP78 is intrinsically linked and essential to its chaperone activity. Previous work in our laboratory has indicated that GRP78 and the UPR are not induced in a mouse model of ALD but that GRP78 is adducted by the lipid electrophiles 4-hydroxynonenal (4-HNE) and 4-oxononenal (4-ONE) in vivo. As impairment of GRP78 has the potential to contribute to pathogenesis in ALD, we investigated the functional consequences of aldehyde adduction on GRP78 function. Identification of 4-HNE and 4-ONE target residues in purified human GRP78 revealed a marked propensity for Lys and His adduction within the ATPase domain and a relative paucity of adduct formation within the peptide-binding domain. Consistent with these findings, we observed a concomitant dose-dependent decrease in ATP-binding and ATPase activity without any discernible impairment of chaperone function. Collectively, our data indicate that ATPase activity is not essential for GRP78-mediated chaperone activity and is consistent with the hypothesis that ER stress does not play a primary initiating role in the early stages of ALD.
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MDA and 4-HNE are reactive lipid peroxides with short half-lives that can form covalent adducts with various proteins and nucleic acids in the body.
“MDA and 4-HNE are reactive lipid peroxides with short half-lives that can form covalent adducts with various proteins and nucleic acids in the body.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [173]
Ethanol intake can induce 4-HNE to interact with mitochondrial, ER, and cytosolic proteins, inactivating them and resulting in accumulation of lipid aldehydes, ER stress, mitochondrial dysfunction, cell signaling alteration, and potentially multitissue injury.
“For instance, ethanol intake can induce 4-HNE to interact with cytochrome C oxidase (complex IV) and ALDH2 in the mitochondria, GRP78 and disulfide isomerase in the ER, and ERK1/2, phosphatase and tensin homolog (PTEN), AMP-activated protein kinase (AMPK), and gamma-glutamylcysteine synthetase (GCS) in the cytosol.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [173]
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- Authors
- Galligan, J. J., Fritz, K. S., Backos, D. S., Shearn, C. T., Smathers, R. L., Jiang, H., MacLean, K. N., Reigan, P. R., & Petersen, D. R.
- Affiliations
- University of Colorado Anschutz (US)
- Corresponding author
- Petersen, Dennis R.
- ORCID
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2014-08
- Volume
- 73
- Pages
- 411-420
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC4395467
- OpenAlex
- W2043979350
- Cited by
- 46
- References
- 42
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 7 · 2020: 2 · 2019: 1 · 2018: 6 · 2017: 4 · 2016: 7 · 2015: 7 · 2014: 2
- FWCI
- 3.32
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health/National Institute of Alcoholism and Alcohol Abuse (R37AA09300, R01DK074487-01, F31AA018606-01)
- Colorado Clinical Translational Science Institute (UL1 RR025780)
- University of Colorado Cancer Center (P30 CA046934)
- NIH/NCATS Colorado CTSI (UL1 TR001082)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
- Keywords
- GRP78, alcoholic liver disease, oxidative stress, 4-hydroxynonenal, endoplasmic reticulum stress, unfolded protein response, ATPase activity, chaperone activity, protein adducts, ATP-binding domain, peptide-binding domain, mouse model
- MeSH terms
- Endoplasmic Reticulum Chaperone BiP, Adenosine Triphosphatases, Aldehydes, Amino Acid Sequence, Animals, Computer Simulation, Endoplasmic Reticulum, Heat-Shock Proteins, Humans, Inflammation, Liver Diseases, Alcoholic, Male, Mice, Inbred C57BL, Models, Molecular, Protein Binding, Protein Structure, Tertiary, Protein Folding, Oxidative Stress, Mice, Unfolded Protein Response, Endoplasmic Reticulum Stress
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