CoChat
Sign Up
Cited by 25Alcohol Consumption and Health EffectsAlcoholism and Thiamine DeficiencyAntioxidant Activity and Oxidative Stress

PROTEIN ADDUCT SPECIES IN MUSCLE AND LIVER OF RATS FOLLOWING ACUTE ETHANOL ADMINISTRATION

B. PATEL, VINOOD, WORRALL, SIMON, EMERY, PETER W., PREEDY, VICTOR R.·2005·Alcohol and Alcoholism
DOI 10.1093/alcalc/agh196
Open this paper in CoChat — free account

Abstract

AIMS: Previous immunohistochemical studies have shown that the post-translational formation of aldehyde-protein adducts may be an important process in the aetiology of alcohol-induced muscle disease. However, other studies have shown that in a variety of tissues, alcohol induces the formation of various other adduct species, including hybrid acetaldehyde-malondialdehyde-protein adducts and adducts with free radicals themselves, e.g. hydroxyethyl radical (HER)-protein adducts. Furthermore, acetaldehyde-protein adducts may be formed in reducing or non-reducing environments resulting in distinct molecular entities, each with unique features of stability and immunogenicity. Some in vitro studies have also suggested that unreduced adducts may be converted to reduced adducts in situ. Our objective was to test the hypothesis that in muscle a variety of different adduct species are formed after acute alcohol exposure and that unreduced adducts predominate. METHODS: Rabbit polyclonal antibodies were raised against unreduced and reduced aldehydes and the HER-protein adducts. These were used to assay different adduct species in soleus (type I fibre-predominant) and plantaris (type II fibre-predominant) muscles and liver in four groups of rats administered acutely with either [A] saline (control); [B] cyanamide (an aldehyde dehydrogenase inhibitor); [C] ethanol; [D] cyanamide+ethanol. RESULTS: Amounts of unreduced acetaldehyde and malondialdehyde adducts were increased in both muscles of alcohol-dosed rats. However there was no increase in the amounts of reduced acetaldehyde adducts, as detected by both the rabbit polyclonal antibody and the RT1.1 mouse monoclonal antibody. Furthermore, there was no detectable increase in malondialdehyde-acetaldehyde and HER-protein adducts. Similar results were obtained in the liver. CONCLUSIONS: Adducts formed in skeletal muscle and liver of rats exposed acutely to ethanol are mainly unreduced acetaldehyde and malondialdehyde species.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1093/alcalc/agh196

Cites

47 of 47 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • AA adducts are formed by interaction of acetaldehyde with certain amino acids including lysine, cysteine, and aromatic amino acids; these amino acids in different proteins may exert unequal preference for AA adduct formation; proteins commonly bound include erythrocyte membrane proteins, hemoglobin, tubulin, lipoproteins, albumin, and collagen.

    “Acetaldehyde adducts (AA adducts) are formed by the interaction of acetaldehyde, a direct metabolite of ethanol oxidation and a human carcinogen, with certain amino acids, including lysine, cysteine, and aromatic amino acids.”

    From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [180]

  • Interactions between acetaldehyde or MDA and cellular proteins lead to formation of MAA adducts, which are highly stable and resistant to rapid degradation; increased MAA adducts from alcohol exposure stimulate protein dysfunction and immune-induced tissue injury through interactions with TLR-3, TLR-6, calpain, collagen alpha-1 (XII) chain, procollagen type XIV alpha-1, protocadherin beta, or补体成分.

    “Interactions between acetaldehyde or MDA and cellular proteins lead to the formation of MAA adducts, which are highly stable and resistant to rapid degradation178,179.”

    From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [180]

  • CYP2E1 contributes to the production of AA and MAA adducts, as demonstrated in experimental rodent and cell culture models.

    “In particular, CYP2E1 contributes to the production of AA and MAA adducts, as demonstrated in experimental rodent and cell culture models137,180,216,273.”

    From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [180]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Related

Authors
B. PATEL, V., WORRALL, S., EMERY, P. W., & PREEDY, V. R.
Affiliations
  • The University of Queensland (AU)
  • King's College London (GB)
ORCID
Venue
Alcohol and Alcoholism
Publisher
Oxford University Press (OUP)
Published
2005-08-30
Volume
40
Issue
6
Pages
485-493
ISSN
  • 0735-0414 (ISSN-L)
  • 1464-3502
DOI
10.1093/alcalc/agh196
OpenAlex
W2134229465
Cited by
25
References
47
Citations by year
2026: 1 · 2021: 2 · 2016: 2 · 2015: 1 · 2014: 1 · 2013: 3 · 2012: 3
FWCI
2.23
Type
journal article
Language
en
Open access
closed
Locations
  • Alcohol and Alcoholism (publishedVersion)
  • PubMed (publishedVersion)
  • Research Portal (King's College London) (submittedVersion)
Topics
  • Health Sciences › Medicine › Pathology and Forensic Medicine › Alcohol Consumption and Health Effects
  • Health Sciences › Medicine › Neurology › Alcoholism and Thiamine Deficiency
  • Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
Keywords
protein adducts, acetaldehyde, malondialdehyde, acute ethanol administration, skeletal muscle, liver, soleus muscle, plantaris muscle, aldehyde dehydrogenase inhibition, cyanamide
MeSH terms
Acetaldehyde, Ethanol, Alcoholic Intoxication, Aldehyde Dehydrogenase, Animals, Cyanamide, Enzyme-Linked Immunosorbent Assay, Liver, Liver Diseases, Alcoholic, Malondialdehyde, Muscle Proteins, Muscular Atrophy, Oxidation-Reduction, Protein Processing, Post-Translational, Rats, Wistar, Muscle, Skeletal, Muscle Fibers, Fast-Twitch, Muscle Fibers, Slow-Twitch, Rats

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review