Acetaldehyde substoichiometrically inhibits bovine neurotubulin polymerization.
Open accessAbstract
Acetaldehyde is known to form covalent adducts with tubulin and to inhibit microtubule formation. Available evidence indicates that lysine residues are prominently involved in adduct formation. Previous work has shown that lysines on tubulin can be divided into two general classes based upon their reactivity toward acetaldehyde; those of normal reactivity ("bulk" lysines) and a highly reactive lysine (HRL) located on the alpha-polypeptide subunit. We took advantage of the fact that the HRL is unreactive when tubulin is in the microtubule form to differentiate the effects of bulk from HRL adducts on tubulin polymerization. Under conditions where both bulk lysines and HRL formed adducts, 0.2 mol acetaldehyde/mol tubulin caused complete inhibition of polymerization. When we modified bulk lysines, but not HRL, tubulin polymerized essentially normally. Finally, when we first blocked bulk lysines on microtubules (HRL unreactive) using unlabeled acetaldehyde and then measured the amount of [14C]acetaldehyde adduct formed with tubulin after depolymerization (HRL reactive), 0.08 mol acetaldehyde/mol tubulin resulted in completely impaired polymerization. These data show that microtubule formation is very sensitive to even small mole fractions of acetaldehyde-modified tubulin (especially with HRL) and further suggest that small amounts of acetaldehyde adduct could be damaging to cytoskeleton function in the cell.
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Acetaldehyde can interact with dopamine to produce AA-DA adducts, including salsolinol, a neurotoxin and potent stimulant in alcohol, which is involved in the pathogenesis of AUD and PD.
“Furthermore, acetaldehyde can interact with dopamine (DA) to produce AA-DA adducts, including salsolinol, a neurotoxin and potent stimulant in alcohol, which is involved in the pathogenesis of AUD and PD194,195.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [194]
AA-protein adducts are widely present in the brains of alcohol-exposed rodents or people with AUD; after alcohol consumption they are rapidly produced in the cerebral cortex primarily with mitochondrial proteins and localized in white matter, deep layers of the frontal cortex, and molecular layer of the cerebellum; they also form AA-tubulin adducts causing microtubule malformation and cytoskeletal
“AA-protein adducts are widely present in the brains of alcohol-exposed rodents or people with alcohol use disorder (AUD)189–192.”
From Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury (2021) · cites this paper as [194]
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- Authors
- Smith, S. L., Jennett, R. B., Sorrell, M. F., & Tuma, D. J.
- Affiliations
- Nebraska Medical Center (US)
- Venue
- Journal of Clinical Investigation
- Published
- 1989-07-01
- Volume
- 84
- Issue
- 1
- Pages
- 337-341
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC303987
- OpenAlex
- W2169530207
- Cited by
- 73
- References
- 20
- Citations by year
- 2024: 2 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 1 · 2015: 2 · 2014: 2 · 2013: 2 · 2012: 2
- FWCI
- 1.53
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Alcohol Abuse and Alcoholism (AA-04961)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Physical Sciences › Chemistry › Organic Chemistry › Synthesis and biological activity
- Keywords
- acetaldehyde, microtubule assembly, microtubule formation, lysine adducts, alpha-tubulin, covalent modification, cytoskeleton damage
- MeSH terms
- Acetaldehyde, Animals, Cattle, Lysine, Microtubules, Polymers, Tubulin Modulators
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