ArticleJournal of clinical lipidology
Posttranslational modifications of apolipoprotein A-II proteoforms in type 2 diabetes.
Article in Journal of clinical lipidology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The trial behind it
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- HDL metabolism and function in diabetes mellitus.Nature reviews. Endocrinology · 2026Review
- Antioxidant and Anti-Inflammatory Functions of High-Density Lipoprotein in Type 1 and Type 2 Diabetes.Antioxidants (Basel, Switzerland) · 2023Review
- Apolipoprotein A-II, a Player in Multiple Processes and Diseases.Biomedicines · 2022Review
- The Human Proteoform Atlas: a FAIR community resource for experimentally derived proteoforms.Nucleic acids research · 2022Article
- Dysfunctional High-Density Lipoproteins in Type 2 Diabetes Mellitus: Molecular Mechanisms and Therapeutic Implications.Journal of clinical medicine · 2021Review
- A high-throughput mass spectrometry-based assay for large-scale profiling of circulating human apolipoproteins.Journal of lipid research · 2020Article
- Mass Spectrometric Studies of Apolipoprotein Proteoforms and Their Role in Lipid Metabolism and Type 2 Diabetes.Proteomes · 2017Review
- Association of Cystatin C Proteoforms with Estimated Glomerular Filtration Rate.Clinical mass spectrometry (Del Mar, Calif.) · 2016Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundApolipoprotein A-II (apoA-II) is the second most abundant protein in high-density lipoprotein particles. However, it exists in plasma in multiple forms. The effect of diabetes on apoA-II proteoforms is not known.
objectiveOur objective was to characterize plasma apoA-II proteoforms in participants with and without type 2 diabetes.
methodsUsing a novel mass spectrometric immunoassay, the relative abundance of apoA-II proteoforms was examined in plasma of 30 participants with type 2 diabetes and 25 participants without diabetes.
resultsSix apoA-II proteoforms (monomer, truncated TQ monomer, truncated Q monomer, dimer, truncated Q dimer, and truncated 2Qs dimer) and their oxidized proteoforms were identified. The ratios of oxidized monomer and all oxidized proteoforms to the native apoA-II were significantly greater in the diabetic group (P = .004 and P = .005, respectively) compared with the nondiabetic group.
conclusionThe relative abundance of oxidized apoA-II is significantly increased in type 2 diabetes.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.