Ida Azizkhanian1, Olgica Trenchevska2, Yara Bashawri3, Jiaqi Hu1, Juraj Koska4, Peter D Reaven4, Randall W Nelson2, Dobrin Nedelkov2, Hussein N Yassine5. 1. Department of Medicine, University of Southern California, Los Angeles, CA, USA. 2. Biodesign, Arizona State University, Tempe, AZ, USA. 3. Department of Medicine, University of Southern California, Los Angeles, CA, USA; King Fahad Medical City, Riyadh, Saudi Arabia. 4. Department of Medicine, Phoenix VA Health Care System, Phoenix, AZ, USA. 5. Department of Medicine, University of Southern California, Los Angeles, CA, USA. Electronic address: hyassine@usc.edu.
Abstract
BACKGROUND: Apolipoprotein 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. OBJECTIVE: Our objective was to characterize plasma apoA-II proteoforms in participants with and without type 2 diabetes. METHODS: Using 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. RESULTS: Six 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. CONCLUSION: The relative abundance of oxidized apoA-II is significantly increased in type 2 diabetes.
BACKGROUND:Apolipoprotein 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-IIproteoforms is not known. OBJECTIVE: Our objective was to characterize plasma apoA-IIproteoforms in participants with and without type 2 diabetes. METHODS: Using a novel mass spectrometric immunoassay, the relative abundance of apoA-IIproteoforms was examined in plasma of 30 participants with type 2 diabetes and 25 participants without diabetes. RESULTS: Six apoA-IIproteoforms (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. CONCLUSION: The relative abundance of oxidized apoA-II is significantly increased in type 2 diabetes.
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