Posttranslational modifications of apolipoprotein A-II proteoforms in type 2 diabetes

Ida Azizkhanian; Olgica Trenchevska; Yara Bashawri; Jiaqi Hu; Juraj Koska; Peter D. Reaven; Randall W. Nelson; Dobrin Nedelkov; Hussein N. Yassine

doi:10.1016/j.jacl.2016.03.001

Posttranslational modifications of apolipoprotein A-II proteoforms in type 2 diabetes

Ida Azizkhanian, Olgica Trenchevska, Yara Bashawri, Jiaqi Hu, Juraj Koska, Peter D. Reaven, Randall W. Nelson, Dobrin Nedelkov, Hussein N. Yassine

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

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.

Original language	English (US)
Pages (from-to)	808-815
Number of pages	8
Journal	Journal of Clinical Lipidology
Volume	10
Issue number	4
DOIs	https://doi.org/10.1016/j.jacl.2016.03.001
State	Published - Jul 1 2016

Keywords

Apolipoprotein A-II
Diabetes
Mass spectrometry
Oxidations

ASJC Scopus subject areas

Internal Medicine
Endocrinology, Diabetes and Metabolism
Nutrition and Dietetics
Cardiology and Cardiovascular Medicine

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10.1016/j.jacl.2016.03.001

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Posttranslational modifications of apolipoprotein A-II proteoforms in type 2 diabetes. / Azizkhanian, Ida; Trenchevska, Olgica; Bashawri, Yara; Hu, Jiaqi; Koska, Juraj; Reaven, Peter D.; Nelson, Randall W.; Nedelkov, Dobrin; Yassine, Hussein N.

In: Journal of Clinical Lipidology, Vol. 10, No. 4, 01.07.2016, p. 808-815.

Research output: Contribution to journal › Article › peer-review

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title = "Posttranslational modifications of apolipoprotein A-II proteoforms in type 2 diabetes",

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.",

keywords = "Apolipoprotein A-II, Diabetes, Mass spectrometry, Oxidations",

author = "Ida Azizkhanian and Olgica Trenchevska and Yara Bashawri and Jiaqi Hu and Juraj Koska and Reaven, {Peter D.} and Nelson, {Randall W.} and Dobrin Nedelkov and Yassine, {Hussein N.}",

note = "Funding Information: Dr Yassine was supported by K23HL107389 from National Institute of Heart, Lung and Blood , 15BGIA25690024 from the American Heart Association , and USC CTSI pilot UL1TR000130 . Mass spectrometry work was supported by Awards R01DK082542 and R24DK090958 from the National Institute of Diabetes And Digestive and Kidney Diseases. ",

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doi = "10.1016/j.jacl.2016.03.001",

language = "English (US)",

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T1 - Posttranslational modifications of apolipoprotein A-II proteoforms in type 2 diabetes

AU - Azizkhanian, Ida

AU - Trenchevska, Olgica

AU - Bashawri, Yara

AU - Hu, Jiaqi

AU - Koska, Juraj

AU - Reaven, Peter D.

AU - Nelson, Randall W.

AU - Nedelkov, Dobrin

AU - Yassine, Hussein N.

N1 - Funding Information: Dr Yassine was supported by K23HL107389 from National Institute of Heart, Lung and Blood , 15BGIA25690024 from the American Heart Association , and USC CTSI pilot UL1TR000130 . Mass spectrometry work was supported by Awards R01DK082542 and R24DK090958 from the National Institute of Diabetes And Digestive and Kidney Diseases.

PY - 2016/7/1

Y1 - 2016/7/1

N2 - 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.

AB - 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.

KW - Apolipoprotein A-II

KW - Diabetes

KW - Mass spectrometry

KW - Oxidations

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Posttranslational modifications of apolipoprotein A-II proteoforms in type 2 diabetes

Abstract

Keywords

ASJC Scopus subject areas

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