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

6 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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/j.jacl.2016.03.001

Cite this

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

@article{793582f8b8ae42d7a06bbc158c5106db,

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. ",

year = "2016",

month = jul,

day = "1",

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

language = "English (US)",

volume = "10",

pages = "808--815",

journal = "Journal of Clinical Lipidology",

issn = "1933-2874",

publisher = "Elsevier BV",

number = "4",

}

TY - JOUR

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

UR - http://www.scopus.com/inward/record.url?scp=84963969074&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84963969074&partnerID=8YFLogxK

U2 - 10.1016/j.jacl.2016.03.001

DO - 10.1016/j.jacl.2016.03.001

M3 - Article

C2 - 27578111

AN - SCOPUS:84963969074

VL - 10

SP - 808

EP - 815

JO - Journal of Clinical Lipidology

JF - Journal of Clinical Lipidology

SN - 1933-2874

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this