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Full-Text Articles in Chemistry
Myeloperoxidase-Mediated Protein Lysine Oxidation Generates 2- Aminoadipic Acid And Lysine Nitrile In Vivo, Hongqiao Lin, Bruce S. Levison, Jennifer A. Buffa, Ying Huang, Xiaoming Fu, Zeneng Wang, Valentin Gogonea, Joseph A. Didonato, Stanley L. Hazen
Myeloperoxidase-Mediated Protein Lysine Oxidation Generates 2- Aminoadipic Acid And Lysine Nitrile In Vivo, Hongqiao Lin, Bruce S. Levison, Jennifer A. Buffa, Ying Huang, Xiaoming Fu, Zeneng Wang, Valentin Gogonea, Joseph A. Didonato, Stanley L. Hazen
Chemistry Faculty Publications
Recent studies reveal 2-aminoadipic acid (2-AAA) is both elevated in subjects at risk for diabetes and mechanistically linked to glucose homeostasis. Prior studies also suggest enrichment of protein-bound 2-AAA as an oxidative post-translational modification of lysyl residues in tissues associated with degenerative diseases of aging. While in vitro studies suggest redox active transition metals or myeloperoxidase (MPO) generated hypochlorous acid (HOCl) may produce protein-bound 2-AAA, the mechanism(s) responsible for generation of 2- AAA during inflammatory diseases are unknown. In initial studies we observed that traditional acid- or basecatalyzed protein hydrolysis methods previously employed to measure tissue 2-AAA can artificially generate …
A Systematic Investigation Of Structure/Function Requirements For The Apolipoprotein A-I/Lecithin Cholesterol Acyltransferase Interaction Loop Of High-Density Lipoprotein, Xiaodong Gu, Zhiping Wu, Ying Huang, Matthew A. Wagner, Camelia Baleanu Gogonea, Ryan A. Mehl, Jennifer A. Buffa, Anthony J. Didonato, Leah B. Hazen, Paul L. Fox, Valentin Gogonea, John S. Parks, Joseph A. Didonato, Stanley L. Hazen
A Systematic Investigation Of Structure/Function Requirements For The Apolipoprotein A-I/Lecithin Cholesterol Acyltransferase Interaction Loop Of High-Density Lipoprotein, Xiaodong Gu, Zhiping Wu, Ying Huang, Matthew A. Wagner, Camelia Baleanu Gogonea, Ryan A. Mehl, Jennifer A. Buffa, Anthony J. Didonato, Leah B. Hazen, Paul L. Fox, Valentin Gogonea, John S. Parks, Joseph A. Didonato, Stanley L. Hazen
Chemistry Faculty Publications
The interaction of lecithin-cholesterol acyltransferase (LCAT) with apolipoprotein A-I (apoA-I) plays a critical role in high-density lipoprotein (HDL) maturation. We previously identified a highly solvent-exposed apoA-I loop domain (Leu159–Leu170) in nascent HDL, the so-called “solar flare” (SF) region, and proposed that it serves as an LCAT docking site (Wu, Z., Wagner, M. A., Zheng, L., Parks, J. S., Shy, J. M., 3rd, Smith, J. D., Gogonea, V., and Hazen, S. L. (2007) Nat. Struct. Mol. Biol. 14, 861–868). The stability and role of the SF domain of apoA-I in supporting HDL binding and activation of LCAT are debated. Here we …
Site-Specific Nitration Of Apolipoprotein A-I At Tyrosine 166 Is Both Abundant Within Human Atherosclerotic Plaque And Dysfunctional, Joseph A. Didonato, Kulwant Aulak, Ying Huang, Matthew A. Wagner, Gary Gerstenecker, Celalettin Topbas, Valentin Gogonea, Anthony J. Didonato, W.H. Wilson Tang, Ryan A. Mehl, Paul L. Fox, Edward F. Plow, Jonathan D. Smith, Edward A. Fisher, Stanley L. Hazen
Site-Specific Nitration Of Apolipoprotein A-I At Tyrosine 166 Is Both Abundant Within Human Atherosclerotic Plaque And Dysfunctional, Joseph A. Didonato, Kulwant Aulak, Ying Huang, Matthew A. Wagner, Gary Gerstenecker, Celalettin Topbas, Valentin Gogonea, Anthony J. Didonato, W.H. Wilson Tang, Ryan A. Mehl, Paul L. Fox, Edward F. Plow, Jonathan D. Smith, Edward A. Fisher, Stanley L. Hazen
Chemistry Faculty Publications
We reported previously that apolipoprotein A-I (apoA-I) is oxidatively modified in the artery wall at tyrosine 166 (Tyr166), serving as a preferred site for post-translational modification through nitration. Recent studies, however, question the extent and functional importance of apoA-I Tyr166 nitration based upon studies of HDL-like particles recovered from atherosclerotic lesions. We developed a monoclonal antibody (mAb 4G11.2) that recognizes, in both free and HDL-bound forms, apoA-I harboring a 3-nitrotyrosine at position 166 apoA-I (NO2-Tyr166-apoA-I) to investigate the presence, distribution, and function of this modified apoA-I form in atherosclerotic and normal artery wall. We also developed recombinant apoA-I with site-specific …