The preferential site of non-enzymatic glycation of human apolipoprotein A-I in vivo

Calvo, Carlos; Ulloa, Natalia; Campos, María; Verdugo, Cecilia; Ayrault-Jarrier, M

doi:10.1016/0009-8981(93)90165-z

Cited by 18 publications

(11 citation statements)

References 16 publications

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“…With the instrument at hand we only found glycated ApoA-I forms in the C-terminal end. The detected glycated and non-glycated forms of Y5 fragments support earlier reports of ApoA-I glycation at position, K263 [9], Fig. 2 and Supplementary data Table 1.…”

Section: Glycated Apoa-isupporting

confidence: 91%

A fast semi-quantitative LC–MS method for measurement of intact apolipoprotein A-I reveals novel proteoforms in serum

Gåfvels

Bengtson²

2015

Clinica Chimica Acta

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Section: Glycated Apoa-isupporting

confidence: 91%

A fast semi-quantitative LC–MS method for measurement of intact apolipoprotein A-I reveals novel proteoforms in serum

Gåfvels

Bengtson²

2015

Clinica Chimica Acta

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“…These discrepancies are probably due to variations in the study populations and the methods used to measure cholesterol esterification [15]. Although there is evidence suggesting that glycation of apoA-I in HDL impairs the LCAT reaction in vivo and in vitro [20][21][22], the underlying mechanism of these observations are not understood. These issues are addressed in the present study using preparations of discoidal reconstituted HDL (rHDL) containing apoA-I and phosphatidylcholine ([A-I]rHDL).…”

Section: Introductionmentioning

confidence: 99%

The impact of glycation on apolipoprotein A-I structure and its ability to activate lecithin:cholesterol acyltransferase

et al. 2007

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Aims/hypothesis Hyperglycaemia, one of the main features of diabetes, results in non-enzymatic glycation of plasma proteins, including apolipoprotein A-I (apoA-I), the most abundant apolipoprotein in HDL. The aim of this study was to determine how glycation affects the structure of apoA-I and its ability to activate lecithin:cholesterol acyltransferase (LCAT), a key enzyme in reverse cholesterol transport. Materials and methods Discoidal reconstituted HDL (rHDL) containing phosphatidylcholine and apoA-I ([A-I] rHDL) were prepared by the cholate dialysis method and glycated by incubation with methylglyoxal. Glycation of apoA-I was quantified as the reduction in detectable arginine, lysine and tryptophan residues. Methylglyoxal-AGE adduct formation in apoA-I was assessed by immunoblotting. (A-I)rHDL size and surface charge were determined by non-denaturing gradient gel electrophoresis and agarose gel electrophoresis, respectively. The kinetics of the LCAT reaction was investigated by incubating varying concentrations of discoidal (A-I)rHDL with a constant amount of purified enzyme. The conformation of apoA-I was assessed by surface plasmon resonance. Results Methylglyoxal-mediated modifications of the arginine, lysine and tryptophan residues in lipid-free and lipidassociated apoA-I were time-and concentration-dependent. These modifications altered the conformation of apoA-I in regions critical for LCAT activation and lipid binding. They also decreased (A-I)rHDL size and surface charge. The rate of LCAT-mediated cholesterol esterification in (A-I)rHDL varied according to the level of apoA-I glycation and progressively decreased as the extent of apoA-I glycation increased. Conclusions/interpretation It is concluded that glycation of apoA-I may adversely affect reverse cholesterol transport in subjects with diabetes.

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“…chemically modified by a single glucose), not enzymatically glycosylated. 45 Some contributions to the glycomic profiles were attributable to the complement factors C4-A and C3, which were detected in the Protein L-enriched fractions and accounted for 3.4 and 2.5% of the TIC area, respectively. The complement factors are capable of binding the Fc domain of antigen-associated IgM.…”

Section: Resultsmentioning

confidence: 97%

Examination of Glycan Profiles from IgG-Depleted Human Immunoglobulins Facilitated by Microscale Affinity Chromatography

et al. 2012

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Among the most important proteins involved in the disease and healing processes are the immunoglobulins (Igs). Although many of the Igs have been studied through proteomics, aside from IgG, immunoglobulin carbohydrates have not been extensively characterized in different states of health. It seems valuable to develop techniques that permit us to understand changes in the structures and abundances of Ig glycans in the context of disease onset and progression. We have devised a strategy for characterization of the glycans for the Ig classes other than IgG (i.e. A, D, E, and M) that contain kappa light chains, while using only a few microliters of biological material. First, we designed a microcolumn containing the recombinant Protein L that was immobilized on macroporous silica particles. A similarly designed Protein G microcolumn was utilized to first perform an on-line depletion of the IgG from the sample, human blood serum, and thereby facilitate enrichment of the other Igs. While only 3 μL of serum were used in these analyses, we were able to recover a significantly-enriched fraction of non-IgG immunoglobulins. The enrichment properties of the Protein L column were characterized using a highly sensitive label-free quantitative proteomics LC-MS/MS approach, and the glycomic profiles of enriched immunoglobulins were measured by MALDI-TOF-MS. As a proof-of-principle, a comparative study was conducted using blood serum from a small group of lung cancer patients and a group of age-matched cancer-free individuals to demonstrate that the method is suitable for investigation of glycosylation changes in disease. The results were in agreement with a glycomic investigation of whole blood serum from a much larger lung cancer cohort.

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The preferential site of non-enzymatic glycation of human apolipoprotein A-I in vivo

Cited by 18 publications

References 16 publications

A fast semi-quantitative LC–MS method for measurement of intact apolipoprotein A-I reveals novel proteoforms in serum

A fast semi-quantitative LC–MS method for measurement of intact apolipoprotein A-I reveals novel proteoforms in serum

The impact of glycation on apolipoprotein A-I structure and its ability to activate lecithin:cholesterol acyltransferase

Examination of Glycan Profiles from IgG-Depleted Human Immunoglobulins Facilitated by Microscale Affinity Chromatography

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