Impact of high glucose concentration on aspirin-induced acetylation of human serum albumin: An in vitro study

Finamore, Francesco; Priego-Capote, Feliciano; Gluck, Florent; Zufferey, Anne; Fontana, Pierre; Sanchez, Jean‐Charles

doi:10.1016/j.euprot.2014.02.001

Cited by 11 publications

(10 citation statements)

References 54 publications

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“…Whereas pre-glycated BSA incubated with acetyl group containing molecules showed decrease in the glycation. ASP, BIS, NDS-458, PAR, ACZ, ACH and NAC showed decrease in glycated peptides by 12,9,11,15,15,13,14 respectively as shown in Figure 3B, details of the modified peptides are listed in (Supplementary Table 1). A representative MS/MS annotation of Amadori modified peptide of BSA is depicted in (Supplementary Figure 3).…”

Section: Lc Ms/ms Analysis Of Glycated Bsamentioning

confidence: 91%

“…Therefore, implication of lysine acetylation in various biological processes and complex association with cellular metabolism offers lot of clinical relevance. Recently, acetylation and glycation prone sites on HSA and other plasma proteins were characterized and quantified for better understanding of their interplay and Please do not adjust margins Please do not adjust margins reciprocal competition 12,13 . Aspirin mediated acetylation and protein glycation influence each other through a dynamic equilibrium between acetylation and glycation 13 .…”

Section: Introductionmentioning

confidence: 99%

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Molecules with O-acetyl group protect protein glycation by acetylating lysine residues

et al. 2016

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Pharmaceutical intervention for reduction of advanced glycation products (AGEs) is considered as a therapeutic strategy to attenuate the pathogenesis of diabetes. Many molecules have been reported to possess antiglycation activity, one such example is acetylsalicylic acid (Aspirin). It protects proteins from glycation by acetylating the lysine residues. Therefore, in this study we have synthesized and screened molecules containing free N-, O-acetyl and acetophenone group. All the selected molecules in this study showed glycation inhibition but interestingly, only molecules with O-acetyl but not Nacetyl and acetophenone group were capable of acetylating lysine residue . Furthermore, we have demonstrated that preacetylation or aspirin treatment prior to the induction of diabetes helps in reducing HbA1c and AGE formation in the streptozotocin induced diabetic mice. Hence pre-acetylation may have an additional therapeutic efficacy of reducing AGE levels in-vivo. Incorporation of O-acetyl group into anti-diabetic molecules could be an useful strategy, as it may have an additive effect in reducing AGEs. Identification of such novel acetylating agents represents a new area in the drug discovery process.

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Section: Lc Ms/ms Analysis Of Glycated Bsamentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Molecules with O-acetyl group protect protein glycation by acetylating lysine residues

et al. 2016

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“…Moreover, acetylation of lysine residues in hen egg white lysozyme has been recently indicated to enhance fibrillation of this protein (Morshedi, Ebrahim-Habibi, Moosavi-Movahedi & Nemat-Gorgani 2010). Under physiological conditions (37 °C, pH 7.4), this reaction is relatively fast and follows a first order kinetics, dependent only on the concentration of aspirin (Finamore et al 2014). Despite the fact that insulin is the most important peptide hormone in the body, the possibility of its modification by aspirin has been little known.…”

Section: ►Fig1 To Be Inserted Here◄mentioning

confidence: 98%

Aspirin-mediated acetylation induces structural alteration and aggregation of bovine pancreatic insulin

Yousefi

Taheri

Alavi

et al. 2015

Journal of Biomolecular Structure and Dynamics

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The simple aggregation of insulin under various chemical and physical stresses is still an important challenge for both pharmaceutical production and clinical formulation. In the storage form, this protein is subjected to various chemical modifications which alter its physicochemical and aggregation properties. Aspirin (acetylsalicylic acid) which is the most widely used medicine worldwide has been indicated to acetylate a large number of proteins both in vitro and in vivo. In this study, as insulin treated with aspirin at 37°C, a significant level of acetylation was observed by flourescamine and o-phthalaldehyde assay. Also, different spectroscopic techniques, gel electrophoresis, and microscopic assessment were applied to compare the structural variation and aggregation/fibrillation propensity among acetylated and non-acetylated insulin samples. The results of spectroscopic assessments elucidate that acetylation induces insulin unfolding which is accompanied with the exposure of protein hydrophobic patches, a transition from alpha-helix to beta-sheet and increased propensity of the protein for aggregation. The kinetic studies propose that acetylation increases aggregation rate of insulin under both thermal and chemical stresses. Also, gel electrophoresis and dynamic light scattering experiments suggest that acetylation induces insulin oligomerization. Additionally, the results of Thioflavin T fluorescence study, Congo red absorption assessment, and microscopic analysis suggest that acetylation with aspirin enhances the process of insulin fibrillation. Overall, the increased susceptibility of acetylated insulin for aggregation may reflect the fact that this type of modification has significant structural destabilizing effect which finally makes the protein more vulnerable for pathogenic aggregation/fibrillation.

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“…An experimental mass spectrometry (MS) approach, previously applied to serum albumin [25] and human plasma [26], was used to obtain qualitative information, by detecting acetylation and glycation sites, as well as quantitative reports determining the levels of these modifications.…”

Section: Introductionmentioning

confidence: 99%

Aspirin-mediated acetylation of haemoglobin increases in presence of high glucose concentration and decreases protein glycation

Finamore

Priego-Capote

Nolli³

et al. 2015

EuPA Open Proteomics

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Aspirin-mediated acetylationRed blood cells Haemoglobin Mass spectrometry Label-free a b s t r a c t Glycation represents the first stage in the development of diabetic complications. Aspirin was shown to prevent sugars reacting with proteins, but the exact mechanism of this interaction was not well defined. We performed a quantitative analysis to calculate the levels of acetylation and glycation of haemoglobin, among others red blood cell (RBC) proteins, using a label free approach. After glucose incubation, increases in the acetylation levels were seen for several haemoglobin subunits, while a parallel decrease of their glycation levels was observed after aspirin incubation. These results suggest that, a mutual influence between these two modifications, occur at protein level.

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Impact of high glucose concentration on aspirin-induced acetylation of human serum albumin: An in vitro study

Cited by 11 publications

References 54 publications

Molecules with O-acetyl group protect protein glycation by acetylating lysine residues

Molecules with O-acetyl group protect protein glycation by acetylating lysine residues

Aspirin-mediated acetylation induces structural alteration and aggregation of bovine pancreatic insulin

Aspirin-mediated acetylation of haemoglobin increases in presence of high glucose concentration and decreases protein glycation

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