Characterisation of the influences of aspirin-acetylation and glycation on human plasma proteins

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

doi:10.1016/j.jprot.2014.11.005

Cited by 17 publications

(20 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This could support the interpretation by which protein glycation favours acetylation in a process governed by a variation of intramolecular chemo-selectivity, potentially due to conformational changes that alter a dynamic equilibrium between non-reactive and reactive sites towards both PTMs. A similar trend was previously described for different plasma proteins showing the same effect of glucose on aspirin-acetylation [26]. Plasma and RBCs are the most representative components of whole blood, 58% and 42% respectively (with a very low percentage of leukocytes and platelets) and, consequently, their proteins interact more likely with glucose compared to the other two blood compartments.…”

Section: Discussionsupporting

confidence: 83%

“…Using fluorescence and circular dichroism experiments, Bakhti et al showed that glycation induces conformational changes in the secondary structure of haemoglobin, which are in turn prevented by aspirin [43]. We recently examined the impact of aspirin on human plasma in the presence of a high glucose concentration, theorizing that the observed interplay between these two PTMs may be the result of conformational changes in proteins [26]. The present study used a combination of high resolution tandem mass spectrometry coupled with label-free quantitation in order to measure the extent of acetylation and glycation on RBC proteins after incubation with a high glucose concentration (30 mM) followed by exposure to a therapeutic dose of aspirin (500 M).…”

Section: Discussionmentioning

confidence: 99%

“…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%

See 2 more Smart Citations

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

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionsupporting

confidence: 83%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

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

Self Cite

View full text Add to dashboard Cite

show abstract

“…Lys 223 is the first site that was identified in HSA to be acetylated by acetylsalicylic acid (51) and was, together with Lys 549 , detected in "pure" HSA products (52). Additionally, acetylated Lys 88 was detected in nondiabetic plasma even prior to incubation with acetylsalicylic acid (53), but none of the other sites observed after HSA or plasma incubation with acetylsalicylic acid were found (52,53). Enzymatic acetylation (and formylation) are regulatory functions in nucleus, liver cell cytosols, and mitochondria (54), but such activities have not been reported to our knowledge in plasma.…”

Section: Discussionmentioning

confidence: 99%

Plasma Proteins Modified by Advanced Glycation End Products (AGEs) Reveal Site-specific Susceptibilities to Glycemic Control in Patients with Type 2 Diabetes

Greifenhagen

Frolov

Blüher

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

Protein glycation refers to the reversible reaction between aldoses (or ketoses) and amino groups yielding relatively stable Amadori (or Heyns) products. Consecutive oxidative cleavage reactions of these products or the reaction of amino groups with other reactive substances (e.g. ␣-dicarbonyls) yield advanced glycation end products (AGEs) that can alter the structures and functions of proteins. AGEs have been identified in all organisms, and their contents appear to rise with some diseases, such as diabetes and obesity. Here, we report a pilot study using highly sensitive and specific proteomics approach to identify and quantify AGE modification sites in plasma proteins by reversed phase HPLC mass spectrometry in tryptic plasma digests. In total, 19 AGE modification sites corresponding to 11 proteins were identified in patients with type 2 diabetes mellitus under poor glycemic control. The modification degrees of 15 modification sites did not differ among cohorts of normoglycemic lean or obese and type 2 diabetes mellitus patients under good and poor glycemic control. The contents of two amide-AGEs in human serum albumin and apolipoprotein A-II were significantly higher in patients with poor glycemic control, although the plasma levels of both proteins were similar among all plasma samples. These two modification sites might be useful to predict long term, AGE-related complications in diabetic patients, such as impaired vision, increased arterial stiffness, or decreased kidney function.The reaction between reducing sugars (i.e. aldoses or ketoses) and amines is termed glycation or nonenzymatic glycosylation (1). The initially formed aldimines or ketimines can rearrange forming relatively stable Amadori or Heyns products, respectively. Consecutive rearrangements and oxidations yield advanced glycation end products (AGEs) 3 (2-6), a structurally heterogeneous group of compounds including cross-linked proteins (1). Alternatively, ␣-dicarbonyls generated by Amadori degradation (7,8), saccharide autoxidation (9, 10), lipid peroxidation (11, 12), and enzymatic reactions (13-15) can modify the side chains of lysine and arginine residues (16 -18). Degradation of glucose-derived Amadori products, for example, yields 1-deoxyglucosone (7, 19) and its tautomers, which upon nucleophilic attack by a N ⑀ -amino group of a lysine residue undergo hydrolytic ␤-cleavage yielding amide-AGEs, such as N ⑀ -acetyl-, formyl-, and glycerinyl-lysine ( Fig. 1) (20). Generally, AGEs can alter the structure of proteins contributing to diabetic retinopathy (21, 22), increased arterial stiffness (23, 24), or impaired renal function (25) along with aging and diabetes. Furthermore, receptor binding-induced activation of proinflammatory signaling pathways is associated with the development and progression of atherosclerosis (26) and nephropathy (25).AGEs have been localized in biological tissues by immunohistochemistry (27-29) and quantified with ELISA using monoclonal antibodies recognizing methylglyoxal-derived hydroimidazolone (30), imidazol...

show abstract

“…Then, a distribution of log (ratios) is calculated and a global scaling factor (the anti-log of the average of the log (ratios)) is determined. The raw intensities for each peptide among different replicates were multiplied by the global scaling factor[23]. Search was done against the decapod section of the Uniprot database (2013-03-21, 6186 sequences), using Mascot version 2.3.…”

mentioning

confidence: 99%

Label-free protein quantification in freshly ejaculated versus post-mating spermatophores of the noble crayfish Astacus astacus

Niksirat

James

Andersson

et al. 2015

Journal of Proteomics

View full text Add to dashboard Cite

Characterisation of the influences of aspirin-acetylation and glycation on human plasma proteins

Cited by 17 publications

References 44 publications

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

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

Plasma Proteins Modified by Advanced Glycation End Products (AGEs) Reveal Site-specific Susceptibilities to Glycemic Control in Patients with Type 2 Diabetes

Label-free protein quantification in freshly ejaculated versus post-mating spermatophores of the noble crayfish Astacus astacus

Contact Info

Product

Resources

About