Investigations on Protein Nonenzymatic Glycation by a New and Effective Mass Spectrometric Method

Traldi, Pietro; Lapolla, Annunziata; Seraglia, Roberta; Catinella, Silvia; D’Alpaos, Martina; Aronica, Rosaria; Fedele, Domenico

doi:10.1006/mchj.1996.0098

Cited by 4 publications

(3 citation statements)

References 7 publications

(8 reference statements)

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“…A review on the use of mass spectrometry for the study of this process has appeared together with a more general review of analytical methods (Deyl & Miksik, 1997). Albumin is a favorite model molecule for such studies (Traldi et al, 1996) and MALDI monitoring of advanced glycation endproducts (AGEs) of albumin has been proposed as a surveillance method for the clinical management of uremea (Thornalley et al, 2000). Formation of a-oxoaldehydes that are important precursors of AGEs, have been investigated and shown to be capable of formation in both early and late stages of glycation (Thornalley, Langborg, & Minhas, 1999).…”

Section: Glycated Proteinsmentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update covering the period 1999–2000

Harvey

2006

Mass Spectrometry Reviews

125

112

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This review describes the use of matrix-assisted laser desorption/ionization (MALDI) mass spectrometry for the analysis of carbohydrates and glycoconjugates and continues coverage of the field from the previous review published in 1999 (D. J. Harvey, Matrix-assisted laser desorption/ionization mass spectrometry of carbohydrates, 1999, Mass Spectrom Rev, 18:349-451) for the period 1999-2000. As MALDI mass spectrometry is acquiring the status of a mature technique in this field, there has been a greater emphasis on applications rather than to method development as opposed to the previous review. The present review covers applications to plant-derived carbohydrates, N- and O-linked glycans from glycoproteins, glycated proteins, mucins, glycosaminoglycans, bacterial glycolipids, glycosphingolipids, glycoglycerolipids and related compounds, and glycosides. Applications of MALDI mass spectrometry to the study of enzymes acting on carbohydrates (glycosyltransferases and glycosidases) and to the synthesis of carbohydrates, are also covered.

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Section: Glycated Proteinsmentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update covering the period 1999–2000

Harvey

2006

Mass Spectrometry Reviews

125

112

View full text Add to dashboard Cite

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“…Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry was proved to be a valid tool to evaluate the glycation level of HSA. After some investigations of in vitro glycation processes on selected proteins, [15][16][17][18][19] extensive studies on healthy subjects and on well-controlled and badly controlled diabetic patients were undertaken. It was shown that a clear increase of the m/z value of the [M + H] + species from HSA, as well as other plasma proteins (IgG and hemoglobin ), is present in the case of the patients.…”

Section: Introductionmentioning

confidence: 99%

Glycated Human Serum Albumin Isolated from Poorly Controlled Diabetic Patients Impairs Cholesterol Efflux from Macrophages: An Investigation by Mass Spectrometry

Traldi

Castilho

Sartori

et al. 2015

Eur J Mass Spectrom (Chichester)

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Advanced glycation end-products impair ABCA-1-mediated cholesterol efflux by eliciting inflammation, the generation of reactive oxygen species and endoplasmatic reticulum (ER) stress. The glycation level of human serum albumin (HSA) from type 1 and type 2 diabetic patients was determined by matrix assisted laser desorption/ionization (MALDI) mass spectrometry and related to possible impairment of ER function and cellular cholesterol efflux. Comparison of the MALDI spectra from healthy and diabetic subjects allowed us to determine an increased HSA mean mass of 1297 Da for type 1 and 890 Da for type 2. These values reflect a mean condensation of at least 8 glucose units and 5 glucose units, respectively. Mouse peritoneal macrophages were treated with HSA from control, type 1 and type 2 diabetic subjects in order to measure the expression of Grp78, Grp94, protein disulfide isomerase (PDI), calreticulin (CRT) and ABCA-1. (14)C-cholesterol overloaded-J774 macrophages were treated with HSA from control and diabetic subjects and further incubated with apo A-1 to determine the cholesterol efflux. Combined analyses comprising HSA from type 1 and type 2 diabetic patients were performed in cellular functional assays. In macrophages, PDI expression increased 89% and CRT 3.4 times in comparison to HSA from the control subjects. ABCA-1 protein level and apo A-I mediated cholesterol efflux were, respectively, 50% and 60% reduced in macrophages exposed to HSA from type 1 and type 2 diabetic patients when compared to that exposed to HSA from control subjects. We provide evidence that the level of glycation that occurs in albumin in vivo damages the ER function related to the impairment in macrophage reverse cholesterol transport and so contributes to atherosclerosis in diabetes.

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“…Studies on the Maillard reaction of food proteins themselves generally employ indirect methods to provide evidence of Maillard chemistry; these include monitoring the loss of lysine during reaction, browning reactions (Friedman, 1996), or immunochemical detection (Pischetsrieder et al, 1997). The direct study of Maillard products of food proteins has received little attention (Kim et al, 1997) despite excellent recent work in the medical arena (Lapolla et al, 1996;Tang et al, 1996;Traldi et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Covalent Protein Adduct Formation and Protein Cross-Linking Resulting from the Maillard Reaction between Cyclotene and a Model Food Protein

Gerrard¹,

Fayle²,

Sutton³

1999

J. Agric. Food Chem.

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Covalent Maillard products of the reactions of carbonyl compounds with proteins are often described in the literature, but, until recently, evidence for their existence has been indirect. Cyclotene (2-hydroxy-3-methylcyclopent-2-enone), a common flavor compound, was incubated with a model food protein, ribonuclease, and found to cross-link the protein. Size exclusion high-performance liquid chromatrography and electrospray mass spectrometry of the early stages of the reaction provide strong evidence for covalent adducts that we believe to be intermediates in the cross-linking reaction.

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Investigations on Protein Nonenzymatic Glycation by a New and Effective Mass Spectrometric Method

Cited by 4 publications

References 7 publications

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update covering the period 1999–2000

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update covering the period 1999–2000

Glycated Human Serum Albumin Isolated from Poorly Controlled Diabetic Patients Impairs Cholesterol Efflux from Macrophages: An Investigation by Mass Spectrometry

Covalent Protein Adduct Formation and Protein Cross-Linking Resulting from the Maillard Reaction between Cyclotene and a Model Food Protein

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