Glycosylation is a major pathway for posttranslational modification of tissue protein and begins with nonenzymatic addition of carbohydrate to the primary amino groups. Excessive glycation of tissue protein has been implicated in the pathogenesis of diabetes and ageing. While glycation of aminophospholipids has also been postulated, glycated aminophospholipids have not been isolated. Using normal phase HPLC with on-line electrospray mass spectrometry we found glycated ethanolamine phospholipids to make up 10-16% of the total phosphatidylethanolamine (PE) of the red blood cells and plasma of the diabetic subjects. The corresponding values for glycated PE of control subjects were 1-2%.
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http://dx.doi.org/10.1016/0014-5793(96)00064-6 | DOI Listing |
Adv Carbohydr Chem Biochem
November 2023
Department of Biochemistry, University of Missouri, Columbia, MO, United States. Electronic address:
1-Amino-1-deoxy-d-fructose (fructosamine, FN) derivatives are omnipresent in all living organisms, as a result of non-enzymatic condensation and Amadori rearrangement reactions between free glucose and biogenic amines such as amino acids, polypeptides, or aminophospholipids. Over decades, steady interest in fructosamine was largely sustained by its role as a key intermediate structure in the Maillard reaction that is responsible for the organoleptic and nutritional value of thermally processed foods, and for pathophysiological effects of hyperglycemia in diabetes. New trends in fructosamine research include the discovery and engineering of FN-processing enzymes, development of advanced tools for hyperglycemia monitoring, and evaluation of the therapeutic potential of both fructosamines and FN-recognizing proteins.
View Article and Find Full Text PDFMolecules
January 2020
Department of Physiological Chemistry, Faculty of Chemistry, University of Vienna, Vienna 1090, Austria.
Non-enzymatic browning reactions between lipid aldehydes and aminophospholipids might play an important role in the oxidative stability of cold-pressed vegetable oils. We, therefore, aimed to study the Maillard-type reaction between hexanal, a lipid oxidation product of linoleic acid, and phosphatidylethanolamine (PE (16:0/18:1)) at a ratio of 2:1 at conditions representative of the extraction of cold-pressed soybean oils (CPSBO) and determine the radical scavenging activity of the carbonyl-amine adducts with the 2,2-diphenyl-1-picrylhydrazyl (DPPH) assay. The reaction product, 2-pentyl-3,5-dibutyl-dihydropyridine, could be identified by means of LC-ESI-QTOF-MS/MS.
View Article and Find Full Text PDFBiochim Biophys Acta Proteins Proteom
November 2019
Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700064, India; Homi Bhabha National Institute, Mumbai 400094, India. Electronic address:
Spectrin, the major protein component of the erythrocyte membrane skeleton has chaperone like activity and is known to bind membrane phospholipids and hemoglobin. We have probed the chaperone activity of spectrin in presence of hemoglobin and phospholipid SUVs of different compositions to elucidate the effect of phospholipid/hemoglobin binding on chaperone function. It is seen that spectrin displays a preference for hemoglobin over other substrates leading to a decrease in chaperone activity in presence of hemoglobin.
View Article and Find Full Text PDFFree Radic Biol Med
November 2019
Mass Spectrometry Centre, Department of Chemistry & QOPNA, University of Aveiro, Campus Universitário de Santiago, 3810-193, Aveiro, Portugal. Electronic address:
The aminophospholipids (APL), phosphatidylethanolamine (PE) and phosphatidylserine (PS) are widely present in cell membranes and lipoproteins. Glucose and reactive oxygen species (ROS), such as the hydroxyl radical (OH), can react with APL leading to an array of oxidised, glycated and glycoxidised derivatives. Modified APL have been implicated in inflammatory diseases and diabetes, and were identified as signalling molecules regulating cell death.
View Article and Find Full Text PDFMass Spectrom Rev
August 2019
Mass Spectrometry Centre, Department of Chemistry and QOPNA, University of Aveiro, Campus Universitário de Santiago, 3810-193, Aveiro, Portugal.
The biological functions of modified aminophospholipids (APL) have become a topic of interest during the last two decades, and distinct roles have been found for these biomolecules in both physiological and pathological contexts. Modifications of APL include oxidation, glycation, and adduction to electrophilic aldehydes, altogether contributing to a high structural variability of modified APL. An outstanding technique used in this challenging field is mass spectrometry (MS).
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