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      Digestibility of Bovine Serum Albumin and Peptidomics of the Digests: Effect of Glycation Derived from α-Dicarbonyl Compounds

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          Abstract

          α-Dicarbonyl compounds, which are widely generated during sugar fragmentation and oil oxidation, are important precursors of advanced glycation end products (AGEs). In this study, the effect of glycation derived from glyoxal (GO), methylglyoxal (MGO) and diacetyl (DA) on the in vitro digestibility of bovine serum albumin (BSA) was investigated. Glycation from α-dicarbonyl compounds reduced digestibility of BSA in both gastric and intestinal stage of digestion according to measurement of degree of hydrolysis. Changes in peptide composition of digests induced by glycation were displayed, showing absence of peptides, occurrence of new peptides and formation of peptide-AGEs, based on the results obtained using liquid chromatography electron-spray-ionization tandem mass spectrometry (LC-ESI-MS/MS). Crosslinked glycation structures derived from DA largely reduced the sensitivity of glycated BSA towards digestive proteases based on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results. Network structures were found to remain in the digests of glycated samples by transmission electron microscope (TEM), thus the impact of AGEs in unabsorbed digests on the gut flora should be an interest for further studies.

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          Amino acid transport across mammalian intestinal and renal epithelia.

          Stefan Bröer (2008)
          The transport of amino acids in kidney and intestine is critical for the supply of amino acids to all tissues and the homeostasis of plasma amino acid levels. This is illustrated by a number of inherited disorders affecting amino acid transport in epithelial cells, such as cystinuria, lysinuric protein intolerance, Hartnup disorder, iminoglycinuria, dicarboxylic aminoaciduria, and some other less well-described disturbances of amino acid transport. The identification of most epithelial amino acid transporters over the past 15 years allows the definition of these disorders at the molecular level and provides a clear picture of the functional cooperation between transporters in the apical and basolateral membranes of mammalian epithelial cells. Transport of amino acids across the apical membrane not only makes use of sodium-dependent symporters, but also uses the proton-motive force and the gradient of other amino acids to efficiently absorb amino acids from the lumen. In the basolateral membrane, antiporters cooperate with facilitators to release amino acids without depleting cells of valuable nutrients. With very few exceptions, individual amino acids are transported by more than one transporter, providing backup capacity for absorption in the case of mutational inactivation of a transport system.
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            Increased accumulation of the glycoxidation product N(epsilon)-(carboxymethyl)lysine in human tissues in diabetes and aging.

            B. Wagner, Andreas Nerlich, E Schleicher (1997)
            N(epsilon)-(Carboxymethyl)lysine (CML), a major product of oxidative modification of glycated proteins, has been suggested to represent a general marker of oxidative stress and long-term damage to proteins in aging, atherosclerosis, and diabetes. To investigate the occurrence and distribution of CML in humans an antiserum specifically recognizing protein-bound CML was generated. The oxidative formation of CML from glycated proteins was reduced by lipoic acid, aminoguanidine, superoxide dismutase, catalase, and particularly vitamin E and desferrioxamine. Immunolocalization of CML in skin, lung, heart, kidney, intestine, intervertebral discs, and particularly in arteries provided evidence for an age-dependent increase in CML accumulation in distinct locations, and acceleration of this process in diabetes. Intense staining of the arterial wall and particularly the elastic membrane was found. High levels of CML modification were observed within atherosclerotic plaques and in foam cells. The preferential location of CML immunoreactivity in lesions may indicate the contribution of glycoxidation to the processes occurring in diabetes and aging. Additionally, we found increased CML content in serum proteins in diabetic patients. The strong dependence of CML formation on oxidative conditions together with the increased occurrence of CML in diabetic serum and tissue proteins suggest a role for CML as endogenous biomarker for oxidative damage.
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              Dicarbonyl intermediates in the maillard reaction.

              Paul Thornalley (2005)
              The complexity of the Maillard reaction arises partly from multiple fragmentation reactions of the sugar moiety, constituting branch points in the reaction progress and establishing many parallel reaction pathways. Reactive intermediates produced by these processes are often alpha-oxoaldehydes. The formation of alpha-oxoaldehydes enhances and redirects glycating activity in the Maillard reaction since alpha-oxoaldehydes are up to 20,000-fold more reactive than glucose in glycation processes and are predominantly arginine-directed glycating agents. alpha-Oxoaldehydes bypass a requirement for a fructosamine precursor in the formation of advanced glycation end products (AGEs) since alpha-oxoaldehydes react with proteins (also nucleotides and basic phospholipids) to form AGEs directly. The major AGE formed from alpha-oxoaldehydes is generally a hydroimidazolone with other products-although for glyoxal, N(omega)-carboxymethylarginine is a major product. alpha-Oxoaldehyde formation also occurs in the absence of an amine substrate, particularly during heat processing of sugar solutions and lipid peroxidation processes-in the latter case, the glycation adducts are advanced lipoxidation products (ALEs). Hydroimidazolones are quantitatively important AGEs in cellular and extracellular proteins in physiological systems. Hydroimidazolone free adducts are liberated by cellular proteolysis and digestion. They are released into blood plasma for urinary excretion. Modification of arginine residues by alpha-oxoaldehydes may be particularly damaging since arginine residues have high-frequency occurrence in ligand and substrate recognition sites in receptor and enzyme active sites. Along with fructosamine formation, alpha-oxoaldehyde intermediates of the Maillard reaction represent a major source of damage to the proteome and genome.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Molecules
                Journal ID (iso-abbrev): Molecules
                Journal ID (publisher-id): molecules
                Title: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
                Publisher: MDPI
                ISSN (Electronic): 1420-3049
                Publication date (Electronic): 21 March 2018
                Publication date Collection: April 2018
                Volume: 23
                Issue: 4
                Electronic Location Identifier: 712
                Affiliations
                [1 ]College of Food Science and Engineering, South China University of Technology, 381 Wushan Road, Guangzhou 510640, China; shengbulei@ 123456outlook.com
                [2 ]Department of Food Science, Aarhus University, Blichers Allé 20, 8830 Tjele, Denmark; lbl@ 123456food.au.dk (L.B.L.); thaothithu.le@ 123456ecu.au (T.T.L.)
                Author notes
                [* ]Correspondence: di.zhao.scut@ 123456hotmail.com ; Tel.: +86-135-703-07327
                Author information
                https://orcid.org/0000-0001-9674-0107
                Article
                Publisher ID: molecules-23-00712
                DOI: 10.3390/molecules23040712
                PMC ID: 6017377
                PubMed ID: 29561799
                SO-VID: dc2fab5c-e673-4ee5-83e3-2fa52261bdc4
                Copyright © © 2018 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 05 January 2018
                Date accepted : 07 March 2018
                Categories
                Subject: Article

                Keywords: α-dicarbonyl compounds,glycation,advanced glycation end products,digestibility,bovine serum albumin
                Data availability:
                Keywords: α-dicarbonyl compounds, glycation, advanced glycation end products, digestibility, bovine serum albumin

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