Identification of N<sup>7</sup>‐(1‐Carboxyethyl)‐Arginine, a Novel Posttranslational Protein Modification of Arginine Formed at High Hydrostatic Pressure

Alt, Nadja; Schieberle, Peter

doi:10.1196/annals.1333.006

Cited by 5 publications

(5 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Here, as illustrated in Fig. 5, the homologous structure N 7 -carboxyethyl arginine (CEA) [50,51] is a minor intermediate of the equilibrium between a kinetically controlled (MG-H3) and a thermodynamically controlled imidazolinone (MG-H1) [52]. In the methylglyoxal reactions the various cyclic imidazolinone and pyrimidine derivatives are Fig.…”

Section: Isomerizationmentioning

confidence: 99%

Pathways of the Maillard reaction under physiological conditions

2016

View full text Add to dashboard Cite

Initially investigated as a color formation process in thermally treated foods, nowadays, the relevance of the Maillard reaction in vivo is generally accepted. Many chronic and age-related diseases such as diabetes, uremia, atherosclerosis, cataractogenesis and Alzheimer's disease are associated with Maillard derived advanced glycation endproducts (AGEs) and α-dicarbonyl compounds as their most important precursors in terms of reactivity and abundance. However, the situation in vivo is very challenging, because Maillard chemistry is paralleled by enzymatic reactions which can lead to both, increases and decreases in certain AGEs. In addition, mechanistic findings established under the harsh conditions of food processing might not be valid under physiological conditions. The present review critically discusses the relevant α-dicarbonyl compounds as central intermediates of AGE formation in vivo with a special focus on fragmentation pathways leading to formation of amide-AGEs.

show abstract

Section: Isomerizationmentioning

confidence: 99%

Pathways of the Maillard reaction under physiological conditions

2016

View full text Add to dashboard Cite

show abstract

“…Limited information is available on acrylamide formation during HP/HT processing. Exploratory studies, mostly restricted to specific Maillard reaction products and limited in processing conditions (with regard to the number and range of temperature and pressure levels), indicated a retarding effect of high pressure on the Maillard reaction (Hill, Ledward, & Ames, 1996;Schwarzenbolz, Klostermeyer, & Henle, 2000;Frank, Heberle, Schieberle, & Hofmann, 2002;Deters, Hofmann, & Schieberle, 2003;Heberle, Schieberle, & Hofmann, 2003;Moreno, Molina, Olano, & Lopez-Fandino, 2003;Alt & Schieberle, 2005;Jaeger, Janositz, & Knorr, 2010).…”

Section: Acrylamide Formationmentioning

confidence: 99%

(Bio)chemical reactions during high pressure/high temperature processing affect safety and quality of plant-based foods

Plancken

Verbeyst

Vleeschouwer

et al. 2012

Trends in Food Science & Technology

View full text Add to dashboard Cite

In recent years, the range of equipment and applications for high pressure pasteurization has gradually increased on the European market. Sterilization under conditions of elevated pressures is in the pipeline, albeit at the research level. Knowledge on the effect of high pressure/high temperature processing on food safety and quality attributes is still too limited. This review discusses recent progress made in understanding the impact of high pressure/high temperature processing on food safety and quality attributes of fruit and vegetable based products, within the EU FP6 integrated project NovelQ. Methodological approach for kinetic studies under HP/HT conditionsWhen performing a kinetic study, process parameters need to be, if not kept constant, at least documented as completely as possible. Rate constants strongly depend on pressure and temperature, both critical process parameters in HP/HT processing. Therefore, incorrectly assuming that process parameters are constant or inadequate knowledge of the temperature, pressure history will lead to incorrect estimates of the kinetic parameters (e.g. rate constants, activation energy and activation volume). Moreover these cannot then be extrapolated to different equipment (Van der Plancken et al., 2008). This is even more pertinent, when larger scale high pressure vessels are used, in which major temperature non-uniformity may arise (Grauwet, Van der Plancken,

show abstract

“… Structural formulas showing different advanced glycation end products (AGEs). Structural formulas of advanced glycation end products (AGEs) formed from lysine [ 95 , 108 , 109 ] ( A ), arginine [ 95 , 110 , 111 , 112 ] ( B ), or cysteine [ 83 , 95 , 113 ] ( C ) and glyoxal (GO; black) or methylglyoxal (MGO; blue). …”

Section: Introductionmentioning

confidence: 99%

Glycation Interferes with the Activity of the Bi-Functional UDP-N-Acetylglucosamine 2-Epimerase/N-Acetyl-mannosamine Kinase (GNE)

et al. 2023

View full text Add to dashboard Cite

Mutations in the gene coding for the bi-functional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE), the key enzyme of the sialic acid biosynthesis, are responsible for autosomal-recessive GNE myopathy (GNEM). GNEM is an adult-onset disease with a yet unknown exact pathophysiology. Since the protein appears to work adequately for a certain period of time even though the mutation is already present, other effects appear to influence the onset and progression of the disease. In this study, we want to investigate whether the late onset of GNEM is based on an age-related effect, e.g., the accumulation of post-translational modifications (PTMs). Furthermore, we also want to investigate what effect on the enzyme activity such an accumulation would have. We will particularly focus on glycation, which is a PTM through non-enzymatic reactions between the carbonyl groups (e.g., of methylglyoxal (MGO) or glyoxal (GO)) with amino groups of proteins or other biomolecules. It is already known that the levels of both MGO and GO increase with age. For our investigations, we express each domain of the GNE separately, treat them with one of the glycation agents, and determine their activity. We demonstrate that the enzymatic activity of the N-acetylmannosamine kinase (GNE-kinase domain) decreases dramatically after glycation with MGO or GO—with a remaining activity of 13% ± 5% (5 mM MGO) and 22% ± 4% (5 mM GO). Whereas the activity of the UDP-N-acetylglucosamine 2-epimerase (GNE-epimerase domain) is only slightly reduced after glycation—with a remaining activity of 60% ± 8% (5 mM MGO) and 63% ± 5% (5 mM GO).

show abstract

Identification of N⁷‐(1‐Carboxyethyl)‐Arginine, a Novel Posttranslational Protein Modification of Arginine Formed at High Hydrostatic Pressure

Cited by 5 publications

References 3 publications

Pathways of the Maillard reaction under physiological conditions

Pathways of the Maillard reaction under physiological conditions

(Bio)chemical reactions during high pressure/high temperature processing affect safety and quality of plant-based foods

Glycation Interferes with the Activity of the Bi-Functional UDP-N-Acetylglucosamine 2-Epimerase/N-Acetyl-mannosamine Kinase (GNE)

Contact Info

Product

Resources

About

Identification of N7‐(1‐Carboxyethyl)‐Arginine, a Novel Posttranslational Protein Modification of Arginine Formed at High Hydrostatic Pressure

Cited by 5 publications

References 3 publications

Pathways of the Maillard reaction under physiological conditions

Pathways of the Maillard reaction under physiological conditions

(Bio)chemical reactions during high pressure/high temperature processing affect safety and quality of plant-based foods

Glycation Interferes with the Activity of the Bi-Functional UDP-N-Acetylglucosamine 2-Epimerase/N-Acetyl-mannosamine Kinase (GNE)

Contact Info

Product

Resources

About

Identification of N⁷‐(1‐Carboxyethyl)‐Arginine, a Novel Posttranslational Protein Modification of Arginine Formed at High Hydrostatic Pressure