Generation of protein carbonyls by glycoxidation and lipoxidation reactions with autoxidation products of ascorbic acid and polyunsaturated fatty acids

Miyata, Toshio; Inagi, Reiko; Asahi, Koichi; Yamada, Yuzo; Horie, Kuniaki; Sakai, Hideto; Uchida, Koji; Kurokawa, Kiyoshi

doi:10.1016/s0014-5793(98)01079-5

Cited by 127 publications

(74 citation statements)

References 37 publications

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“…In our study, lower levels of protein carbonyls were found in the pathological group, which had a slightly higher protein concentration compared to the reference group. This result is not in accordance with previous findings that defend the accumulation of protein carbonyls in vascular lesions as a common phenomenon in most, if not all, types of vascular damage (56). However, in our study, the higher plasma protein level in the pathological group could lead to a carbonyl/protein ratio lower than that observed in the other groups.…”

Section: Redox Balance In Atherosclerosis 67contrasting

confidence: 99%

“…The evaluation of the carbonyl groups in plasma proteins is a respected marker of free-radical reaction intensity (27,55) in aging and in various diseases (56)(57)(58). In our study, lower levels of protein carbonyls were found in the pathological group, which had a slightly higher protein concentration compared to the reference group.…”

Section: Redox Balance In Atherosclerosis 67supporting

confidence: 46%

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Systemic Markers of the Redox Balance and Apolipoprotein E Polymorphism in Atherosclerosis: The Relevance for an Integrated Study

Lopes

Napoleão

Pinheiro

et al. 2006

BTER

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H u m a n a J o u r n a l s . c o mS e a r c h , R e a d a n d D o w n l o a d Featured in this issue: ABSTRACTProspective studies have demonstrated that an imbalance between oxidative damage and antioxidative protection can play a role in the development and progression of atherosclerosis. Also, genotypes with the apolipoprotein E ε4 allele have been associated with an increase risk for this pathology. Based on this knowledge, the aim of this study was to evaluate indicators of the redox balance, trace elements, and apolipoprotein E allelic profile in subjects from the Lisbon population with clinically stable atherosclerosis, at risk for atherosclerotic events, and in healthy subjects for comparison. The activities of superoxide dismutase in erythrocytes and glutathione peroxidase in whole blood, plasma total thiols, and serum ceruloplasmin were kept unchanged among the three groups. Serum α-tocopherol was increased in atherosclerotic patients. *Author to whom all correspondence and reprint requests should be addressed.lipid and protein oxidative damage, respectively, reached their highest values in risk subjects. The concentrations of potassium and calcium, in plasma and in blood cells, were slightly elevated in patients and might reflect an electrolytic imbalance. Regarding the apolipoprotein E polymorphism, atherosclerotic patients had an increased incidence of the high-risk genotypes for atherogenesis (ε3/ε4 and ε4/ε4). A multivariate model applied to the general population using most of the parameters clearly separated the three groups at study (i.e., the healthy group from the steady-state group of risk disease and from the atherosclerotic one). As shown by us, the usefulness of biochemical and complementary genetic markers is warranted for a better knowledge on atherosclerosis molecular basis.

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Section: Redox Balance In Atherosclerosis 67contrasting

confidence: 99%

Section: Redox Balance In Atherosclerosis 67supporting

confidence: 46%

Systemic Markers of the Redox Balance and Apolipoprotein E Polymorphism in Atherosclerosis: The Relevance for an Integrated Study

Lopes

Napoleão

Pinheiro

et al. 2006

BTER

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“…Potential mechanisms mediating this role include the LDL oxidation (34), enhanced expression of cell adhesion molecules (35), impairment of endothelial-dependent vasodilatation (36), and the increased formation of advanced glycation end products (37). Dietary antioxidants may be protective against oxidative stress and thereby atherosclerosis.…”

Section: T T H E S E L E C T E D F a C T O R S I N C L U D E Dmentioning

confidence: 99%

A Cross-Sectional Study of the Effects of Type 2 Diabetes and Other Cardiovascular Risk Factors on Structure and Function of Nonstenotic Arteries of the Lower Limb

O’Neal¹,

Dragicevic²,

Rowley³

et al. 2003

Diabetes Care

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OBJECTIVE -To compare intimal-medial thickness (IMT) and pulse wave conduction velocity (PWCV) in unstenosed arteries of the lower limb in subjects with and without type 2 diabetes and to determine the contribution of a range of cardiovascular risk factors.RESEARCH DESIGN AND METHODS -IMT and PWCV were determined in lowerlimb arteries of 79 subjects with diabetes and 77 euglycemic subjects. Plasma lipids were determined by enzymatic assays, and LDL particle size was measured by gradient gel electrophoresis. Lag time for copper-induced oxidation of LDL was determined. ␣-Tocopherol, retinol, and ascorbate levels were determined by high-performance liquid chromatography, soluble E-selectin by enzyme-linked immunosorbent assay, and fibrinogen and factor VII by automated assays.RESULTS -Subjects with diabetes had greater superficial femoral artery (SFA) IMT, popliteal artery (PA) IMT, and SFA PWCV (all P Ͻ 0.0001). In univariate analysis, IMT and PWCV correlated with increased waist-to-hip ratio, triglycerides, and fibrinogen and inversely with HDL cholesterol and LDL size. Ascorbate was inversely associated with IMT, and LDL lag time was inversely correlated with PWCV. Subjects with the greatest number of features of the metabolic syndrome had the highest IMT and PWCV.CONCLUSIONS -Adverse changes in the structure and function of unstenosed lower-limb arteries are present in type 2 diabetes and are associated with features of the metabolic syndrome.

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“…Both the arginine and (hydroxy-)lysine content of cartilage collagen decrease significantly with age, implying an age-related increase in amino acid modification. The age-related modification of amino acids can be due to several processes, including glycation and lipid oxidation [31,32]. Furthermore, the modification of (hydroxy-)lysine residues can also be the result of enzymic collagen cross-linking.…”

Section: Maillard Reaction Products In Articular Cartilage Collagenmentioning

confidence: 99%

Age-related accumulation of Maillard reaction products in human articular cartilage collagen

Verzijl

DeGroot

Oldehinkel³

et al. 2000

Biochemical Journal

239

100

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Non-enzymic modification of tissue proteins by reducing sugars, the so-called Maillard reaction, is a prominent feature of aging. In articular cartilage, relatively high levels of the advanced glycation end product (AGE) pentosidine accumulate with age. Higher pentosidine levels have been associated with a stiffer collagen network in cartilage. However, even in cartilage, pentosidine levels themselves represent 1 cross-link per 20 collagen molecules, and as such cannot be expected to contribute substantially to the increase in collagen network stiffness. In the present study, we investigated a broad range of Maillard reaction products in cartilage collagen in order to determine whether pentosidine serves as an adequate marker for AGE levels. Not only did the well-characterized AGEs pentosidine, N ε -(carboxymethyl)lysine, and N ε -(carboxyethyl)lysine increase with age in cartilage collagen (all P 0.0001), but also general measures of AGE cross-linking, such as browning and fluorescence (both P 0.0001), increased. The levels of these AGEs are all higher in cartilage collagen than in skin collagen. INTRODUCTIONDuring aging, long-lived proteins such as collagen and eye lens proteins are non-enzymically modified by reducing sugars. The major initial product is fructose-lysine (FL) [1,2], which results from glycation of ε-amino groups on lysine residues. In subsequent Maillard or browning reactions, products known as advanced glycation end products (AGEs) are formed from FL [3,4], and accumulate with age in long-lived proteins [1,2,[5][6][7][8]. These AGEs include structurally characterized adducts, such as N ε -(carboxymethyl)lysine (CML) [1][2][3] and N ε -(carboxyethyl)-lysine (CEL) [9], fluorescent cross-links, such as pentosidine formed between lysine and arginine residues [5,10], as well as chemically unidentified compounds which result in proteinbound browning or fluorescence, and cross-linking [11][12][13][14].In comparison with other collagen-rich tissues such as skin, cartilage contains relatively large amounts of pentosidine [5,15]. Pentosidine levels in articular cartilage increase linearly with age [6-8], as was previously described for skin collagen [16] and lens proteins [10]. Pentosidine is also present in the proteoglycans in articular cartilage [17], but appears to be localized predominantly in the collagen component of the tissue [7]. Age-related accumulation of AGE cross-links in articular cartilage collagen may result in increased stiffening of the collagen network, as was shown after in itro ribosylation of cartilage [7]. Thus AGE cross-linking in i o may contribute to the age-related impairment of the ability of articular collagen to resist mechanically induced damage and eventually cartilage degeneration [18][19][20].Abbreviations used : AGE, advanced glycation end product ; CEL, N ε -(carboxyethyl)lysine ; CML, N ε -(carboxymethyl)lysine ; FL, fructose-lysine. 1 To whom correspondence should be addressed (e-mail JM.TeKoppele!pg.tno.nl).As a functional measure of glycation the digestibility o...

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Generation of protein carbonyls by glycoxidation and lipoxidation reactions with autoxidation products of ascorbic acid and polyunsaturated fatty acids

Cited by 127 publications

References 37 publications

Systemic Markers of the Redox Balance and Apolipoprotein E Polymorphism in Atherosclerosis: The Relevance for an Integrated Study

Systemic Markers of the Redox Balance and Apolipoprotein E Polymorphism in Atherosclerosis: The Relevance for an Integrated Study

A Cross-Sectional Study of the Effects of Type 2 Diabetes and Other Cardiovascular Risk Factors on Structure and Function of Nonstenotic Arteries of the Lower Limb

Age-related accumulation of Maillard reaction products in human articular cartilage collagen

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