Aspirin prevents the nonenzymatic glycosylation and carbamylation of the human eye lens crystallins in vitro

Rao, Gadiparthi N.; Cotlier, Edward

doi:10.1016/s0006-291x(88)80463-7

Cited by 42 publications

(25 citation statements)

References 16 publications

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“…Both in vitro and in vivo experiments have shown that the protecting effect of ASA against glycation is due to a non-enzymatic transacetylation affecting the reactive amino groups in proteins (Rao and Cotlier, 1988;Crompton et al, 1985;Rao et al, 1985). Rendell et al (1986) studied the inhibitory effect of ASA on albumin glycation and concluded that the sites of glycation coincide with those of transacetylation.…”

Section: Discussionmentioning

confidence: 99%

“…Rendell et al (1986) studied the inhibitory effect of ASA on albumin glycation and concluded that the sites of glycation coincide with those of transacetylation. To confirm transacetylation Rao and Cotlier (1988) used 14 Clabelled ASA to treat human lens crystallins in vitro and undoubtedly showed that the 14 C-radioactive atom is covalently bound to the proteins. In similar experiments Cherian and Abraham (1993) have found that the 14 C-radioactive atoms of ASA are preferentially (four times more) incorporated into the rat gamma-crystallin molecules compared to the alpha-and beta-crystallins.…”

Section: Discussionmentioning

confidence: 99%

“…Using [ 14 C]-acetylsalicylic acid Rao and Cotlier (1988) proved that the inhibition of glycation of human and rat eye crystallins was due to the acetylation of their side chain amino groups. It was also shown that ASA blocks by acetylation the glycation of hemoglobin (Rendell et al, 1986), collagen (Malik and Meek, 1996), bovine crystallins (Ajiboye and Harding, 1989), etc.…”

Section: Introductionmentioning

confidence: 99%

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Inhibitory Effect of Some Acetyl Esters and Acetamides on Glycation of the Histone H1

Stoynev

Srebreva

Gugova

et al. 2008

Zeitschrift Für Naturforschung C

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Non-enzymatic glycosylation (glycation) is a spontaneous set of reactions between reducing sugars and free amino groups in proteins or other biomolecules leading to the formation of fluorescent and coloured compounds known as advanced glycation end products (AGEs). AGEs cause structural changes of key proteins in humans, and therefore they are related with a number of physiological processes and diseases such as aging, atherosclerosis, cataract, arthritis, Alzheimer's disease. Two main strategies have been employed to prevent the formation of AGEs: a) low carbohydrate diet and b) pharmacological intervention. The latter includes treatment with reactive compounds which might be either sugar competitors (type A), carbonyl traps (type B) or free radical trapping antioxidants (type C). Acetylsalicylic acid (ASA, aspirin) is a good example of sugar competitor capable of inhibiting glycation by acetylating ε-amino groups of lysine residues in proteins. Taking into consideration the inhibiting effect of ASA on glycation we designed to study the antiglycation activity of other acetyl group-containing compounds (acetamides and acetyl esters) using the lysine-rich protein histone H1 as a model. The glycation of the histone H1 was carried out by either fructose or a complex mixture of glycating agents obtained from E. coli and monitored by fluorescent spectroscopy, SDS-PAGE and measurement of the content of reactive carbonyl groups in the target protein. Our results showed that the inhibitory effect of phenyl acetate, acetanilide, 4-acetamidophenylacetic acid and isopropenyl acetate was comparable to that of ASA. Based on the obtained results we conclude that these compounds act as free radical scavengers protecting proteins from the damaging effect of reactive oxygen species produced during the formation of AGEs.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Inhibitory Effect of Some Acetyl Esters and Acetamides on Glycation of the Histone H1

Stoynev

Srebreva

Gugova

et al. 2008

Zeitschrift Für Naturforschung C

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“…The formation of new glycation-induced cross-links is slowed by several drugs and natural substances [21][22][23][24]. It has been reported that aspirin and amino guanidine inhibit the formation of pathological AGEs cross-links [25][26][27][28][29][30][31][32][33][34]. It has been previously shown that glycation and subsequent AGEs formation alters the molecular packing of collagen, both in vivo and in vitro [35][36][37][38].…”

Section: Introductionmentioning

confidence: 99%

Aggregation and self assembly of non-enzymatic glycation of collagen in the presence of amino guanidine and aspirin: An in vitro study

Usha

Jaimohan

Rajaram

et al. 2010

International Journal of Biological Macromolecules

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“…It was demonstrated that aspirin pro tected the crystallins from carbamylation [9] and reaction with glucosamine [10], galactose [11] and glucose [12], The protective effect was increased by pre-incubation with aspirin [9,13] and was demonstrated to be due to ace tylation of the crystallins [9,13,14], Ibuprofen has been shown to decrease the rate of crystallin binding by glucosamine [10], fructose [15], galactose and cyanate [16]. However, in the case of aspirin-like analge sics, such as ibuprofen and paracetamol, the mechanism of protection is not likely to be via acetylation.…”

Section: Introductionmentioning

confidence: 99%

Ibuprofen Protects Alpha-Crystallin against Posttranslational Modification by Preventing Protein Cross-Linking

1997

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Posttranslational modification of bovine α-crystallin by D-erythrose-4-phosphate, fructose-6-phosphate, .D-ribose-5-phosphate and carbamylation using potassium cyanate induced the loss of chaperone-like activity, as assessed by γ-crystallin aggregation. The presence of high-molecular-weight aggregates indicated that erythrosylated, fructosylated and carbamylated α-crystallins were modified by non-reducible cross-linking. In contrast, ribosylation of α-crystallin induced the formation of reducible cross-links. Analysis of ribosylated, erythrosylated and carbamylated α-crystallin using non-denaturing acrylamide gels showed that the cross-linking did not sterically inhibit the normal aggregate formation or alter the oligomerisation of the aggregate. Co-incubation of ibuprofen in the presence of α-crystallin and the modifying agents protected the chaperone-like activity of α-crystallin, enabling the inhibition of γ-crystallin aggregation. In addition, ibuprofen inhibited the formation of both reducible and non-reducible cross-linked high-molecular-weight α-crystallin aggregates. We show in this paper that ibuprofen can inhibit in vitro cross-linking events responsible for the loss of chaperone-like activity of α-crystallin and suggest that the protective effect of ibuprofen may be exerted by the binding of ibuprofen breakdown products to α-crystallin lysine groups, preventing posttranslational modification responsible for the loss of chaperone-like activity.

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Aspirin prevents the nonenzymatic glycosylation and carbamylation of the human eye lens crystallins in vitro

Cited by 42 publications

References 16 publications

Inhibitory Effect of Some Acetyl Esters and Acetamides on Glycation of the Histone H1

Inhibitory Effect of Some Acetyl Esters and Acetamides on Glycation of the Histone H1

Aggregation and self assembly of non-enzymatic glycation of collagen in the presence of amino guanidine and aspirin: An in vitro study

Ibuprofen Protects Alpha-Crystallin against Posttranslational Modification by Preventing Protein Cross-Linking

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