The principal site of nonenzymatic glycosylation of human serum albumin in vivo.

Garlick, Robert; Mazer, J S

doi:10.1016/s0021-9258(18)32384-6

Cited by 291 publications

(54 citation statements)

References 40 publications

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“…Day et al (1979) noticed that acetylation of serum albumin by aspirin inhibited glycosylation of the protein in vitro. The basis of this inhibition is not simply competition for identical binding sites since the major human serum albumin modification site for aspirin is Lys-199 whereas the major glycosylation site is Lys-525 (Walker, 1976;Garlick & Mazer, 1983). It is therefore probable that acetylation induces a conformational change which masks the glucose-binding site.…”

Section: Discussionmentioning

confidence: 99%

Conformational changes induced in lens α- and γ-crystallins by modification with glucose 6-phosphate. Implications for cataract

Beswick

Harding

1987

Biochemical Journal

116

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There is good evidence that the non-enzymic chemical modification of proteins plays a role in the aetiology of cataract and diabetic sequelae. This paper presents new evidence that glycosylation of two major lens structural crystallins, alpha- and gamma-crystallins, by glucose 6-phosphate (G6P) induces conformational changes in the proteins. In addition the surface charge on the molecules is altered. These changes would affect protein-protein and protein-water interactions within the lens and could lead to disruption of the short-range order of the lens proteins which is essential for lens transparency. Conformational changes to lens proteins are known to occur in human cataractous lenses but their cause in vivo is not established. Cumulative chemical modification of proteins, over a period of decades, is a strong candidate as a causal agent.

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Section: Discussionmentioning

confidence: 99%

Conformational changes induced in lens α- and γ-crystallins by modification with glucose 6-phosphate. Implications for cataract

Beswick

Harding

1987

Biochemical Journal

116

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“…Residues like lysine (Lys), arginine (Arg) and cysteine (Cys) due to their nucleophilic characteristics are accountable to glycation under different experimental conditions. Literatures indicate that Lys 525 is the major glycation site along with Lys 525, Lys 199, 281 and 489 that play a significant contribution to glycation (Garlick & Mazer, 1983;Shaklai, Garlick, & Bunn, 1984;Iberg & Fluckiger, 1986).…”

Section: Carbonyl Content From Dnph Assaymentioning

confidence: 99%

Glycation of human serum albumin alters its binding efficacy towards the dietary polyphenols: a comparative approach

Roy

Ghosh

Dasgupta

2015

Journal of Biomolecular Structure and Dynamics

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Diabetes is a major problem in the world. The proteins became modified during glycation after reacting with the reducing sugars (e.g. D-glucose) via non-enzymatic pathways. The glycated analogue of human serum albumin (HSA) has been characterized with the help of multi-spectroscopic methods. It has been observed that six glucose molecules can bind covalently to HSA under experimental condition. The binding affinity of the modified HSA towards the dietary polyphenols has been estimated using UV-vis and fluorescence spectroscopic techniques. The binding constant values of the ligands were found to decrease after the modification of HSA.

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“…In Figure 2 , we can find that some sites ( e.g. , K20, K41, R145, R197, R209, K212, R222, R337, and K524) had never been identified in analyses of glycation modifications, indicating that they are insensitive to changes in glucose concentrations, and further explorations of the underlying mechanism are needed to determine their roles[ 64 - 71 ].…”

Section: Methods For Assessment Of Glycated Hsamentioning

confidence: 99%

Comprehensive overview of human serum albumin glycation in diabetes mellitus

Qiu¹,

Hou²,

Shi³

et al. 2021

WJD

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The presence of excess glucose in blood is regarded as a sweet hurt for patients with diabetes. Human serum albumin (HSA) is the most abundant protein in human plasma, which undergoes severe non-enzymatic glycation with glucose in patients with diabetes; this modifies the structure and function of HSA. Furthermore, the advanced glycation end products produced by glycated HSA can cause pathological damage to the human body through various signaling pathways, eventually leading to complications of diabetes. Many potential glycation sites on HSA have different degrees of sensitivity to glucose concentration. This review provides a comprehensive assessment of the in vivo glycation sites of HSA; it also discusses the effects of glycation on the structure and function of HSA. Moreover, it addresses the relationship between HSA glycation and diabetes complications. Finally, it focuses on the value of non-enzymatic glycation of HSA in diabetes-related clinical applications.

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The principal site of nonenzymatic glycosylation of human serum albumin in vivo.

Cited by 291 publications

References 40 publications

Conformational changes induced in lens α- and γ-crystallins by modification with glucose 6-phosphate. Implications for cataract

Conformational changes induced in lens α- and γ-crystallins by modification with glucose 6-phosphate. Implications for cataract

Glycation of human serum albumin alters its binding efficacy towards the dietary polyphenols: a comparative approach

Comprehensive overview of human serum albumin glycation in diabetes mellitus

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