New fluorescence of nonenzymatically glucosylated human serum albumin

Sakurai, Tamiko; Takahashi, Hiroshi; Tsuchiya, Susumu

doi:10.1016/0014-5793(84)80905-9

Cited by 19 publications

(13 citation statements)

References 16 publications

(6 reference statements)

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“…Proteins with AGE are reported to display characteristic increases in emmission at around 430 nm following excitation at 370 nm [7][8][9]. Figure i shows the emission spectra of fresh BSA, AGE-BSA, and control BSA.…”

Section: Resultsmentioning

confidence: 99%

“…Such treatment has been shown to be sufficient for the accumulation of large amounts of AGE on albumin [9,10]. Control BSA was treated similarly.…”

Section: Preparation Of a Ge-bsamentioning

confidence: 99%

“…Proteins with advanced glycosylation end products are reported to emit increased fluorescence at 430 nm upon excitation at 370 nm [7][8][9]. The emission spectra of AGE-BSA, control B SA, and fresh B SA were measured by preparing suspensions of each (2 mg/ml) in PBS.…”

Section: Fluorescence Measurementsmentioning

confidence: 99%

“…A slow rearrangement of the ketoamines takes place, however, which is not reversible. Advanced glycosylation end products (AGE) are formed by this rearrangement, and they continue to accumulate throughout the lifetime of the protein [2,[4][5][6][7][8][9].…”

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confidence: 99%

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Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate

Gilcrease

Hoover

1990

Diabetologia

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Summary.Non-enzymatic glycosylation of proteins is thought to play an important role in the development of diabetic vascular disease. Advanced glycosylation end products have been shown to accumulate on basement membranes and collagen in diabetes, and receptors for such adducts have recently been found on murine macrophages. We have observed that human monocytes activated by endotoxin express receptors for advanced glycosylation end products of similar affinity and number as has been previously reported for murine macrophages. In addition, there is an increased adherence of activated human monocytes to a nonenzymatically glycosylated albumin substrate, and such adhesion can be competitively inhibited up to 50% by soluble, non-enzymatically glycosylated albumin. We suggest that increased adherence of activated monocytes to non-enzymatically glycosylated proteins in the vessel wall may result in monocyte stimulation and/or local monocyte accumulation and thereby contribute to vascular disease in diabetes.

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Section: Resultsmentioning

confidence: 99%

“…Such treatment has been shown to be sufficient for the accumulation of large amounts of AGE on albumin [9,10]. Control BSA was treated similarly.…”

Section: Preparation Of a Ge-bsamentioning

confidence: 99%

Section: Fluorescence Measurementsmentioning

confidence: 99%

mentioning

confidence: 99%

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Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate

Gilcrease

Hoover

1990

Diabetologia

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“…11 Such treatment has been shown to be sufficient for the accumulation of large amounts of AGE on albumin. 11,12 We verified the presence of AGE structures in our preparation of AGE-BSA by a direct ELISA using a specific antiserum to a common AGE immunological epitope found both in vitro and in vivo as described. 13 We ruled out the effect of early glycosylation products by incubating AGE-BSA with 200-fold molar excess of sodium borohydride.…”

Section: Preparation Of Age-modified Albuminmentioning

confidence: 99%

Regulation of Endothelial Nitric Oxide Synthase Expression by Albumin-Derived Advanced Glycosylation End Products

Rojas

Romay

González

et al. 2000

Circulation Research

114

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Abstract-We examined whether albumin-derived advanced glycosylation end products (AGEs) downregulate the expression of endothelial nitric oxide synthase (NOS). Significant reductions in NOS activity and cGMP levels in bovine aortic endothelial cells were observed when exposed to different concentrations of albumin-derived AGEs. Western and Northern blot analyses showed significant decreases at the protein and transcript levels. Both reductions became evident after 24 hours of exposure. Nuclear run-on assays showed that AGE-BSA did not modify the transcription rate of the NOS III gene; however, AGE-BSA treatment markedly reduced the half-life of NOS III mRNA. In addition, AGE-treated endothelial cells displayed significant reduction on their antiplatelet properties. These results indicate that NOS expression is reduced by AGEs by increasing the rate of mRNA degradation and may be relevant to the impairment of some endothelial functions observed in diabetes and aging. Key Words: advanced glycosylation end products Ⅲ nitric oxide synthase Ⅲ diabetes E ndothelial cell-generated nitric oxide (NO) accounts for the biological activity of endothelium-derived relaxing factor. NO is derived from the guanidino nitrogen atoms(s) of the amino acid L-arginine through a reaction catalyzed by NO synthase. In endothelial cells, NO synthase (NOS III) has been characterized as a constitutively expressed calcium-and calmodulin-dependent enzyme. However, the level of NOS III expression can be altered by a growing number of different stimuli. Tumor necrosis factor-␣ 1 and lipopolysaccharide 2 decrease expression of NOS III. In contrast, estrogens 3 and shear stress 4 can increase NOS III expression. The effect of hypoxia is less clear; some authors have reported either an increase 5 or decrease 6 in NOS III mRNA.Vascular diseases account for the majority of the clinical complications of diabetes mellitus. 7 Although the molecular basis of the mechanisms involved for the development of vascular disease in diabetes mellitus is poorly understood, several lines of evidences demonstrate impairment in endothelium-dependent relaxation of diabetic blood vessels. 8 Reducing sugar such as glucose can react nonenzymatically with the amino groups of proteins to form complex structures called advanced glycosylation end products (AGEs). In normal aging processes and in some pathological conditions such as diabetes, the excessive accumulation of AGEs could lead to tissue dysfunction. 9 Recently, AGEs have been shown to quench NO and, therefore, may play a role in the defective endothelium-dependent vasodilatation in experimental diabetes. 10 To our knowledge, the effect of AGEs on NOS III expression is unknown. We have undertaken the present study to test the hypothesis that AGEs reduce the expression level of NOS III. We show a significant decrease in the amount of NOS III protein and mRNA in AGE-exposed bovine endothelial cells.

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Pathophysiologic Significance

Cohen¹

1986

Diabetes and Protein Glycosylation

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New fluorescence of nonenzymatically glucosylated human serum albumin

Cited by 19 publications

References 16 publications

Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate

Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate

Regulation of Endothelial Nitric Oxide Synthase Expression by Albumin-Derived Advanced Glycosylation End Products

Pathophysiologic Significance

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