Effects of non-enzymatic glycation in human serum albumin. Spectroscopic analysis

Szkudlarek, Agnieszka; Sułkowska, Anna; Maciążek-Jurczyk, Małgorzata; Chudzik, Mariola; Równicka-Zubik, J.

doi:10.1016/j.saa.2015.01.120

Cited by 46 publications

(25 citation statements)

References 38 publications

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“…The samples were diluted to a protein concentration of 1 mg mL −1 with PBS (pH 7.4) and kept at 25 °C. Fluorescence emission spectra (350–550 nm) of the BSA glycation products were recorded at an excitation wavelength of 335 nm and slit widths of 5 nm . Fluorescence emission spectra (290–410 nm) of the BSA were recorded at an excitation wavelength of 280 nm and slit widths of 5 nm.…”

Section: Methodsmentioning

confidence: 99%

Differentiation of glycated residue numbers on heat‐induced structural changes of bovine serum albumin

2017

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Section: Methodsmentioning

confidence: 99%

Differentiation of glycated residue numbers on heat‐induced structural changes of bovine serum albumin

2017

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“…In vitro GA has also been intensively characterized by fluorescence studies [97,124,130,131]. An interesting feature of fluorescence (and Raman spectroscopy, see Section 3.2.10) is that these measurements can be performed in a noninvasive manner.…”

Section: Fluorescence Spectrometrymentioning

confidence: 99%

“…Circular dichroism spectrometry is frequently used because it provides direct information about the secondary structure composition of the protein [97,164,98,[165][166][167]. Fluorescence spectroscopic studies have investigated effects of glycation of tryptophan fluorescence, which can report local structural changes, but these studies can be complicated by the presence of glycation-derived chromophores absorbing at the Trp fluorescence emission wavelength [124,130]. Other techniques to investigate glycation-induced structural changes in albumin include differential scanning calorimetry [97,164,98], Fourier transform infrared spectrometry (FT-IR) [168], the binding of hydrophobic site probe molecules, such as anilinonaphthalene-8-sulfonate (ANS) [166], and monoclonal antibodies [169].…”

Section: Structural Consequences Of Albumin Glycationmentioning

confidence: 99%

“…The two major drug-binding sites are Sudlow site I and site II [170][171][172], but other sites for drug binding exist as well [173,174]. Drug binding to GA has been investigated for several drugs, including warfarin [175][176][177], acetohexamide [178], tolbutamide [179], phenylbutazone [180], diclofenac [181], captopril [182], diazepam [183], ketoprofen [130,184], and others. The observed effects of glycation on drug binding are drug and glycation dependent, are not generally predictable and sometime contradictory.…”

Section: Effect Of Glycation Of Albumin On Drug Bindingmentioning

confidence: 99%

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Glycated Serum Albumin and AGE Receptors

Vetter

2015

Advances in Clinical Chemistry

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“…This type of in vitro model would mimic the cross-links and AGEs generation. Finally, AGEs can glycate some plasmatic proteins, such as globulins or albumin, changing their physicochemical properties [20, 21]. …”

Section: Introductionmentioning

confidence: 99%

Increased AGE-RAGE ratio in idiopathic pulmonary fibrosis

et al. 2016

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BackgroundThe abnormal epithelial-mesenchymal restorative capacity in idiopathic pulmonary fibrosis (IPF) has been recently associated with an accelerated aging process as a key point for the altered wound healing. The advanced glycation end-products (AGEs) are the consequence of non-enzymatic reactions between lipid and protein with several oxidants in the aging process. The receptor for AGEs (RAGEs) has been implicated in the lung fibrotic process and the alveolar homeostasis. However, this AGE-RAGE aging pathway has been under-explored in IPF.MethodsLung samples from 16 IPF and 9 control patients were obtained through surgical lung biopsy. Differences in AGEs and RAGE expression between both groups were evaluated by RT-PCR, Western blot and immunohistochemistry. The effect of AGEs on cell viability of primary lung fibrotic fibroblasts and alveolar epithelial cells was assessed. Cell transformation of fibrotic fibroblasts cultured into glycated matrices was evaluated in different experimental conditions.ResultsOur study demonstrates an increase of AGEs together with a decrease of RAGEs in IPF lungs, compared with control samples. Two specific AGEs involved in aging, pentosidine and Nε-Carboxymethyl lysine, were significantly increased in IPF samples. The immunohistochemistry identified higher staining of AGEs related to extracellular matrix (ECM) proteins and the apical surface of the alveolar epithelial cells (AECs) surrounding fibroblast foci in fibrotic lungs. On the other hand, RAGE location was present at the cell membrane of AECs in control lungs, while it was almost missing in pulmonary fibrotic tissue. In addition, in vitro cultures showed that the effect of AGEs on cell viability was different for AECs and fibrotic fibroblasts. AGEs decreased cell viability in AECs, even at low concentration, while fibroblast viability was less affected. Furthermore, fibroblast to myofibroblast transformation could be enhanced by ECM glycation.ConclusionsAll of these findings suggest a possible role of the increased ratio AGEs-RAGEs in IPF, which could be a relevant accelerating aging tissue reaction in the abnormal wound healing of the lung fibrotic process.

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Effects of non-enzymatic glycation in human serum albumin. Spectroscopic analysis

Cited by 46 publications

References 38 publications

Differentiation of glycated residue numbers on heat‐induced structural changes of bovine serum albumin

Differentiation of glycated residue numbers on heat‐induced structural changes of bovine serum albumin

Glycated Serum Albumin and AGE Receptors

Increased AGE-RAGE ratio in idiopathic pulmonary fibrosis

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