Effect of Non-Enzymatic Glycation on Cystatin: A Spectroscopic Study

Bhat, Sheraz Ahmad; Sohail, Aamir; Siddiqui, Azad Alam; Bano, Bilqees

doi:10.1007/s10895-014-1391-2

Cited by 22 publications

(19 citation statements)

References 35 publications

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“…The emission scans were obtained from 400 to 600 nm using an excitation wavelength of 385 nm on a Shimadzu spectrofluorometer at room temperature [17].…”

Section: Fluorescence Spectrometrymentioning

confidence: 99%

Vitamin D prevents glycation of proteins: an in vitro study

2016

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Human serum albumin (HSA) is an important protein involved in the transport of hormones, fatty acids, drugs, and other macromolecules. Under hyperglycemic conditions, this molecule undergoes irreversible modification that affects its structure and function. In this study, we explored the effect of two forms of vitamin D, a nutraceutical, on glycation modification in HSA. The protein was incubated with a physiologically high concentration of glucose in the presence of vitamin D metabolites. After 21 days, samples were tested for secondary structural changes, side chain modification, and the presence of advanced glycation end products. Vitamin D metabolites could reduce glycation modification, albeit only to a small extent. Interaction studies reveal that Vitamin D interaction with HSA can prevent protein glycation.Keywords: calcitriol; glycation; protein Type 2 Diabetes is a global health issue growing at an unprecedented rate. The disease accounts for 90% of diabetes cases worldwide and is characterized by defects in glucose metabolism [1]. Persistently high blood glucose concentration encountered in diabetes often initiates Maillard reaction which causes nonenzymatic glycation of proteins and yields a plethora of reactive compounds called advanced glycation end products (AGEs) [2].Modification of protein structure and function by AGEs is consistent with the progression of diabetic complications and correlates positively with the severity of conditions like retinopathy, neuropathy, and nephropathy [3]. Once initiated, AGEs formation continues throughout the lifespan of proteins, and cannot be reversed by normalizing hyperglycemia [2,4].Human serum albumin (HSA) frequently undergoes Maillard reaction to from covalently cross-linked composites [3]. In normal adults, 6-10% of lysine chains are modified by nonenzymatic glycation, however, this number increases by 2-3 folds in individuals suffering from diabetes [5]. This may interfere with HSA function [5]. Since HSA is involved in the transportation of several moieties: nutrients, steroids, and a wide variety of drugs this can have detrimental physiological effects [6].Research suggests that vitamin D is involved in controlling AGE-associated damage in both diabetes and heart disorders [7]. Vitamin D is a fat-soluble micronutrient which is produced in the body by UV irradiation of a precursor steroid stored in the skin. The functionally active form of vitamin D, calcitriol, has a wide array of health implications [8]. Multiple studies have demonstrated its ability in limiting oxidative damage and regulating the status of a potent cellular antioxidant-reduced glutathione (GSH) [7]. Vitamin D deficiency is thought to be a risk factor for the development of diabetes; Low vitamin D status is associated with increased insulin resistance, glycated hemoglobin (HbA1c), and AGE formation [9][10][11]. Previous reports have correlated low circulating concentrations of vitamin D with increased risk of diabetic macrovascular and microvascular complications: mainly nephropathy a...

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“…The emission scans were obtained from 400 to 600 nm using an excitation wavelength of 385 nm on a Shimadzu spectrofluorometer at room temperature [17].…”

Section: Fluorescence Spectrometrymentioning

confidence: 99%

Vitamin D prevents glycation of proteins: an in vitro study

2016

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“…The purification of cystatin was done by the method as reported earlier by our group [36]. 100 gm of chickpea, overnight soaked, was homogenized in homogenization buffer (50 mM sodium phosphate, 3 mM EDTA, 0.15M NaCl, pH 7.5) in a homogenizer.…”

Section: Purification Of Chickpea Cystatin (Cpc)mentioning

confidence: 99%

“…In the present work, chickpea cystatin (CPC) has been purified from chickpea seeds by the method used by Sharma et al [52] and modified by Bhat et al [36]. As detailed in the methods section, the procedure involved two steps after homogenisation, i.e., ammonium sulphate precipitation (40-60%) and gel filtration chromatography on Sephacryl S-100 HR column.…”

Section: Purification Of the Inhibitormentioning

confidence: 99%

Purification and Biochemical Characterization of a Cystatin-Like Thiol Proteinase Inhibitor from Cicer arietinum (Chickpea)

Ab¹,

Fb²,

Aaliya³

et al. 2016

J Chromatogr Sep Tech

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“…AGEs or Maillard products are heterogeneous molecules produced through the non-enzymatic reaction of proteins with reducing sugars [5,6,7] ( Figure 1). The multitude of physiological processes occurring in the body determines their continuous formation in cells and tissues.…”

Section: Introductionmentioning

confidence: 99%

“…The multitude of physiological processes occurring in the body determines their continuous formation in cells and tissues. However, the AGE formation rate is increased in DM as a consequence of hyperglycemia [8,6]. A great number of studies suggest the implication of AGEs in the pathogenesis of diabetes complications such as: retinopathy, neuropathy, chronic renal disease and cardiovascular disease [6,8,9].…”

Section: Introductionmentioning

confidence: 99%

The Assessment of Fluorophores Advanced Glycation End Products-to-Kynurenine Ratio in Healthy and Diabetic Rats and Humans

Olar¹,

Ciobanu²,

Matei³

et al. 2018

Studia UBB Chemia

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In this study, we calculated the ratio of the serum contributions of two highly studied fluorophore products (advanced glycation end productsAGEs and kynurenine -KYN) in the area of nutrition and metabolic diseases including diabetes mellitus (DM), by using a non-invasive, economical and easy-to-perform method. Blood serum spectrofluorimetric analysis was performed both in the case of normoglycemic (n=10) and diabetic rats (n=10), and in the case of non-diabetic (n=14) and type 2 diabetes mellitus (T2DM) patients (n=52). Our results showed a significant increase in the contributions of the two products in diabetic patients and rats compared to the control group. The ratio of the two compounds was positively correlated with serum glucose levels in the case of rats, and with serum triglyceride values in the case of humans. Also, the presence of DM complications in human subjects and the subsequent calculation of ROC curves led to a predictive value of the investigated ratio (AGEs/KYN) for the presence of peripheral diabetic polyneuropathy (PNP). The obtained results suggest a high potential for the investigated ratio to be considered as a new biomarker for the presence of PNP.

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Effect of Non-Enzymatic Glycation on Cystatin: A Spectroscopic Study

Cited by 22 publications

References 35 publications

Vitamin D prevents glycation of proteins: an in vitro study

Vitamin D prevents glycation of proteins: an in vitro study

Purification and Biochemical Characterization of a Cystatin-Like Thiol Proteinase Inhibitor from Cicer arietinum (Chickpea)

The Assessment of Fluorophores Advanced Glycation End Products-to-Kynurenine Ratio in Healthy and Diabetic Rats and Humans

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