A Biophysical Comparison of Human Serum Albumin to be Glycated In Vivo and In Vitro

Sattarahmady, N.; Moosavi-Movahedi, Ali A.; Habibi-Rezaei, Mehran

doi:10.2478/v10011-010-0026-7

Cited by 12 publications

(3 citation statements)

References 25 publications

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“…3B) was accompanied with the reduction in solvent exposed hydrophobic patches of these proteins (Fig. 3A) [41]. Our results are in agreement with previous studies suggesting an inverse correlation between the surface tension and surface hydrophobicity of protein [19].…”

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confidence: 93%

Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients

Yousefi

Javadi

Amirghofran

et al. 2016

International Journal of Biological Macromolecules

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Total soluble lens proteins (TSPs) and α-crystallin (α-Cry) were individually subjected to the long-term glycation in the presence of d-glucose. The glycated and non-glycated protein counterparts were incubated under different stress conditions and compared according to their structure, stability and aggregation propensity by various spectroscopic techniques and gel mobility shift analyses. Extensive glycation of the lens proteins was accompanied with structural alteration, reduction in their surface hydrophobicity and increment of their surface tension. Our results suggest that glycation causes lens crystallins to partially resist against structural alteration and aggregation/fibrillation under both thermal and thermochemical systems. The conformational stability of lens crystallins was increased upon glycation, showing the reason behind resistance of glycated proteins against stress-induced structural alteration and aggregation. Due to the resistance of glycated lens crystallins against aggregation, the role of this modification in development of senile cataract can be explained with the associated damaging consequences highlighted in this article.

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Section: ►Fig3 To Be Inserted Here◄supporting

confidence: 93%

Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients

Yousefi

Javadi

Amirghofran

et al. 2016

International Journal of Biological Macromolecules

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“…Different physiological and pathological conditions have long been known to be associated with alteration in glycosylation (11)(12)(13), which may affect the biochemical and functional characteristics of glyco proteins. The glycosylation of proteins in cancer is the most attractive area of research, as it frequently leads to the discovery of new glycosylation patterns of the examined proteins (11,14).…”

Section: Discussionmentioning

confidence: 99%

N-Glycosylation Pattern of Human Placental Insulin-Like Growth Factor and Insulin Receptors in Well-Controlled Pregestational Diabetes Mellitus

Robajac¹,

Masnikosa²,

Filimonović³

et al. 2012

Journal of Medical Biochemistry

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Summary: Diabetes mellitus is a complex disease that leads to alterations in the glycosylation of proteins. Insulin-like growth factor and insulin receptors are involved in the regulation of fetal and placental growth and development. In this work the N-glycans of these receptors, originating from placentas obtained from pregnancies complicated by pregestational insulin dependent diabetes mellitus, were studied. Dia betic mothers were under regular insulin therapy. Solubilised membrane samples from healthy and diabetic placentas were analysed using lectin-affinity chromatography. N-glycans bound to insulin-like growth factor and insulin receptors were studied in terms of their interaction with eleven aga rose--immobilised lectins: wheat germ agglutinin, succinyla ted wheat germ agglutinin, Ricinus communis agglutinin I, Sambucus nigra agglutinin, Erythrina cristagalli lectin, Ulex europaeus agglutinin, Lens culinaris agglutinin, Canavalia en siformis lectin, Phaseolus vulgaris erythro-and leukoagglutinin and Maackia amurensis agglutinin. A very similar type of N-glycans and content of the terminal saccharide residues were found in both groups of placentas. The results of this work suggest that the tight glycemic control may prevent alterations in the glycosylation of insulin-like growth factor and insulin receptors, thus maintaining physiological homeostasis during pregnancy and fetal growth.Keywords: diabetes mellitus, insulin-like growth factor receptors, insulin receptor, N-glycosylation, placenta Kratak sadr`aj: Dijabetes melitus je kompleksno oboljenje koje uzrokuje promene u na~inu glikozilovanja prote ina. Receptori za insulin i insulinu sli~ne faktore rasta u~es -tvuju u regulaciji rasta i razvitka fetusa i placente. U ovom radu ispitivani su N-glikani vezani kovalentnom vezom za pome nute receptore. Receptori za insulin i insulinu sli~ne faktore rasta dobijeni su iz placenti majki sa pregestacijskim insu lin-zavisnim dijabetesom. Dijabeti~ne majke bile su na re dov noj terapiji insulinom. Uzorci }elijskih membrana, izolovani i solubilizovani iz placenti zdravih majki i majki sa dijabetesom, analizirani su primenom lektinske afinitetne hromatografije. Ispitivana je interakcija N-glikana vezanih za receptore sa jedanaest razli~itih lektina, imobilisanih na agaroznom gelu: lektin iz p{eni~nih klica, sukcinilovani lektin iz p{eni~nih klica, Ricinus communis lektin I, lektin iz kore zove, lektin iz koralnog drveta, lektin iz Ulex europaeus-a, lektin iz so~iva, konkanavalin A, dva lektina iz pasulja i lektin iz Maackia amurensis-a. Rezultati ovog rada pokazali su da receptori za insulin i insulinu sli~ne faktore rasta poreklom iz humane placente zdravih majki i onih sa pregestacijskim dijabetesom imaju veoma sli~an tip N-glikana kao i sastav terminalnih ostataka saharida, {to ukazuje na to da se dobrom kontrolom glikemije kod trudnica sa dijabetesom mogu spre~iti promene u na~inu gliko zilova nja ovih receptora, ~ime bi se pomoglo odr`avanju fiziolo{ke homeostaze za vreme rasta fetusa.

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“…A FIGURA 1 mostra simplificadamente a formação da base de Schiff e do produto de Amadori.Sua formação é, em maior parte, um processo endógeno, porém essas moléculas também podem ser introduzidas no organismo de maneira exógena, através da alimentação e do fumo. Alimentos ricos em lipídeos e carboidratos são a principal fonte exógena de AGEs e métodos de preparo utilizando altas temperaturas e baixa umidade, como fritar, grelhar ou assar, podem potencializar a formação dessas substâncias(29).Dentre as proteínas presentes no organismo passíveis a glicação, pode-se citar a albumina (HSA -do inglês human serum albumin), proteína sérica de baixo peso molecular (67 kDa) mais abundante (aproximadamente 40 mg/ml) Durante o processo de glicação a molécula sofre alterações ou perda na sua estrutura helicoidal e diminuição do número de Į-hélices (33)…”

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Utilização da espectroscopia de fluorescência para mensuramento de moléculas autoflurescentes em indivíduos diabéticos

Gomes¹

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Diabetes Mellitus (DM) comprises a complex metabolic syndrome, caused by reduced or absent secretion of insulin by pancreatic beta cells, leading to hyperglycemia. Hyperglycemia promotes glycation of proteins and, consequently, the appearance of advanced glycation end products (AGEs). Currently, diabetic patients are monitored by determining levels of glucose and glycated hemoglobin (HbA1c). The complications caused by hyperglycemia may be divided into micro and macrovascular complications, represented by retinopathy, nephropathy, neuropathy and cardiovascular disease. Albumin (HSA) is the most abundant serum protein in the human body and is subject to glycation. The Protoporphyrin IX (PpIX) is the precursor molecule of heme synthesis, structural component of hemoglobin. The in vitro and animals studies have indicated that hyperglycemia promotes a decrease in its concentration in erythrocytes. The fluorescence spectroscopy is a technique widely used in biomedical field. The autofluorescence corresponds to the intrinsic fluorescence present in some molecules, this being associated with the same structure. The aim of this study was to use fluorescence spectroscopy to measure levels of erythrocyte PpIX autofluorescence and AGE-HSA in diabetic and healthy subjects and compare them with levels of blood glucose and HbA1c. This study was conducted with 151 subjects (58 controls and 93 diabetics). Epidemiological data of patients and controls were obtained from medical records. For control subjects, blood glucose levels were obtained from medical records and levels of Hb1Ac obtained by using commercial kits. The determination of the PpIX autofluorescence was performed with excitation at 405 nm and emission at 632 nm. Determination of AGE-HSA was performed with excitation at 370 nm and emission at 455 nm. Approximately 50% of diabetic had micro and macrovascular lesions resulting from hyperglycemia. There were no significant differences in the PpIX emission intensity values between groups (P = 0.89). In the analysis of AGE-HSA was observed significant differences in the values of emission intensity between the two groups, and this value was 1.45-fold greater for the group of diabetic (P <0.0001). Patients with diabetic complications had fluorescence emission intensity of 1.19-fold higher than individuals without disease complications (P = 0.01), even with no significant differences in HbA1c values between the two groups. We conclude that fluorescence spectroscopy was an effective technique in the identification of the PpIX autofluorescence and AGE-HSA. The PpIX was not an effective biomarker for the monitoring of diabetes. The determination of AGE-HSA autofluorecência was efficient for the discrimination between groups and monitoring disease progression, may be more effective than HbA1c dosage. The fluorescence spectroscopy is a simple, fast and low cost for the monitoring of diabetic patients.

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A Biophysical Comparison of Human Serum Albumin to be Glycated In Vivo and In Vitro

Cited by 12 publications

References 25 publications

Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients

Assessment of structure, stability and aggregation of soluble lens proteins and alpha-crystallin upon non-enzymatic glycation: The pathomechanisms underlying cataract development in diabetic patients

N-Glycosylation Pattern of Human Placental Insulin-Like Growth Factor and Insulin Receptors in Well-Controlled Pregestational Diabetes Mellitus

Utilização da espectroscopia de fluorescência para mensuramento de moléculas autoflurescentes em indivíduos diabéticos

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