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Impact of in vitro non-enzymatic glycation on biophysical and biochemical regimes of human serum albumin: relevance in diabetes associated complications

机译：体外非酶促糖基对人血清白蛋白生物物理和生化制度的影响：糖尿病相关并发症的相关性

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摘要

Early glycation involves attachment of glucose on epsilon-NH2 of lysine residues. Human serum albumin (HSA), a lysine rich protein, is highly prone to non-enzymatic glycation. In this study, the effect of different concentrations of glucose on HSA through early glycation was assessed by various physicochemical techniques. An early glycation product Amadori HSA was estimated by colorimetric method, nitro blue tetrazolium (NBT) and thiobarbituric acid assay (TBA). The conformational changes were confirmed by UV-visible spectroscopy, tryptophan fluorescence quenching, circular dichroism (CD), and sodium dodecyl sulphate poly acrylamide gel electrophoresis (SDS-PAGE). Biochemical alterations in AmadoriHSA were analyzed by NaBH4 reduction, increased carbonyl content and decrease in free lysine, arginine and sulfhydryl groups. Most studies have reported the structural changes in protein due to AGEs or Amadori protein at a particular glucose concentration; to the best of our knowledge, no reports have been published comparing the physicochemical changes in HSA due to early glycation within a range of glucose concentrations. In the present study, the investigations confirmed the structural and biochemical alterations in Amadori-HSA which is directly proportional to glucose concentration. This might interfere with the normal function of HSA and can contribute to the progression of diabetes and its associated complications. Amadori modified HSA might be used as a biomarker for early detection of diabetes and be beneficial in preventing the diabetic complications at early stages of diabetes. In this context, this study provides additional information about biochemical and biophysical changes occurring in Amadori-HSA within the glucose range upon early glycation.
机译：早期的糖化涉及葡萄糖在赖氨酸残基的ePsilon-NH 2上附着。人血清白蛋白（HSA），富含赖氨酸富含蛋白质，高度容易发生非酶促糖钙化。在该研究中，通过各种物理化学技术评估了通过早期糖化的不同浓度葡萄糖对HSA的影响。通过比色法，硝基蓝四唑（NBT）和硫​​氨基脲酸测定（TBA）估计了早期的糖糖产物Amadori HSA。通过UV可见光谱，色氨酸荧光猝灭，圆形二色性（CD）和十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）确认了构象变化。通过NaBH4还原，增加羰基含量和游离赖氨酸，精氨酸和巯基的降低分析Amadorihsa的生化改变。大多数研究报告了特定葡萄糖浓度的年龄或Amadori蛋白导致的蛋白质的结构变化;据我们所知，由于一系列葡萄糖浓度内的早期糖化，未公布报告的比较HSA的物理化学变化。在本研究中，调查证实了Amadori-HSA中的结构和生化改变，其与葡萄糖浓度成正比成比例。这可能会干扰HSA的正常功能，可以有助于糖尿病的进展及其相关的并发症。 Amadori改性的HSA可能用作早期检测糖尿病的生物标志物，并有利于预防糖尿病早期阶段的糖尿病并发症。在这种情况下，该研究提供了有关在早期糖化的葡萄糖范围内的Amadori-HSA中发生的生化和生物物理变化的额外信息。

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  • 来源
    《RSC Advances》 |2015年第78期|共10页
  • 作者

    Neelofar; Ahmad Jamal; Alam Khursheed;

  • 作者单位

    Aligarh Muslim Univ Fac Med Rajiv Gandhi Ctr Diabet &

    Endocrinol Aligarh 202002 Uttar Pradesh India;

    Aligarh Muslim Univ Fac Med Rajiv Gandhi Ctr Diabet &

    Endocrinol Aligarh 202002 Uttar Pradesh India;

    Aligarh Muslim Univ Fac Med Dept Biochem Aligarh 202002 Uttar Pradesh India;

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  • 正文语种 eng
  • 中图分类 化学;
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