Proteomic Analysis of Glycated Proteins from Streptozotocin-Induced Diabetic Rat Kidney

Chougale, Ashok D.; Bhat, Shweta; Bhujbal, Swapnil Vilas; Zambare, Mandar R; Puntambekar, Shraddha; Somani, Rahul; Boppana, Ramanamurthy; Giri, Ashok P.; Kulkarni, Mahesh J.

doi:10.1007/s12033-011-9409-3

Cited by 14 publications

(18 citation statements)

References 46 publications

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“…The experiment was repeated independently three times. modified by various glycation modifications, common to our previous study (12). Hence, these results provided additional evidence that the protease resistance of these proteins is caused by a variety of AGE modifications.…”

Section: Fig 4 Validation Of Lc-mssupporting

confidence: 84%

“…Proteins of extracellular matrix, kidney, as well as proteins from circulation, get AGE modified and trapped in the kidney (12). Both intracellular and extracellular AGEs have been observed in the diabetic kidney.…”

mentioning

confidence: 99%

“…Together AGE modification and decreased proteasomal function may be responsible for the accumulation of protease resistant proteins (PRPs) in the diabetic kidney. In our previous study, we have reported the presence of AGE modified proteins in the kidney of the streptozotocin (STZ) induced diabetic rat (12). The current work is inspired by a DARTS (drug affinity responsive target stability) approach, wherein the drug targets are relatively less susceptible to protease action on drug binding (16).…”

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confidence: 99%

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Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney

Bansode

Chougale

Joshi

et al. 2013

Molecular & Cellular Proteomics

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Glycation induced protein aggregation has been implicated in the development of diabetic complications and neurodegenerative diseases. These aggregates are known to be resistant to proteolytic digestion. Here we report the identification of protease resistant proteins from the streptozotocin induced diabetic rat kidney, which included enzymes in glucose metabolism and stress response proteins. These protease resistant proteins were characterized to be advanced glycation end products modified and ubiquitinated by immunological and mass spectrometry analysis. Further, diabetic rat kidney exhibited significantly impaired proteasomal activity. The functional analysis of identified physiologically important enzymes showed that their activity was reduced in diabetic condition. Loss of functional activity of these proteins was compensated by enhanced gene expression. Aggregation prone regions were predicted by in silico analysis and compared with advanced glycation end products modification sites. These findings suggested that the accumulation of protein aggregates is an inevitable consequence of impaired proteasomal activity and protease resistance due to advanced glycation end products modification. Molecular & Cellular

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Section: Fig 4 Validation Of Lc-mssupporting

confidence: 84%

mentioning

confidence: 99%

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confidence: 99%

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Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney

Bansode

Chougale

Joshi

et al. 2013

Molecular & Cellular Proteomics

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“…abundant plasma protein (22) and preferentially gets glycated (23). Amadori-modified albumin is reported to be independently associated with nephropathy in type 1 diabetic patients (24), and in our previous study, AGE-modified serum albumin was detected in the kidney of STZ-induced diabetic rats (25). Glycated albumin levels are reported to be elevated significantly in type 2 diabetic patients with coronary artery disease (26).…”

Section: Elevated Human Serum Albumin In Cics Of Plasma From Prediabementioning

confidence: 77%

Proteomic Insight Reveals Elevated Levels of Albumin in Circulating Immune Complexes in Diabetic Plasma

Bhat

Jagadeeshaprasad

Patil

et al. 2016

Molecular & Cellular Proteomics

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A Hyperglycemic condition in diabetes promotes formation of advanced glycation end products, which are known to elicit immune response and form complexes with immunoglobulins called circulating immune complexes. To investigate the involvement of advanced glycation end product (AGE)-modified proteins in the elicitation of an immune response, circulating immune complexes were isolated and proteins associated were identified and characterized. Label-free-based mass spectrometric analysis of circulating immune complexes in clinical plasma of prediabetic, newly diagnosed diabetes, and diabetic microalbuminurea revealed elevated levels of serum albumin in the circulating immune complexes, which were also observed to be AGE modified. Further, to examine the role of glycation, circulating immune complexes were analyzed in the streptozotocin-induced diabetic mice treated with or without aminoguanidine, a prototype glycation inhibitor. Mass spectrometric analysis of circulating immune complexes showed elevated levels of serum albumin in plasma from diabetic mice over that of control animals. Aminoguanidine-treated diabetic mice displayed decreased AGE modification of plasma albumin, accompanied by a reduced level of albumin in the circulating immune complexes. In addition, elevated levels of proinflammatory cytokines such as IL-1b, IL-2, and TNF-alpha were observed in diabetes, which were reduced with aminoguanidine treatment, suggesting the involvement of glycation in the immune response.

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“…Very recently, iTRAQ based proteomic studies from IGIB, New Delhi have shown that downregulation of apolipoproteins and albumin might be responsible for impaired reverse cholesterol transport in stable CAD [76]. Interesting findings in Type 2 diabetes have emerged from proteomic studies carried out at NCL, Pune in human plasma and drug induced animal models [77–85]. One of the novel initiatives undertaken by this group is to study advanced glycation end products (AGE) in a diabetic animal model using MALDI–TOF–MS based proteomics [82].…”

Section: Reviewmentioning

confidence: 99%

Proteomics in India: the clinical aspect

Mukherjee

Bandyopadhyay

2016

Clin Proteom

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Proteomics has emerged as a highly promising bioanalytical technique in various aspects of applied biological research. In Indian academia, proteomics research has grown remarkably over the last decade. It is being extensively used for both basic as well as translation research in the areas of infectious and immune disorders, reproductive disorders, cardiovascular diseases, diabetes, eye disorders, human cancers and hematological disorders. Recently, some seminal works on clinical proteomics have been reported from several laboratories across India. This review aims to shed light on the increasing use of proteomics in India in a variety of biological conditions. It also highlights that India has the expertise and infrastructure needed for pursuing proteomics research in the country and to participate in global initiatives. Research in clinical proteomics is gradually picking up pace in India and its future seems very bright.

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Proteomic Analysis of Glycated Proteins from Streptozotocin-Induced Diabetic Rat Kidney

Cited by 14 publications

References 46 publications

Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney

Proteomic Analysis of Protease Resistant Proteins in the Diabetic Rat Kidney

Proteomic Insight Reveals Elevated Levels of Albumin in Circulating Immune Complexes in Diabetic Plasma

Proteomics in India: the clinical aspect

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