Serum protein patterns in newly diagnosed type 2 diabetes mellitus—influence of diabetic environment and family history of diabetes

Sundsten, Tea; Östenson, Claes‐Göran; Bergsten, Peter

doi:10.1002/dmrr.789

Cited by 27 publications

(33 citation statements)

References 44 publications

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“…The differences in plasma proteins were interpreted as manifestations of the disease state, rather than being causative. This conclusion was consistent with the results from another study where the aim was to determine the relative importance of the diabetic environment versus genetic background for the development of β-cell failure (Sundsten, et al 2008b). Serum protein profiles of NGT and newly diagnosed T2DM individuals were compared and persons with differences both in β-cell function (estimated by HOMA-β) and family history of diabetes (FHD) were included.…”

Section: Many Individual Serum Proteins Have Been Shown To Vary Betwesupporting

confidence: 83%

“…For instance increased levels of ApoCIII found in T2DM patients (Sundsten, et al 2008a) have also been measured in serum from individuals with T1DM (Juntti-Berggren, et al 2004) and are also considered a cardiovascular risk factor (Gervaise, et al 2000). Transthyretin on the other hand was decreased in serum from individuals with T2DM in both studies Sundsten et al 2008b). The finding aligned well with results reporting lowering of TTR in streptozotocin-treated rats (Kim, et al 2006).…”

Section: Many Individual Serum Proteins Have Been Shown To Vary Betwementioning

confidence: 83%

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Proteomics in diabetes research

Sundsten

Ortsäter

2009

Molecular and Cellular Endocrinology

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SummaryBoth type 1 and type 2 diabetes mellitus are heterogeneous diseases with alterations in many genes and their products. Not all transcriptional alterations lead to protein changes, which makes it very important to, in conjunction with mRNA expression studies, also address changes in cellular protein levels. Various proteomic techniques are available for measuring many protein changes simultaneously. Many proteomic studies have been performed in the context diabetes research, with the aims of both describing the healthy tissue and to unravel the complex pathophysiology behind the disease. In addition, effects on proteins induced by different treatments have also been investigated using proteomic approaches. In this paper the field of diabetes proteomics today will be reviewed. Findings from proteomic studies investigating pancreatic islets and β-cells as well as serum, fat, skeletal muscle and liver are described.

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Section: Many Individual Serum Proteins Have Been Shown To Vary Betwesupporting

confidence: 83%

Section: Many Individual Serum Proteins Have Been Shown To Vary Betwementioning

confidence: 83%

Proteomics in diabetes research

Sundsten

Ortsäter

2009

Molecular and Cellular Endocrinology

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“…Novel mathematical treatments of MALDI data have been conceived (Montazery-Kordy et al, 2008;Alexandrov et al, 2009;Liu, 2009). There remains an on-going documentation of blood by MALDI parent ion patterns in response to a variety of physiological states such as disease, drug response, the image or proximity of romantic partners or the use of performance enhancing drugs (Tammen et al, 2002;Guerrier, Lomas, & Boschetti, 2005;Schwegler et al, 2005;de Seny et al, 2005;Orvisky et al, 2006;Ragazzi et al, 2006;Zheng et al, 2006a;Lin et al, 2006b;de Noo et al, 2006b;Au et al, 2007;Cui et al, 2007Cui et al, , 2008bHui et al, 2007;Lim et al, 2007;Taguchi et al, 2007;Tiss et al, 2007;Yildiz et al, 2007;Das et al, 2008;Datta, 2008;Jacot et al, 2008;Kojima et al, 2008;Meuleman et al, 2008Meuleman et al, , 2009Ransohoff et al, 2008;Sundsten, Ostenson, & Bergsten, 2008a;Wei et al, 2008;Zinkin et al, 2008;Han et al, 2008a,b;Liu et al, 2008a;Wang et al, 2008aWang et al, ,c, 2008dCallesen et al, 2008bCallesen et al, , 2009Sundsten et al, 2008b;Albitar et al, 2009;Caron et al, 2009;…”

Section: Maldi Pattern Analysismentioning

confidence: 99%

Mass spectrometry of peptides and proteins from human blood

Zhu

Bowden

Zhang

et al. 2010

Mass Spectrometry Reviews

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It is difficult to convey the accelerating rate and growing importance of mass spectrometry applications to human blood proteins and peptides. Mass spectrometry can rapidly detect and identify the ionizable peptides from the proteins in a simple mixture and reveal many of their post-translational modifications. However, blood is a complex mixture that may contain many proteins first expressed in cells and tissues. The complete analysis of blood proteins is a daunting task that will rely on a wide range of disciplines from physics, chemistry, biochemistry, genetics, electromagnetic instrumentation, mathematics and computation. Therefore the comprehensive discovery and analysis of blood proteins will rank among the great technical challenges and require the cumulative sum of many of mankind's scientific achievements together. A variety of methods have been used to fractionate, analyze and identify proteins from blood, each yielding a small piece of the whole and throwing the great size of the task into sharp relief. The approaches attempted to date clearly indicate that enumerating the proteins and peptides of blood can be accomplished. There is no doubt that the mass spectrometry of blood will be crucial to the discovery and analysis of proteins, enzyme activities, and post-translational processes that underlay the mechanisms of disease. At present both discovery and quantification of proteins from blood are commonly reaching sensitivities of ∼1 ng/mL.

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“…The proteomic approaches for comprehensive characterization of plasma revealed numerous plasma markers of diabetes mellitus [26]: proteomic approach on human serum in the context of diabetes and an approach where fractionated serum samples for analysis of low abundant serum proteins [27]. Sundsten et al [28] investigated the relative importance of the diabetic environment versus genetic background for the development of β cell failure.…”

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis of Plasma Proteins in Diabetic Rats by 2D Electrophoresis and MALDI-TOF-MS

Karthik

Ilavenil

Kaleeswaran

et al. 2012

Appl Biochem Biotechnol

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Despite tremendous advances in our understanding of the molecular basis of diabetes mellitus, substantial gaps still remain in our understanding of disease pathogenesis and in the development of effective strategies for early diagnosis and treatment. The proteomic approach has offered many opportunities and challenges in identifying new marker proteins and therapeutic targets, i.e., using 2D-polyacrylamide gel electrophoresis and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry. The differential protein expressions were analyzed in alloxan-induced diabetic rats treated with Cynodon dactylon leaf extract. The plant extract was administered for 15 days that resulted in a significant increase in plasma insulin and C-peptide levels. We have also identified four differentially expressed proteins from rat plasma. These four diabetes-associated proteins were broadly classified into three groups as per their function: (1) lipid metabolism-associated protein (Apo A-IV), (2) antioxidant activity-related proteins [preprohaptoglobin and heat shock proteins B8 (HspB8)], and (3) muscle function-related protein (TPM3). Apo A-IV, HspB8, and preprohaptoglobin may play a key role in the recovery of diabetes mellitus and also prevent the diabetes-associated complications such as prevention of oxidative stress due to free radical and free hemoglobin. These results show the value of proteomic approach in identifying the potential markers that may eventually serve as diagnostic markers or therapeutic targets.

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Serum protein patterns in newly diagnosed type 2 diabetes mellitus—influence of diabetic environment and family history of diabetes

Abstract: Using the SELDI-technique, serum protein profiles of NGT and T2DM persons with differences in beta-cell function and FHD were compared. The diabetic environment had a major influence on most of these proteins, while FHD was an important factor for apoC3 and albumin.

Cited by 27 publications

References 44 publications

Proteomics in diabetes research

Proteomics in diabetes research

Mass spectrometry of peptides and proteins from human blood

Proteomic Analysis of Plasma Proteins in Diabetic Rats by 2D Electrophoresis and MALDI-TOF-MS

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