Proteomics-Based Identification of Differentially-Expressed Proteins Including Galectin-1 in the Blood Plasma of Type 2 Diabetic Patients

Liu, Xiaojun; Feng, Qi-ping; Chen, Yong; Zuo, Jun; Gupta, Nishith; Chang, Yongsheng; Fang, Fude

doi:10.1021/pr800850a

Cited by 41 publications

(34 citation statements)

References 32 publications

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“…As reported previously by Xiao Junliu et al, galectin-1 was increased 4.8 times in Type 2 diabetic patients compared with normal individuals and a dose-dependent treatment of rat skeletal muscle cells with glucose resulted in an up-regulation of galectin-1 [16]. Similarly, we found that galectin-1 expression is a little higher in Type 1 diabetic mice than in normal mice (Fig.…”

Section: Discussionsupporting

confidence: 89%

“…This immunopharmacological profile of APS may be related to its beneficial effects in diseases with Th1/Th2 cytokine ratio imbalance, such as T1DM. Although APS may improve the metabolism of streptozotocin (STZ)-induced diabetic rats [14], enable insulin-sensitizing and anti-hyperglycemic activity in fat-fed STZ-treated rats [15], and delay onset of T1DM in NOD mice pretreated with APS [16], the mechanisms for improved hyperglycemia associated with APS may be multifaceted and at present remain unclear. Therefore, the purpose of our study was to investigate the therapeutic effects of APS on T1DM and elucidate the immunotherapeutic molecular mechanisms.…”

Section: Introductionmentioning

confidence: 99%

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Increased galectin-1 expression in muscle of Astragalus polysaccharide-treated Type 1 diabetic mice

Zhou

Guo-ming

et al. 2011

J Nat Med

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In order to investigate the immunopharmacological function of Astragalus polysaccharide (APS) in Type 1 diabetes mellitus (T1DM), multiple low-dose streptozotocin-induced diabetic mice and normal mice were administered either APS or saline intraperitoneally once daily. The changes in galectin-1 expression in different organs of the mice were detected by ELISA, Real-time fluorescence quantitative RT-PCR and Western blot. The percentages of apoptotic CD8(+) T cells from spleens of APS-treated diabetic mice were measured by flow cytometry. We found that the expression of galectin-1 was increased in serum of APS-treated diabetic mice compared to the non-treated diabetic mice (*p < 0.05). Increased galectin-1 was mainly expressed in the muscle of APS-treated mice. In vitro, APS up-regulated the expression of galectin-1 in muscle cells in a dose-dependent manner. The percentage of apoptotic CD8(+) T cells in spleens of APS-treated mice was positively correlated with the concentration of APS treatment, and the blocking of galectin-1 in vivo by specific antibody reduced the percentage of apoptotic CD8(+) T cells in APS-treated mice. Our findings indicated that APS could up-regulate the expression of galectin-1 in muscle of T1DM mice, resulting in the apoptosis of CD8(+) T cells. This may be an important mechanism by which APS protects β cells of the pancreatic islets from apoptosis induced by CD8(+) T cells in T1DM in vivo.

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Section: Discussionsupporting

confidence: 89%

Section: Introductionmentioning

confidence: 99%

Increased galectin-1 expression in muscle of Astragalus polysaccharide-treated Type 1 diabetic mice

Zhou

Guo-ming

et al. 2011

J Nat Med

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“…Recently, mass spectroscopic analysis of differentially expressed proteins in the plasma of Type II diabetic patients revealed a 4.8-fold increase in galectin-1 protein (22). Galectin-1 also binds the neuropilin-1 receptor on the surface of endothelial cells leading to the increased phosphorylation of the VEGFR-2 co-receptor, which activates the stress-activated protein kinase-1/c-Jun NH 2 -terminal kinase signaling pathway (11) and could influence angiogenesis in diabetic tissues.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional analysis of the endothelial response to diabetes reveals a role for galectin-3

Darrow

Shohet

Maresh

2011

Physiological Genomics

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Darrow AL, Shohet RV, Maresh JG. Transcriptional analysis of the endothelial response to diabetes reveals a role for galectin-3. Physiol Genomics 43: 1144 -1152, 2011. First published July 26, 2011 doi:10.1152/physiolgenomics.00035.2011.-To characterize the endothelial dysfunction associated with Type II diabetes, we surveyed transcriptional responses in the vascular endothelia of mice receiving a diabetogenic, high-fat diet. Tie2-GFP mice were fed a diet containing 60% fat calories (HFD); controls were littermates fed normal chow. Following 4, 6, and 8 wk, aortic and leg muscle tissues were enzymatically dispersed, and endothelial cells were obtained by fluorescence-activated cell sorting. Relative mRNA abundance in HFD vs. control endothelia was measured with long-oligo microarrays; highly dysregulated genes were confirmed by real-time PCR and protein quantification. HFD mice were hyperglycemic by 2 wk and displayed vascular insulin resistance and decreased glucose tolerance by 5 and 6 wk, respectively. Endothelial transcripts upregulated by HFD included galectin-3 (Lgals3), 5-lipoxygenase-activating protein, and chemokine ligands 8 and 9. Increased LGALS3 protein was detected in muscle endothelium by immunohistology accompanied by elevated LGALS3 in the serum of HFD mice. Our comprehensive analysis of the endothelial transcriptional response in a model of Type II diabetes reveals novel regulation of transcripts with roles in inflammation, insulin sensitivity, oxidative stress, and atherosclerosis. Increased endothelial expression and elevated humoral levels of LGALS3 supports a role for this molecule in the vascular response to diabetes, and its potential as a direct biomarker for the inflammatory state in diabetes. gene expression; microarray; vascular biology; endothelial dysfunction; metabolic syndrome TYPE II DIABETES IS ASSOCIATED with increased atherosclerosis, retinopathy, skin ulceration, and other vascular-related diseases, all of which may involve damaged or dysfunctional endothelium. A major consequence of diabetes is endothelial exposure to elevated glucose and fatty acids, leading to endothelial nitric oxide synthase uncoupling and subsequent generation of reactive oxygen and nitrogen species (46) as well as the formation of advanced glycation end-products (AGEs) (45). Furthermore, hyperinsulinemia and other hormonal changes can alter endothelial signaling pathways (34). These changes may promote inflammation, impair vasoregulation, disrupt hemostasis, and inhibit reverse cholesterol transport (2, 32). By examining the transcriptional changes that occur in both the micro-and macrovascular endothelium of mice exposed to a dietary model of Type II diabetes, we expect to gain further insight into the underlying mechanisms of the endothelial dysfunction characteristic of diabetes and the metabolic syndrome.Transcriptional analysis has been used to examine the responses of cultured endothelium exposed to high glucose and insulin (9, 44). However, an in vitro analysis may only partially reflect the co...

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“…One of these, a-1-antitrypsin, was also identified in the recent diabetes urine proteome analyses as being increased in diabetic patients relative to controls but was not found to be specific to T2D in comparison to T1D (84). Fewer proteins were identified in the plasma proteome study of T2D, which used a 2DGE and MALDI-MS approach; however, the galectin-1 protein found and confirmed by ELISA to be significantly upregulated was also found to be induced by glucose in skeletal muscle cells (88). In summary, these studies demonstrate the usefulness of proteomic analysis of biological fluids for identifying novel candidate biomarkers and molecular mechanisms of pathogenesis in chronic disease.…”

Section: Proteomic Applications In Nutritionmentioning

confidence: 95%

“…This later study both validated a set of markers for distinguishing diabetic patients and identified markers capable of differentiating T2D and T1D, although an acknowledged weakness of this study was the variation in the clinical characteristics of each sample group. Additional research has focused on the salivary (87) and plasma (88) proteomes of T2D patients. Using label-free quantitation and multidimensional LC-MS/MS with significant fractionation, Rao et al (87) identified a notable 487 salivary proteins, of which 65 were differentially expressed in T2D.…”

Section: Proteomic Applications In Nutritionmentioning

confidence: 99%

Proteomics and Systems Biology: Current and Future Applications in the Nutritional Sciences

Moore¹,

Weeks²

2011

Advances in Nutrition

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In the last decade, advances in genomics, proteomics, and metabolomics have yielded large-scale datasets that have driven an interest in global analyses, with the objective of understanding biological systems as a whole. Systems biology integrates computational modeling and experimental biology to predict and characterize the dynamic properties of biological systems, which are viewed as complex signaling networks. Whereas the systems analysis of disease-perturbed networks holds promise for identification of drug targets for therapy, equally the identified critical network nodes may be targeted through nutritional intervention in either a preventative or therapeutic fashion. As such, in the context of the nutritional sciences, it is envisioned that systems analysis of normal and nutrient-perturbed signaling networks in combination with knowledge of underlying genetic polymorphisms will lead to a future in which the health of individuals will be improved through predictive and preventative nutrition. Although high-throughput transcriptomic microarray data were initially most readily available and amenable to systems analysis, recent technological and methodological advances in MS have contributed to a linear increase in proteomic investigations. It is now commonplace for combined proteomic technologies to generate complex, multi-faceted datasets, and these will be the keystone of future systems biology research. This review will define systems biology, outline current proteomic methodologies, highlight successful applications of proteomics in nutrition research, and discuss the challenges for future applications of systems biology approaches in the nutritional sciences.

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Proteomics-Based Identification of Differentially-Expressed Proteins Including Galectin-1 in the Blood Plasma of Type 2 Diabetic Patients

Cited by 41 publications

References 32 publications

Increased galectin-1 expression in muscle of Astragalus polysaccharide-treated Type 1 diabetic mice

Increased galectin-1 expression in muscle of Astragalus polysaccharide-treated Type 1 diabetic mice

Transcriptional analysis of the endothelial response to diabetes reveals a role for galectin-3

Proteomics and Systems Biology: Current and Future Applications in the Nutritional Sciences

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