Diabetes Affects α-Crystallin Chaperone Function

Cherian, M.; Abraham, E.C.

doi:10.1006/bbrc.1995.1954

Cited by 39 publications

(29 citation statements)

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“…Consistent with this is the independent observation that the heat shock protein HSP27 interacts with the insulin-like growth factor receptor 1 and its signal transducer, the serine/threonine kinase protein Akt, which together modulate adipocyte metabolism (52,53). Diabetes alters the metabolism of the chaperone crystallin ␣, increasing its glycation status (43,44). In the lens of the eye, this biochemical change contributes to cataract formation; its effect in adipose tissue, if any, remains to be determined.…”

Section: Resultsmentioning

confidence: 82%

“…The heat shock proteins serve as chaperones, controlling protein folding in the endoplasmic reticulum and their subsequent intracellular trafficking (42). There is a growing body of literature linking chaperone-like molecules to adipogenesis, obesity, and diabetes (43)(44)(45)(46). For example, adipogenesis in 3T3-L1 cells is accompanied by increased expression of the chaperone-related immunophilin, FK-binding protein 51 (47).…”

Section: Resultsmentioning

confidence: 99%

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Proteomic Analysis of Primary Cultures of Human Adipose-derived Stem Cells

DeLany

Floyd

Zvonic

et al. 2005

Molecular & Cellular Proteomics

132

128

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Adipogenesis plays a critical role in energy metabolism and is a contributing factor to the obesity epidemic. This study examined the proteome of primary cultures of human adipose-derived adult stem (ADAS) cells as an in vitro model of adipogenesis. Protein lysates obtained from four individual donors were compared before and after adipocyte differentiation by two-dimensional gel electrophoresis and tandem mass spectroscopy. Over 170 individual protein features in the undifferentiated adipose-derived adult stem cells were identified. Following adipogenesis, over 40 proteins were up-regulated by >2-fold, whereas 13 showed a >3-fold reduction. The majority of the modulated proteins belonged to the following functional categories: cytoskeleton, metabolic, redox, protein degradation, and heat shock protein/chaperones. Additional immunoblot analysis documented the induction of four individual heat shock proteins and confirmed the presence of the heat shock protein 27 phosphoserine 82 isoform, as predicted by the proteomic analysis, as well as the crystallin ␣ phosphorylated isoforms. These findings suggest that the heat shock protein family proteome warrants further investigation with respect to the etiology of obesity and type 2 diabetes. Molecular & Cellular Proteomics 4:731-740, 2005.Obesity is a health problem of epidemic proportions. It is estimated that in 2000 over 60% of adults are overweight (BMI 1 Ͼ 25) and that 30% are obese (BMI Ͼ 30); this compares to levels of 46 and 14%, respectively, in 1980. Obesity and increased adiposity are associated clinically with the onset of insulin resistance, dysfunctional glucose sensing and utilization, hypertension, and hypertriglyceridemia, all contributing to the pathologic sequelae of type 2 diabetes. Paradoxically type 2 diabetes also occurs in patients with inherited or acquired forms of lipodystrophy or loss of adipose tissue depots (1, 2). Lipodystrophy occurs through defects in genes associated with triglyceride metabolism or as a consequence of antiretroviral therapy in human immunodeficiency viruspositive patients (1, 2). Animal models confirm these clinical observations; multiple strains of transgenic mice with a lipodystrophic phenotype exhibit type 2 diabetes (3-5). Diabetes in these animals responds not to insulin therapy but to transplantation of subcutaneous adipose tissue or to leptin treatment (3-5). These clinical and experimental observations have led to the hypothesis that a failure in adipocyte differentiation is a critical etiologic factor leading to type 2 diabetes (6 -8). Danforth (6) and others postulate that in obese individuals adipose tissue depots have already committed all of their stem cell reserves to the adipocyte lineage and have lost their capacity to create new adipocytic cells (6 -8). In the face of excess energy balance, both obese and lipodystrophic individuals deposit triglycerides in ectopic sites, such as muscle and liver, thereby contributing to the metabolic dysfunction associated with type 2 diabetes (increased hepatic glucon...

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Section: Resultsmentioning

confidence: 82%

Section: Resultsmentioning

confidence: 99%

Proteomic Analysis of Primary Cultures of Human Adipose-derived Stem Cells

DeLany

Floyd

Zvonic

et al. 2005

Molecular & Cellular Proteomics

132

128

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“…HSPs are molecular chaperones that are classified into families according to their molecular weight (Ellis 1999, Hwang et al 2009. A growing body of literature has linked chaperone-like molecules to adipogenesis, obesity and diabetes (Cherian & Abraham 1995, Kurucz et al 2002, Young et al 2004. HSP27 is a chaperone of the small HSP group, which has been implicated in multiple functions such as inflammation, cytoprotective stress proteins, inhibition of apoptosis, cell development, cell differentiation and signal transduction (Arrigo 2007, Salari et al 2013.…”

Section: Oxidative Stressmentioning

confidence: 99%

2D-DIGE to identify proteins associated with gestational diabetes in omental adipose tissue

Oliva

Barker

Rice

et al. 2013

Journal of Endocrinology

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Gestational diabetes mellitus (GDM) is a significant risk factor for the type 2 diabetes epidemic in many populations. Maternal adipose tissue plays a central role in the pathophysiology of GDM. Thus, the aim of this study was to determine the effect of GDM on the proteome of adipose tissue. Omental adipose tissue was obtained at the time of term Caesarean section from women with normal glucose tolerance (NGT) or GDM. 2D-difference gel electrophoresis (DIGE), followed by mass spectrometry, was used to identify protein spots (nZ6 patients per group). Western blotting was used for confirmation of six of the spot differences (nZ6 patients per group). We found 14 proteins that were differentially expressed between NGT and GDM adipose tissue (R1.4-fold, P!0.05). GDM was associated with an up-regulation of four proteins: collagen alpha-2(VI) chain (CO6A2 (COL6A2)), fibrinogen beta chain (FIBB (FGB)), lumican (LUM) and S100A9. On the other hand, a total of ten proteins were found to be down-regulated in adipose tissue from GDM women. These were alpha-1-antitrypsin (AIAT (SERPINA1)), annexin A5 (ANXA5), fatty acid-binding protein, adipocyte (FABP4), glutathione S-transferase P (GSTP (GSTP1)), heat-shock protein beta-1 (HSP27 (HSPB1)), lactate dehydrogenase B chain (LDHB), perilipin-1 (PLIN1), peroxiredoxin-6 (PRX6 (PRDX6)), selenium-binding protein 1 (SBP1) and vinculin (VINC (VCL)). In conclusion, proteomic analysis of omental fat reveals differential expression of several proteins in GDM patients and NGT pregnant women. This study revealed differences in expression of proteins that are involved in inflammation, lipid and glucose metabolism and oxidative stress and added further evidence to support the role of visceral adiposity in the pathogenesis of GDM.

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“…Preferential glycation has been shown to affect alpha-crystallins in diabetic rat and human lens [66,67], whereas acetylation has been found to regulate chaperone function of Hsp90 [68]. The increased glycation correlates with an increase in the size of the aggregates formed by alpha-crystallins [67], leading to decreased chaperone activity of the protein [69,70]. It has also been shown that increased expression of alpha-crystallins in spontaneously diabetic OLETF rats is associated with increased phosphorylation on serine residues 45 and 59 [40].…”

Section: Regulation Of Functionmentioning

confidence: 99%

Impact of diabetes on alpha-crystallins and other heat shock proteins in the eye

Heise

Fort

2011

j ocul biol dis inform

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Diabetes and its related complications represent a major growing health concern and economic burden worldwide. Ocular manifestations of diabetes include cataractogenesis and retinopathy, the latter being the leading cause of blindness in the working-age population. Despite numerous studies and recent progress, the exact pathophysiology of the disease remains to be fully elucidated and development of new and improved therapeutic strategies for this chronic condition are greatly needed. Heat shock proteins (Hsps) are highly conserved families of proteins, which are generally regarded as protective molecules that play a wide variety of roles and can be expressed in response to different types of cellular stresses. In recent years, numerous studies have reported their implication in various ocular diseases including diabetic retinopathy. The present review focuses on the potential implication of Hsps in ocular diabetic complications and discusses their specific mechanisms of regulation with respect to their expression, functions and alteration during diabetes. The review will conclude by examining the potential of Hsps as therapeutic agents or targets for the treatment of diabetic retinopathy.

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Diabetes Affects α-Crystallin Chaperone Function

Cited by 39 publications

References 0 publications

Proteomic Analysis of Primary Cultures of Human Adipose-derived Stem Cells

Proteomic Analysis of Primary Cultures of Human Adipose-derived Stem Cells

2D-DIGE to identify proteins associated with gestational diabetes in omental adipose tissue

Impact of diabetes on alpha-crystallins and other heat shock proteins in the eye

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