CRYAB-650 C&gt;G (rs2234702) affects susceptibility to Type 1 diabetes and IAA-positivity in Swedish population

Sun, Chengjun; Sedimbi, Saikiran K.; Ashok, Ayyappa K.; Sanjeevi, Carani B.

doi:10.1016/j.humimm.2012.04.004

Cited by 2 publications

(2 citation statements)

References 388 publications

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“…They found that the CRYAB −650 C>G (rs2234702) polymorphism, which had been reported to be associated with the development of MS in a Dutch population, was also found to confer a susceptibility relationship with the development of T1D in the Swedish cohort (OR = 1.48, P = 0.03). The CRYAB −650C was also associated with the development of IAA-positivity in T1D patients, especially in those carrying T1D high-risk HLA haplotypes (Sun et al 2012 ).…”

Section: Cryab ( Hspb5 ) Snp and Type 1 Diabetesmentioning

confidence: 93%

“…T1D and MS share similarities in disease epidemiology, infl uence from environmental factors, genetic risk factors and pathogenic mechanisms (Handel et al 2009 ). Sun et al investigated the associations of CRYAB variants with risk of T1D in a Swedish population (Sun et al 2012 ). They found that the CRYAB −650 C>G (rs2234702) polymorphism, which had been reported to be associated with the development of MS in a Dutch population, was also found to confer a susceptibility relationship with the development of T1D in the Swedish cohort (OR = 1.48, P = 0.03).…”

Section: Cryab ( Hspb5 ) Snp and Type 1 Diabetesmentioning

confidence: 99%

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Small HSP Variants and Human Diseases

Guo

2015

Heat Shock Proteins

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Small heat shock proteins (sHSPs) are key members of the HSP superfamily that are ubiquitous among all organisms. The amino acid sequences of the sHSPs are not as highly conserved as the larger HSPs but it comprises a characteristic α-crystallin domain (ACD). The mammalian sHSP family, now referred to as the HSPB family, includes 11 members: HSP27/HSPB1, MKBP (myotonic dystrophy protein kinase-binding protein)/HSPB2, HSPB3, alphaA-crystallin / HSPB4, alphaB-crystallin/HSPB5, HSP20/HSPB6, cvHSP (cardiovascular heat shock protein)/HSPB7, HSP22/HSPB8, HSPB9, ODF1 (outer dense fi ber protein)/ HSPB10, and HSPB11. They have been reported to have a wide range of cellular functions, including endowing cells with thermotolerance and acting as molecular chaperones. Because of these functions, sHSPs can participate in a large number of fundamental cellular processes such as controlling protein folding, F-actindependent processes, cytoprotection/anti-apoptosis, differentiation, cell proliferation, and gene expression, and thereby are involved in many pathological diseases, such as neurodegenerative diseases, cancer, and cardiovascular diseases. Genetic mutation or variations of sHSPs genes may change their expression levels and affect protein functions, thus contributing to cell malfunction especially during stress.Here we examined the current reports regarding the mutations or variations of sHSPs genes, and we analyzed their associations with the development, progression, and prognosis of some human diseases. We also addressed the biological functions for the potential causal sHSPs variations and discussed their possible implications in human diseases.

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Section: Cryab ( Hspb5 ) Snp and Type 1 Diabetesmentioning

confidence: 93%

Section: Cryab ( Hspb5 ) Snp and Type 1 Diabetesmentioning

confidence: 99%

Small HSP Variants and Human Diseases

Guo

2015

Heat Shock Proteins

View full text Add to dashboard Cite

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A Systematic Review of Proteomics in Obesity: Unpacking the Molecular Puzzle

Rodriguez-Muñoz,

Motahari-Rad,

Martin-Chaves

et al. 2024

Curr Obes Rep

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Purpose of Review The present study aims to review the existing literature to identify pathophysiological proteins in obesity by conducting a systematic review of proteomics studies. Proteomics may reveal the mechanisms of obesity development and clarify the links between obesity and related diseases, improving our comprehension of obesity and its clinical implications. Recent Findings Most of the molecular events implicated in obesity development remain incomplete. Proteomics stands as a powerful tool for elucidating the intricate interactions among proteins in the context of obesity. This methodology has the potential to identify proteins involved in pathological processes and to evaluate changes in protein abundance during obesity development, contributing to the identification of early disease predisposition, monitoring the effectiveness of interventions and improving disease management overall. Despite many non-targeted proteomic studies exploring obesity, a comprehensive and up-to-date systematic review of the molecular events implicated in obesity development is lacking. The lack of such a review presents a significant challenge for researchers trying to interpret the existing literature. Summary This systematic review was conducted following the PRISMA guidelines and included sixteen human proteomic studies, each of which delineated proteins exhibiting significant alterations in obesity. A total of 41 proteins were reported to be altered in obesity by at least two or more studies. These proteins were involved in metabolic pathways, oxidative stress responses, inflammatory processes, protein folding, coagulation, as well as structure/cytoskeleton. Many of the identified proteomic biomarkers of obesity have also been reported to be dysregulated in obesity-related disease. Among them, seven proteins, which belong to metabolic pathways (aldehyde dehydrogenase and apolipoprotein A1), the chaperone family (albumin, heat shock protein beta 1, protein disulfide-isomerase A3) and oxidative stress and inflammation proteins (catalase and complement C3), could potentially serve as biomarkers for the progression of obesity and the development of comorbidities, contributing to personalized medicine in the field of obesity. Our systematic review in proteomics represents a substantial step forward in unravelling the complexities of protein alterations associated with obesity. It provides valuable insights into the pathophysiological mechanisms underlying obesity, thereby opening avenues for the discovery of potential biomarkers and the development of personalized medicine in obesity

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CRYAB-650 C>G (rs2234702) affects susceptibility to Type 1 diabetes and IAA-positivity in Swedish population

Cited by 2 publications

References 388 publications

Small HSP Variants and Human Diseases

Small HSP Variants and Human Diseases

A Systematic Review of Proteomics in Obesity: Unpacking the Molecular Puzzle

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