A Novel p.G112E Mutation in BFSP2 Associated with Autosomal Dominant Pulverulent Cataract with Sutural Opacities

Liu, Qing; Wang, Kai Jie; Zhu, Si Quan

doi:10.3109/02713683.2014.891749

Cited by 7 publications

(5 citation statements)

References 23 publications

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“…These genes are mainly involved in the formation of the lens. They are classified as crystallin genes (CRYA, CRYB, and CRYG), lens specific connexin genes (Cx43, Cx46, and Cx50), major intrinsic protein gene (MIP) or aquaporine, cytoskeletal structural protein genes, paired-like homeodomain transcription factor 3 (PITX3), avian musculoaponeurotic fibrosarcoma (MAF), heat shock transcription factor 4 (HSF4), beaded filament structural protein 2(BFSP2) and non-muscle myosin heavy chain IIA, NMMHC-IIA (MYH9) [7,9,10] . Besides, Ephrin receptor subfamily (EPHA1, EPHA2), RPGR interacting protein 1 (RPGRIP1) and paired box 6 (PAX6) also play a vital role in pathogenesis of cataract.…”

Section: Introductionmentioning

confidence: 99%

Novel mutations associated with autosomal dominant congenital cataract are identified in Chinese families

Wang

Huang

Sun

et al. 2018

Preprint

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PurposeAs the leading cause of the impairment of vision of children, congenital cataract is considered as a hereditary disease, especially autosomal dominant congenital cataract (ADCC). The purpose of this study is to identify the genetic defect of six Chinese families with ADCC. Subjects and MethodsSix Chinese families with ADCC were recruited in the study. (103 members in total, 96 members alive, 27 patients in total) Genomic DNA samples extracting from probands' peripheral blood cells were captured the mutations using a specific eye disease enrichment panel with next generation sequencing. After initial pathogenicity prediction, sites with specific pathogenicity were screened for further validation. Sanger sequencing was conducted in the other individuals in the families and other 100 normal controls. Mutations definitely related with ADCC will then be analyzed by bioinformatics analysis. The pathogenic effect of the amino acid changes and structural and functional changes of the proteins were finally analyzed by bioinformatics analysis.

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Section: Introductionmentioning

confidence: 99%

Novel mutations associated with autosomal dominant congenital cataract are identified in Chinese families

Wang

Huang

Sun

et al. 2018

Preprint

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“…The fi rst, and by far the strongest, is the phenocopying by mutations in both sHSP and IF proteins (e.g. cardiomyopathy caused by mutations in αB-crystallin ) and desmin; (Goldfarb et al 1998 ); cataract caused by mutations in both αA-crystallin , αB-crystallin (Liu et al 2006c ), vimentin ), BFSP1 Ramachandran et al 2007 ) and BFSP2 Ma et al 2008 ;Zhang et al 2006 ;Liu et al 2014 ); neuropathies caused by mutations in HSP27 ), HSP22 ) and neurofi lament light chain, NFL (Jordanova et al 2003 ;Mersiyanova et al 2000 ). Recent reviews have elaborated on the role for keratins (Toivola et al 2010 ;Pan et al 2013 ) and nuclear lamins (Shimi and Goldman 2014 ) in combatting different stresses.…”

Section: Other Tauopathiesmentioning

confidence: 99%

The Big Book on Small Heat Shock Proteins

Hightower¹,

Tanguay²

2015

Heat Shock Proteins

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Heat Shock Proteins: key mediators of Health and Disease. Heat shock proteins (HSP) are essential molecules conserved through cellular evolution required for cells to survive the stresses encountered in the environment and in the tissues of the developing and aging organism. These proteins play the essential roles in stress of preventing the initiation of programmed cell death and repairing damage to the proteome permitting resumption of normal metabolism. Loss of the HSP is lethal either in the short-term in cases of acute stress or in the long-term when exposure to stress is chronic. Cells appear to walk a fi ne line in terms of HSP expression. If expression falls below a certain level, cells become sensitive to oxidative damage that infl uences aging and protein aggregation disease. If HSP levels rise above the normal range, infl ammatory and oncogenic changes occur. It is becoming clear that HSP are emerging as remarkably versatile mediators of health and disease. The aim of this series of volumes is to examine how HSP regulation and expression become altered in pathological states and how this may be remedied by pharmacological and other interventions.More information about this series at

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“…The fi rst, and by far the strongest, is the phenocopying by mutations in both sHSP and IF proteins (e.g. cardiomyopathy caused by mutations in αB-crystallin (Vicart et al 1998 )) and desmin; (Goldfarb et al 1998 ); cataract caused by mutations in both αA-crystallin , αB-crystallin (Liu et al 2006c ), vimentin (Müller et al 2009 ), BFSP1 Ramachandran et al 2007 ) and BFSP2 (Zhang et al 2004 ;Ma et al 2008 ;Zhang et al 2006 ;Liu et al 2014 ); neuropathies caused by mutations in HSP27 (Evgrafov et al 2004 ), HSP22 ) and neurofi lament light chain, NFL (Jordanova et al 2003 ;Mersiyanova et al 2000 ). Recent reviews have elaborated on the role for keratins (Toivola et al 2010 ;Pan et al 2013 ) and nuclear lamins (Shimi and Goldman 2014 ) in combatting different stresses.…”

Section: Where It All Began -The Identifi Cation Of the Dynamic Duo Omentioning

confidence: 99%

The Dynamic Duo of Small Heat Proteins and IFs Maintain Cell Homeostasis, Resist Cellular Stress and Enable Evolution in Cells and Tissues

Perng

Quinlan

2015

Heat Shock Proteins

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As with many proteins, their initial christening with a name corrals our thinking on their functions and roles. IFs were not named as heat shock proteins, but along with heat shock proteins, they continue to be expressed in response to heat shock. In this review we outline the case for exposing the identity of the "dynamic duo" as small heat shock proteins (sHSPs) and their IF (IF) partners in their battle to assuage stress. Together they maintain the homeostasis of and integrate key cellular processes within cells that allow potential evolutionary opportunity to be seized (Quinlan RA, Ellis RJ, Philos Trans R Soc Lond B Biol Sci 368:20130091, 2013). Both sHSPs and IFs form dynamic polymeric structures -nano-particles and intermediate (nano) fi laments respectively. Both have a wide range of interaction (client) proteins. IFs provide a convenient matrix to host small heat shock proteins and potentiate their role as chaperones, whilst IF function is sHSP-dependent. Together, it is their emerging capacity as integrators of both cell homeostasis and the stress response within and between tissues, however, which is the most exciting. This is because the dynamic duo co-operate on the two central chaperone activities -assisting protein assemblies and dealing with the consequences of protein damage. We propose that the sHSP-IF partnership is key to understanding the stress response, not least because it emphasizes the role of these protein chaperones in assisting the building, regulation and turnover of the IF protein assemblies as well as in diseases caused by their malfunction.

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A Novel p.G112E Mutation in BFSP2 Associated with Autosomal Dominant Pulverulent Cataract with Sutural Opacities

Abstract: We report a novel mutation (p.G112E) in the BFSP2 gene, underscoring the physiological importance of the beaded filament protein and supporting its role in human cataract formation.

Cited by 7 publications

References 23 publications

Novel mutations associated with autosomal dominant congenital cataract are identified in Chinese families

Novel mutations associated with autosomal dominant congenital cataract are identified in Chinese families

The Big Book on Small Heat Shock Proteins

The Dynamic Duo of Small Heat Proteins and IFs Maintain Cell Homeostasis, Resist Cellular Stress and Enable Evolution in Cells and Tissues

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