Purpose: : In our previous studies, we have demonstrated that alpha-crystallins can negatively regulate stress-induced apoptosis through suppression of the ERK-mediated pathway and activation of the AKT signaling pathway. In the present study, we present evidence to show that alpha-crystallins can regulate the ATR-p53 pathway to prevent UVA-induced apoptosis. Methods: : UVA was used to irradiate human lens epithelial cells stably expressing vector, alphaA, and alphaB. Western blot analysis was used for detection of ATR, CHK1/2 and p53 activation. Reporter gene activity assay was used to explore the transactivity of p53. Hoechst staining was used for apoptosis assay. Results: : Human lens epithelial cells expressing either alphaA- or alphaB-crystallin are substantially resistant to UVA-induced apoptosis. UVA-induces activation of ATR and CHK1/2 kinases to activate p53 in vector-transfected cells. However, in alphaA- or alphaB-crystallin-transfected cells, activation of ATR, CHK1/2 kinases and p53 ...
Human alpha-crystallins were separated from fetal, young, senile nondiabetic and diabetic lenses. The effects of aging and diabetes mellitus were studied by fluorescence measurements, including emission maximum, quantum yield and polarization, using both intrinsic probes (tryptophan and non-tryptophan) and extrinsic probes [4-(N-iodoacetoxy)N-methylamino-7-nitrobenz-2-oxa-1,3-diazole (IANBD) and 6-(p-toluidinyl)naphthalene-2-sulfonate (TNS)]. Results indicate that diabetic effects (glycation and aggregation) give fluorescence change to a far greater extent than that of aging. This was demonstrated by a large decrease in tryptophan quantum yield and an increase in non-tryptophan quantum yield, and also by a decrease in polarization of non-tryptophan. The sulfhydryl (SH)-specific probe IANBD shows a blue-shift in emission maximum, a decrease in intensity and an increase in polarization. The hydrophobic probe TNS shows a decrease in both intensity and polarization. These results suggest that tryptophan
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The chaperone-like protein alpha-crystallin is a approximately 35 subunit hetero-oligomer consisting of alphaA and alphaB subunits in a 3:1 molar ratio and has the function of maintaining eye lens transparency. We studied the thermal denaturation of alpha-crystallin by differential scanning calorimetry (DSC), circular dichroism (CD), and dynamic light scattering (DLS) as a function of pH. Our results show that between pH 7 and 10 the protein undergoes a reversible thermal transition. However, the thermodynamic parameters obtained by DSC are inconsistent with the complete denaturation of an oligomeric protein of the size of alpha-crystallin. Accordingly, the CD data suggest the presence of extensive residual secondary structure above the transition temperature. Within the pH range from 4 to 7 the increased aggregation propensity around the isoelectric point (pI approximately 6) precludes observation of a thermal transition. As pH decreases below 4 the protein undergoes a substantial unfolding. ...
Results. Effect of [alpha]-crystallin on restriction enzyme digestion. To determine whether the partially purified [alpha]-crystallin had inhibitory effects on restriction digestion of DNA, we assayed several commonly used restriction enzymes for activity in the presence of [alpha]-crystallin. The commonly used restriction enzymes, Bam HI, Hind III, Nde I, Pst I and Sst I all remained active in the presence of [alpha]-crystallin. For this experiment, a 5 fold excess of each enzyme (5 units) was incubated for 1 hour with 1 µg of plasmid DNA using manufacturers supplied buffer. Each reaction also contained 1 µl of the purified [alpha]-crystallin (10 mg/ml), final concentration, 1 mg/ml. Each selected enzyme digested the plasmid to completion indicating that [alpha]-crystallin had no major detrimental effects on restriction enzyme digestion (data not shown).. To assay the ability of [alpha]-crystallin to protect restriction enzymes from heat inactivation, we chose the enzyme Nde I. Unlike the ...
Ample evidence suggests that oxidative stress and other external stressors contribute to retinal and retinal pigment epithelium (RPE) pathology, as implicated in diseases like age-related macular degeneration. Therefore the understanding of cellular protection against these insults is of therapeutic importance. We adapted two approaches for studying the mechanisms of macular and retinal degeneration. In one, the contribution and significance of these pathologic processes was investigated by use of cultured human and mouse RPE. In the in vivo counterpart studies, we assessed the importance of alpha-crystallins in the retina (and RPE) in models using knockout mice and cobalt chloride injections. In addition to alpha-crystallins, we looked at other oxidative stress protectants of the cell and examined the redox regulation and antioxidant functions mediated by hepatocyte growth factor (HGF). These studies have greatly contributed to the elucidation of the pathways involved in retinal dysfunction and ...
A method for expressing proteins as a fusion chimera with a domain of p26 or alpha crystallin type proteins to improve the protein stability and solubility when over expressed in bacteria such as E. coli is provided. Genes of interest are cloned into the multiple cloning site of the Vector System just downstream of the p26 or alpha crystallin type protein and a thrombin cleavage site. Protein expression is driven by a strong bacterial promoter (TAC). The expression is induced by the addition of 1 mM IPTG that overcomes the lac repression (lac Iq). The soluble recombinant protein is purified using a fusion tag.
Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.
Crystallins are water-soluble proteins that compose about ninety% in the protein inside the lens.[13] The three main crystallin sorts present in the human eye are α-, β-, and γ-crystallins. Crystallins have a tendency to variety soluble, high-molecular pounds aggregates that pack tightly in lens fibers, Therefore raising the index of refraction of the lens while protecting its transparency. β and γ crystallins are found mostly during the lens, while subunits of α -crystallin happen to be isolated from other areas of the eye and the human body ...
Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity).
Ed to contribute to its chaperone-like activity , while the N-terminal domains contain phosphorylation sites that are the targets of various protein kinases .
Alpha-crystallin B chain is a protein that in humans is encoded by the CRYAB gene. It is part of the small heat shock protein family and functions as molecular chaperone that primarily binds misfolded proteins to prevent protein aggregation, as well as inhibit apoptosis and contribute to intracellular architecture. Post-translational modifications decrease the ability to chaperone. Defects in this gene/protein have been associated with cancer and neurodegenerative diseases such as Alzheimers disease and Parkinsons disease. Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and ...
... , Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
... , Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
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View mouse Hspb11 Chr4:107253593-107279938 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
Complete information for HSPB1P2 gene (Pseudogene), Heat Shock Protein Family B (Small) Member 1 Pseudogene 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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In Leuconostoc oenos, different stresses such as heat, ethanol, and acid shocks dramatically induce the expression of an 18-kDa small heat shock protein called Lo 18. The corresponding gene (hsp18) was cloned from a genomic library of L. oenos constructed in Escherichia coli. A 2.3-kb DNA fragment carrying the hsp18 gene was sequenced. The hsp18 gene encodes a polypeptide of 148 amino acids with a calculated molecular mass of 16,938 Da. The Lo18 protein has a significant identity with small heat shock proteins of the alpha-crystallin family. The transcriptional start site was determined by primer extension. This experiment allowed us to identify the promoter region exhibiting high similarity to consensus promoter sequences of gram-positive bacteria, as well as E. coli. Northern blot analysis showed that hsp18 consists of a unique transcription unit of 0.6 kb. Moreover, hsp18 expression seemed to be controlled at the transcriptional level. This small heat shock protein was found to be ...
A quantitative analysis of cell division and cell elongation was carried out during lens morphogenesis in the rat. At 13 days of development elongating cells in the posterior part of the lens vesicle (presumptive fibre cells) have a lower mitotic activity than cells in the anterior vesicle. By 14 days these elongating cells do not divide. Thus at 14 days of development the lens can be separated into two compartments; a proliferation compartment in the anterior lens and an elongation compartment in the posterior lens.. The three main groups of lens-specific proteins, α-,β- and γ-crystallins, were localized by immunofiuorescence. Alpha-crystallin is the first crystallin to be detected and is localized in some lens pit cells at 12 days of development. By 14 days all lens cells contain α-crystallin. Beta- and β-crystallins are detected later at 12½ days and are localized in some cells situated primarily in the posterior part of the lens vesicle. At later stages of development these crystallins ...
Helianthus annuus hsp17.6 G1 protein: a small heat-shock protein from sunflower; amino acid sequence in first source; GenBank Z95153
Complete information for HSPA2 gene (Protein Coding), Heat Shock Protein Family A (Hsp70) Member 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Chen X, Lin S, Liu Q, Huang J, Zhang W, Lin J, Wang Y, Ke Y, He H. Expression and interaction of small heat shock proteins (sHsps) in rice in response to heat stress. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 2014, 1844 (4): 818-828. ...
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Hsp27, a small heat-shock protein, has important roles in many cellular processes, including cytoskeleton dynamics, cell differentiation, and apoptosis. Its expression in normal epidermis correlates with differentiation; however, little is known about the regulatory mechanisms involved. In this study, we report that Hsp27 undergoes upregulation, phosphorylation, and redistribution to the cytoskeleton during the late phase of epidermal keratinocyte differentiation. Our results also show that the expression of the dual leucine zipper-bearing kinase (DLK), an upstream activator of the MAP kinase pathways, is sufficient by itself to induce Hsp27 phosphorylation, cell periphery localization, and redistribution to the insoluble protein fraction (cytoskeleton) in poorly differentiated keratinocytes. This redistribution correlates with the insolubilization of cornified envelope-associated proteins such as involucrin. Interestingly, the effects of DLK on Hsp27 were blocked by PD98059, a selective ...
α-Crystallin, a member of small heat shock protein (sHsp) family, is comprised of αA and αB subunits and acts as a molecular chaperone by interacting with unfolding proteins to prevent their aggregation. The αA-crystallin homopolymer consists of 30-40 subunits that are undergoing dynamic exchange. α-Crystallin and αA-crystallin are poorer chaperones in the presence of the crowding agent, dextran. Using fluorescence resonance energy transfer, it is shown that the αAcrystallin subunit exchange rate strongly increased with temperature. Binding of reduced ovotransferrin to αA-crystallin markedly decreases the rate of subunit exchange, as does the presence of dextran. In addition, in the presence of dextran the effect of reduced ovotransferrin on decreasing the rate of subunit exchange of αA-crystallin is stronger than in the absence of dextran. Under the conditions of molecular crowding, the αA-crystallin subunit exchange rate is not temperature-dependent. The exchange rate of αA-crystallin
Under changes in conditions as diverse as temperature, oxidation or pH, proteins in an organism may undergo harmful denaturation. Small Heat Shock proteins act as "paramedics of the cell": during such events they quicky intervene by binding nascently unfolding proteins, leading them to refolding or denaturation pathways. Small heat shock proteins are ubiquitous in all kingdoms of life, but especially effective in plants: after all, plants cannot escape from harsh environmental conditions!. Collaborating with Benesch (University of Oxford) and Vierling (UMass) groups, we have contributed to shedding light into the mode of action of small Heat Shock Proteins in wheat and pea.. We describe a mechanism whereby dimers of these proteins are responsible for capturing their substrate, before assemblying into larger complexes. With our own integrative modelling methods using distance restraints and collision cross-section measurements, we demonstrate that small heat shock protein dimers assemble into ...
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ATGen operates in the Commercial Physical Research sector. ATGen is a Korea-based company principally engaged in developing and manufacturing reagent used for experimentation . The Companys product portfolio consists of recombination proteins including binding immunoglobulin protein, carboxy terminus of HSP70 interacting protein, BCL2-associated athanogene 2; monoclonal antibodies including 14-3-3 beta antibody, A crystallin A antibody , alpha-crystallin B and NK Vue Kit used for physical examination and diagnosis. The Company distributes its products within domestic market and to overseas markets.
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Heat shock proteins (HSPs) are ubiquitous in living organisms. HSPs are an essential component for cell growth and survival; the main function of HSPs is controlling the folding and unfolding process of proteins. According to molecular function and mass, HSPs are categorized into six different families: HSP20 (small HSPS), HSP40 (J-proteins), HSP60, HSP70, HSP90, and HSP100. In this paper, improved methods for HSP prediction are proposed—the split amino acid composition (SAAC), the dipeptide composition (DC), the conjoint triad feature (CTF), and the pseudoaverage chemical shift (PseACS) were selected to predict the HSPs with a support vector machine (SVM). In order to overcome the imbalance data classification problems, the syntactic minority oversampling technique (SMOTE) was used to balance the dataset. The overall accuracy was 99.72% with a balanced dataset in the jackknife test by using the optimized combination feature SAAC+DC+CTF+PseACS, which was 4.81% higher than the
Dr. Mason Posner has students use molecular biology techniques to understand how eye lens proteins adapt to changes in environmental temperature.. We are currently investigating the evolution and biological role of lens proteins called crystallins. These proteins are responsible for making the lens transparent and refracting light so that focused images fall on the retina. Amazingly, one family of crystallins, the alpha crystallins, also protect other proteins from the harmful effects of aging that can lead to lens cataracts, one of the leading causes of blindness in humans. Alpha crystallins are also involved in the original development of the lens in vertebrate embryos, and they have been linked to many diseases of the nervous system, heart, skeletal muscle, and are now known to be involved in many cancers.. Most research into alpha crystallins is done with mammals. However, by studying how this protein has evolved in a number of fish species that live at different environmental temperatures, ...
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Purpose: : A previous microarray study from our laboratory demonstrated that in lens epithelial cells treated with quercetin (10 µM), 65% of genes that showed significant increased expression (p≤0.01) were regulated by hypoxia inducible factor-1 (HIF-1). We have, therefore, investigated the effect of quercetin on the HIF-1 signalling pathway in human lens epithelial cells. Methods: : FHL-124 cells were grown to 90% confluency and exposed to quercetin (10 or 30 µM). Protein and mRNA levels were analyzed by Western blot and qRT-PCR respectively. Immunocytochemistry experiments were carried out for visualisation of HIF-1. VEGF was measured in cell medium using ELISA. Results: : Quercetin (30 µM) induced an increase in HIF-1 protein levels after 4 and 24 hr, with a greater than 50-fold increase compared to untreated cells at 4 hr. At 10 µM quercetin, increases were seen after 24 hr. Visualisation of HIF-1 within the cell showed that quercetin caused its translocation to the nucleus and this ...
Gene target information for Dnajb11 - DnaJ heat shock protein family (Hsp40) member B11 (house mouse). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
article{c39ed0c6-71b3-44bd-ae7d-1c63648fa85e, abstract = {,p,The small heat shock protein (sHsp) chaperones are crucial for cell survival and can prevent aggregation of client proteins that partially unfold under destabilizing conditions. Most investigations on the chaperone activity of sHsps are based on a limited set of thermosensitive model substrate client proteins since the endogenous targets are often not known. There is a high diversity among sHsps with a single conserved β-sandwich fold domain defining the family, the α-crystallin domain, whereas the N-terminal and C-terminal regions are highly variable in length and sequence among various sHsps and conserved only within orthologues. The endogenous targets are probably also varying among various sHsps, cellular compartments, cell type and organism. Here we have investigated Hsp21, a non-metazoan sHsp expressed in the chloroplasts in green plants which experience huge environmental fluctuations not least in temperature. We describe how ...
Human Lens Epithelial Cells (HLEpiC) from Creative Bioarray are isolated from the human lens. HLEpiC are cryopreserved at primary culture and delivered frozen. Each vial contains >5 x 10^5 cells in 1 ml volume. HLEpiC are characterized by immunofluorescent method with antibodies to cytokeratin-18, cytokeratin-19 and fibronectin. HLEpiC are negative for HIV-1, HBV, HCV, mycoplasma, bacteria, yeast and fungi. HLEpiC are guaranteed to further culture in the conditions provided by Creative Bioarray ...
The eleven students involved learned basic experimental design (with positive and negative controls), troubleshooting, a wide variety of laboratory techniques, and data collection, analysis and presentations skills. In addition, students learned to read and analyze scientific work from other labs since they are given scientific articles to read beginning on their first day in the lab. This project is in collaboration with Ivor Benjamin M.D., Ph.D. at the University of Utah, which allowed these students the unique opportunity of discussing their research with a larger audience once a month. In addition to intellectual enrichment, students learned to function as a team, with those more experienced (graduate students Kelsey Langston and Whitney Hayes) mentoring those who are new in the lab. As students progressed in their understanding of the project and mastery of basic laboratory skills, they become involved in planning our weekly group meeting, preparing figures for presentations/publications, ...
Ultrasonic and cryogenic instrumentation for the removal of unwanted tissue material from an animal, such as a human, and more particularly, adapted for the removal of cataracts, in surgical operations. The ultrasonic and cryogenic instrumentation include hand-held instruments with the cryogenic instrumentation adapted to first freeze the cataract lens and after the cataract lens has unfrozen the ultrasonic instrumentation is adapted by a vibrating tool to reduce the volume of the cataract and thereafter, through the simultaneous introduction of a fluid and creating a flow, the cataract mass exits through the incision around the vibrating tool until all of the unwanted tissue forming the cataract lens is removed.
Distal hereditary motor neuronopathies (dHMNs) are a clinically and genetically heterogeneous group of disorders in which motor neurons selectively undergo age-dependant degeneration. Mutations in the small heat-shock protein HSPB1 (HSP27) are responsible for one form of dHMN. In this study, we have analysed the effect of expressing a form of mutant HSPB1 in primary neuronal cells in culture. Mutant (P182L) but not wild-type HSPB1 led to the formation of insoluble intracellular aggregates and to the sequestration in the cytoplasm of selective cellular components, including neurofilament middle chain subunit (NF-M) and p150 dynactin. These findings suggest a possible pathogenic mechanism for HSPB1 whereby the mutation may lead to preferential motor neuron loss by disrupting selective components essential for axonal structure and transport.
TY - JOUR. T1 - Rapidly progressive amyotrophic lateral sclerosis is associated with microglial reactivity and small heat shock protein expression in reactive astrocytes. AU - Gorter, R. P.. AU - Stephenson, J.. AU - Nutma, E.. AU - Anink, J.. AU - de Jonge, J. C.. AU - Baron, W.. AU - Jahreiss, M. -C.. AU - Belien, J. A. M.. AU - van Noort, J. M.. AU - Mijnsbergen, C.. AU - Aronica, E.. AU - Amor, S.. N1 - This article is protected by copyright. All rights reserved.. PY - 2019/8. Y1 - 2019/8. N2 - AIMS: Amyotrophic lateral sclerosis (ALS) is a chronic neurodegenerative disease characterised by progressive loss of motor neurons, muscle weakness, spasticity, paralysis and death usually within 2-5 years of onset. Neuroinflammation is a hallmark of ALS pathology characterized by activation of glial cells, which respond by upregulating small heat shock proteins (HSPBs), but the exact underlying pathological mechanisms are still largely unknown. Here, we investigated the association between ALS ...
Small heat shock protein HspB8: its distribution in Alzheimers disease brains s inhibition of amyloid-beta protein aggregation and cerebrovascular d-beta toxicity ...
Current models derived from in vitro studies propose that sHsps prevent irreversible substrate aggregation by binding heat-denatured substrates, and then present substrate to other cellular components for ATP-dependent refolding (Waters et al., 1996; Ehrnsperger et al., 1997;Lee et al., 1997; Veinger et al., 1998). Our data extend this model for sHsp chaperone activity in several important ways. First, we determined that the chaperones required for high levels of refolding of Hsp18.1-bound Luc were Hsp/Hsc70 plus DnaJ homologs. The addition of Hsp90 and Hop gave minimal or no further enhancement of refolding. Despite the eukaryotic origin of Hsp18.1, the highest Luc refolding rates were observed when Hsp18.1-bound Luc was reactivated in the presence of the prokaryotic DnaK system. These findings imply that the mechanism of sHsp action in conjunction with Hsp70 systems is universal among eukaryotes and prokaryotes, and suggest that sHsps may not physically interact with the Hsp70 systems. Also, ...
Any of a group of proteins in living cells that assist newly synthesized or denatured proteins to fold into their functional three-dimensional structures. The chaperones bind to the protein and prevent improper interactions within the polypeptide chain, so that it assumes the correct folded orientation. This process may require energy in the form of ATP. Other functions include assisting the translocation of proteins across the membranes of cell organelles and binding denatured proteins under stress conditions or in degenerative disease. There are several unrelated families of chaperones, including five classes of heat-shock proteins - HSP25 (small heat-shock proteins), HSP60, HSP70, HSP90, and HSP100 - chaperonins, calnexin, and calreticulin. ...
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Heat-stress induced alterations in localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for ?B-crystallin and hsp ...
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