Log in

Relevant bibliographies by topics / Α-crystallin / Journal articles

Journal articles on the topic 'Α-crystallin'

To see the other types of publications on this topic, follow the link: Α-crystallin.

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Α-crystallin.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Selivanova, Olga M., and Oxana V. Galzitskaya. "Structural and Functional Peculiarities of α-Crystallin." Biology 9, no. 4 (April 23, 2020): 85. http://dx.doi.org/10.3390/biology9040085.

Full text

Abstract:

α-Crystallin is the major protein of the eye lens and a member of the family of small heat-shock proteins. Its concentration in the human eye lens is extremely high (about 450 mg/mL). Three-dimensional structure of native α-crystallin is unknown. First of all, this is the result of the highly heterogeneous nature of α-crystallin, which hampers obtaining it in a crystalline form. The modeling based on the electron microscopy (EM) analysis of α-crystallin preparations shows that the main population of the α-crystallin polydisperse complex is represented by oligomeric particles of rounded, slightly ellipsoidal shape with the diameter of about 13.5 nm. These complexes have molecular mass of about 700 kDa. In our opinion, the heterogeneity of the α-crystallin complex makes it impossible to obtain a reliable 3D model. In the literature, there is evidence of an enhanced chaperone function of α-crystallin during its dissociation into smaller components. This may indirectly indicate that the formation of heterogeneous complexes is probably necessary to preserve α-crystallin in a state inactive before stressful conditions. Then, not only the heterogeneity of the α-crystallin complex is an evolutionary adaptation that protects α-crystallin from crystallization but also the enhancement of the function of α-crystallin during its dissociation is also an evolutionary acquisition. An analysis of the literature on the study of α-crystallin in vitro led us to the assumption that, of the two α-crystallin isoforms (αA- and αB-crystallins), it is αA-crystallin that plays the role of a special chaperone for αB-crystallin. In addition, our data on X-ray diffraction analysis of α-crystallin at the sample concentration of about 170–190 mg/mL allowed us to assume that, at a high concentration, the eye lens α-crystallin can be in a gel-like stage. Finally, we conclude that, since all the accumulated data on structural-functional studies of α-crystallin were carried out under conditions far from native, they cannot adequately reflect the features of the functioning of α-crystallin in vivo.

APA, Harvard, Vancouver, ISO, and other styles

2

Evans, Paul, Christine Slingsby, and B. A. Wallace. "Association of partially folded lens βB2-crystallins with the α-crystallin molecular chaperone." Biochemical Journal 409, no. 3 (January 15, 2008): 691–99. http://dx.doi.org/10.1042/bj20070993.

Full text

Abstract:

Age-related cataract is a result of crystallins, the predominant lens proteins, forming light-scattering aggregates. In the low protein turnover environment of the eye lens, the crystallins are susceptible to modifications that can reduce stability, increasing the probability of unfolding and aggregation events occurring. It is hypothesized that the α-crystallin molecular chaperone system recognizes and binds these proteins before they can form the light-scattering centres that result in cataract, thus maintaining the long-term transparency of the lens. In the present study, we investigated the unfolding and aggregation of (wild-type) human and calf βB2-crystallins and the formation of a complex between α-crystallin and βB2-crystallins under destabilizing conditions. Human and calf βB2-crystallin unfold through a structurally similar pathway, but the increased stability of the C-terminal domain of human βB2-crystallin relative to calf βB2-crystallin results in the increased population of a partially folded intermediate during unfolding. This intermediate is aggregation-prone and prevents constructive refolding of human βB2-crystallin, while calf βB2-crystallin can refold with high efficiency. α-Crystallin can effectively chaperone both human and calf βB2-crystallins from thermal aggregation, although chaperone-bound βB2-crystallins are unable to refold once returned to native conditions. Ordered secondary structure is seen to increase in α-crystallin with elevated temperatures up to 60 °C; structure is rapidly lost at temperatures of 70 °C and above. Our experimental results combined with previously reported observations of α-crystallin quaternary structure have led us to propose a structural model of how activated α-crystallin chaperones unfolded βB2-crystallin.

APA, Harvard, Vancouver, ISO, and other styles

3

DERHAM, Barry K., and John J. HARDING. "Effects of modifications of α-crystallin on its chaperone and other properties." Biochemical Journal 364, no. 3 (June 15, 2002): 711–17. http://dx.doi.org/10.1042/bj20011512.

Full text

Abstract:

The role of α-crystallin, a small heat-shock protein and chaperone, may explain how the lens stays transparent for so long. α-Crystallin prevents the aggregation of other lens crystallins and proteins that have become unfolded by ‘trapping’ the protein in a high-molecular-mass complex. However, during aging, the chaperone function of α-crystallin becomes compromised, allowing the formation of light-scattering aggregates that can proceed to form cataracts. Within the central part of the lens there is no turnover of damaged protein, and therefore post-translational modifications of α-crystallin accumulate that can reduce chaperone function; this is compounded in cataract lenses. Extensive in vitro glycation, carbamylation and oxidation all decrease chaperone ability. In the present study, we report the effect of the modifiers malondialdehyde, acetaldehyde and methylglyoxal, all of which are pertinent to cataract. Also modification by aspirin, which is known to delay cataract and other diseases, has been investigated. Recently, two point mutations of arginine residues were shown to cause congenital cataract. 1,2-Cyclohexanedione modifies arginine residues, and the extent of modification needed for a change in chaperone function was investigated. Only methylglyoxal and extensive modification by 1,2-cyclohexanedione caused a decrease in chaperone function. This highlights the robust nature of α-crystallin.

APA, Harvard, Vancouver, ISO, and other styles

4

Sathish, Hasige A., Hanane A. Koteiche, and Hassane S. Mchaourab. "Binding of Destabilized βB2-Crystallin Mutants to α-Crystallin." Journal of Biological Chemistry 279, no. 16 (February 3, 2004): 16425–32. http://dx.doi.org/10.1074/jbc.m313402200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Singh, Kamalendra, D. Zewge, B. Groth-Vasselli, and P. N. Farnsworth. "A comparison of structural relationships among α-crystallin, human Hsp27, γ-crystallins and βB2-crystallin." International Journal of Biological Macromolecules 19, no. 4 (December 1996): 227–33. http://dx.doi.org/10.1016/s0141-8130(96)01131-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

LINDNER, Robyn A., Teresa M. TREWEEK, and John A. CARVER. "The molecular chaperone α-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of α-lactalbumin." Biochemical Journal 354, no. 1 (February 8, 2001): 79–87. http://dx.doi.org/10.1042/bj3540079.

Full text

Abstract:

In vivo, α-crystallin and other small heat-shock proteins (sHsps) act as molecular chaperones to prevent the precipitation of ‘substrate’ proteins under stress conditions through the formation of a soluble sHsp–substrate complex. Using a range of different salt conditions, the rate and extent of precipitation of reduced α-lactalbumin have been altered. The interaction of α-crystallin with reduced α-lactalbumin under these various salt conditions was then studied using a range of spectroscopic techniques. Under conditions of low salt, α-lactalbumin aggregates but does not precipitate. α-Crystallin is able to prevent this aggregation, initially by stabilization of a monomeric molten-globule species of α-lactalbumin. It is proposed that this stabilization occurs through weak transient interactions between α-crystallin and α-lactalbumin. Eventually a stable, soluble high-molecular-mass complex is formed between the two proteins. Thus it appears that a tendency for α-lactalbumin to aggregate (but not necessarily precipitate) is the essential requirement for α-crystallin–α-lactalbumin interaction. In other words, α-crystallin interacts with a non-aggregated form of the substrate to prevent aggregation. The rate of precipitation of α-lactalbumin is increased significantly in the presence of Na2SO4 compared with NaCl. However, in the former case, α-crystallin is unable to prevent this aggregation and precipitation except in the presence of a large excess of α-crystallin, i.e. at mass ratios more than 10 times greater than in the presence of NaCl. It is concluded that a kinetic competition exists between aggregation and interaction of unfolding proteins with α-crystallin.

APA, Harvard, Vancouver, ISO, and other styles

7

Crabbe, M. J., and D. Goode. "α-Crystallin: chaperoning and aggregation." Biochemical Journal 297, no. 3 (February 1, 1994): 653–54. http://dx.doi.org/10.1042/bj2970653.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Merck, K. B., W. A. de Haard-Hoekman, H. Bloemendal, and W. W. de Jong. "Protein engineering of α-crystallin." Experimental Eye Research 55 (September 1992): 165. http://dx.doi.org/10.1016/0014-4835(92)90772-k.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Nagaraj, Ram H., Rooban B. Nahomi, Niklaus H. Mueller, Cibin T. Raghavan, David A. Ammar, and J. Mark Petrash. "Therapeutic potential of α-crystallin." Biochimica et Biophysica Acta (BBA) - General Subjects 1860, no. 1 (January 2016): 252–57. http://dx.doi.org/10.1016/j.bbagen.2015.03.012.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Narberhaus, Franz. "α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network." Microbiology and Molecular Biology Reviews 66, no. 1 (March 2002): 64–93. http://dx.doi.org/10.1128/mmbr.66.1.64-93.2002.

Full text

Abstract:

SUMMARY α-Crystallins were originally recognized as proteins contributing to the transparency of the mammalian eye lens. Subsequently, they have been found in many, but not all, members of the Archaea, Bacteria, and Eucarya. Most members of the diverse α-crystallin family have four common structural and functional features: (i) a small monomeric molecular mass between 12 and 43 kDa; (ii) the formation of large oligomeric complexes; (iii) the presence of a moderately conserved central region, the so-called α-crystallin domain; and (iv) molecular chaperone activity. Since α-crystallins are induced by a temperature upshift in many organisms, they are often referred to as small heat shock proteins (sHsps) or, more accurately, α-Hsps. α-Crystallins are integrated into a highly flexible and synergistic multichaperone network evolved to secure protein quality control in the cell. Their chaperone activity is limited to the binding of unfolding intermediates in order to protect them from irreversible aggregation. Productive release and refolding of captured proteins into the native state requires close cooperation with other cellular chaperones. In addition, α-Hsps seem to play an important role in membrane stabilization. The review compiles information on the abundance, sequence conservation, regulation, structure, and function of α-Hsps with an emphasis on the microbial members of this chaperone family.

APA, Harvard, Vancouver, ISO, and other styles

11

Malik, Ajamaluddin, Hajar Ahmed Almaharfi, Javed Masood Khan, Malik Hisamuddin, Salman Freeh Alamery, Samina Hyder Haq, and Mohammad Z. Ahmed. "Protection of ζ-crystallin by α-crystallin under thermal stress." International Journal of Biological Macromolecules 167 (January 2021): 289–98. http://dx.doi.org/10.1016/j.ijbiomac.2020.11.183.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

GOENKA, Shradha, Bakthisaran RAMAN, Tangirala RAMAKRISHNA, and Ch Mohan RAO. "Unfolding and refolding of a quinone oxidoreductase: α-crystallin, a molecular chaperone, assists its reactivation." Biochemical Journal 359, no. 3 (October 25, 2001): 547–56. http://dx.doi.org/10.1042/bj3590547.

Full text

Abstract:

α-Crystallin, a member of the small heat-shock protein family and present in vertebrate eye lens, is known to prevent the aggregation of other proteins under conditions of stress. However, its role in the reactivation of enzymes from their non-native inactive states has not been clearly demonstrated. We have studied the effect of α-crystallin on the refolding of ∊-crystallin, a quinone oxidoreductase, from its different urea-denatured states. Co-refolding ∊-crystallin from its denatured state in 2.5M urea with either calf eye lens α-crystallin or recombinant human αB-crystallin could significantly enhance its reactivation yield. αB-crystallin was found to be more efficient than αA-crystallin in chaperoning the refolding of ∊-crystallin. In order to understand the nature of the denatured state(s) of ∊-crystallin that can interact with α-crystallin, we have investigated the unfolding pathway of ∊-crystallin. We find that it unfolds through three distinct intermediates: an altered tetramer, a partially unfolded dimer, which is competent to fold back to its active state, and a partially unfolded monomer. The partially unfolded monomer is inactive, exhibits highly exposed hydrophobic surfaces and has significant secondary structural elements with little or no tertiary structure. This intermediate does not refold into the active state without assistance. α-Crystallin provides the required assistance and improves the reactivation yield several-fold.

APA, Harvard, Vancouver, ISO, and other styles

13

Kumar, P. Anil, M. Satish Kumar, and G. Bhanuprakash Reddy. "Effect of glycation on α-crystallin structure and chaperone-like function." Biochemical Journal 408, no. 2 (November 14, 2007): 251–58. http://dx.doi.org/10.1042/bj20070989.

Full text

Abstract:

The chaperone-like activity of α-crystallin is considered to play an important role in the maintenance of the transparency of the eye lens. However, in the case of aging and in diabetes, the chaperone function of α-crystallin is compromized, resulting in cataract formation. Several post-translational modifications, including non-enzymatic glycation, have been shown to affect the chaperone function of α-crystallin in aging and in diabetes. A variety of agents have been identified as the predominant sources for the formation of AGEs (advanced glycation end-products) in various tissues, including the lens. Nevertheless, glycation of α-crystallin with various sugars has resulted in divergent results. In the present in vitro study, we have investigated the effect of glucose, fructose, G6P (glucose 6-phosphate) and MGO (methylglyoxal), which represent the major classes of glycating agents, on the structure and chaperone function of α-crystallin. Modification of α-crystallin with all four agents resulted in the formation of glycated protein, increased AGE fluorescence, protein cross-linking and HMM (high-molecular-mass) aggregation. Interestingly, these glycation-related profiles were found to vary with different glycating agents. For instance, CML [Nϵ-(carboxymethyl)lysine] was the predominant AGE formed upon glycation of α-crystallin with these agents. Although fructose and MGO caused significant conformational changes, there were no significant structural perturbations with glucose and G6P. With the exception of MGO modification, glycation with other sugars resulted in decreased chaperone activity in aggregation assays. However, modification with all four sugars led to the loss of chaperone activity as assessed using an enzyme inactivation assay. Glycation-induced loss of α-crystallin chaperone activity was associated with decreased hydrophobicity. Furthermore, α-crystallin isolated from glycated TSP (total lens soluble protein) had also increased AGE fluorescence, CML formation and diminished chaperone activity. These results indicate the susceptibility of α-crystallin to non-enzymatic glycation by various sugars and their derivatives, whose levels are elevated in diabetes. We also describes the effects of glycation on the structure and chaperone-like activity of α-crystallin.

APA, Harvard, Vancouver, ISO, and other styles

14

DERHAM, K. Barry, and J. John HARDING. "Effect of aging on the chaperone-like function of human α-crystallin assessed by three methods." Biochemical Journal 328, no. 3 (December 15, 1997): 763–68. http://dx.doi.org/10.1042/bj3280763.

Full text

Abstract:

α-Crystallin can function as a molecular chaperone by preventing unwanted interactions. This paper presents the effects of aging and cataract on the chaperone-like properties of α-crystallin from soluble fractions from the cortex and nucleus of human lenses by using three assays: enzyme inactivation and two turbidity experiments. The three methods complemented each other. There was no decrease with age of chaperone-like function of cortical α-low and α-high crystallin. Nuclear α-low crystallin showed a decrease, whereas α-high crystallin showed no age-related change but its protective effect was diminished. Results from the nucleus of 40-year-old cataractous lenses seemed similar to those for clear lenses of equivalent age, whereas 80-year-old cataractous lenses showed decreased chaperone-like behaviour.

APA, Harvard, Vancouver, ISO, and other styles

15

Timsina, Raju, and Laxman Mainali. "Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation." Membranes 11, no. 6 (June 15, 2021): 447. http://dx.doi.org/10.3390/membranes11060447.

Full text

Abstract:

α-crystallin is a major protein found in the mammalian eye lens that works as a molecular chaperone by preventing the aggregation of proteins and providing tolerance to stress in the eye lens. These functions of α-crystallin are significant for maintaining lens transparency. However, with age and cataract formation, the concentration of α-crystallin in the eye lens cytoplasm decreases with a corresponding increase in the membrane-bound α-crystallin, accompanied by increased light scattering. The purpose of this review is to summarize previous and recent findings of the role of the: (1) lens membrane components, i.e., the major phospholipids (PLs) and sphingolipids, cholesterol (Chol), cholesterol bilayer domains (CBDs), and the integral membrane proteins aquaporin-0 (AQP0; formally MIP26) and connexins, and (2) α-crystallin mutations and post-translational modifications (PTMs) in the association of α-crystallin to the eye lens’s fiber cell plasma membrane, providing thorough insights into a molecular basis of such an association. Furthermore, this review highlights the current knowledge and need for further studies to understand the fundamental molecular processes involved in the association of α-crystallin to the lens membrane, potentially leading to new avenues for preventing cataract formation and progression.

APA, Harvard, Vancouver, ISO, and other styles

16

Karmakar, Srabani, Shrutidhara Biswas, Kali P. Das, and Umakanta Tripathy. "Surface plasmon resonance study of the interaction of 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid dipotassium salt (bis-ANS) and adenosine triphosphate (ATP) with oligomeric recombinant human lens αA-crystallin." Canadian Journal of Chemistry 97, no. 6 (June 2019): 504–11. http://dx.doi.org/10.1139/cjc-2018-0412.

Full text

Abstract:

α-Crystallin, an abundant mammalian lens protein made up of two subunits (αA- and αB-crystallin), is involved in the maintenance of the optimal refractive index in the lens. The protein is implicated in the pathophysiology of a large number of retinal diseases including cataract, age-related macular degeneration, diabetic retinopathy, and uveitis. α-Crystallin belongs to the small heat shock protein (sHSP) family, forms large oligomeric structures, and functions as a molecular chaperone appearing very early during embryonic development. To gain mechanistic insight into the structural and functional role of α-crystallin and its alterations in various retinal diseases, it is important to study the interaction chemistry with its known partners. The hydrophobic sites in α-crystallin have been studied extensively using environmentally sensitive fluorescent probes such as 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid dipotassium salt (bis-ANS) that interacts with both subunits of α-cystallin in 1:1 stoichiometry at 37 °C and diminishes the chaperone-like activity of the protein. Furthermore, it has been shown that ATP plays a crucial role in the association of α-crystallin with substrate proteins. We use surface plasmon resonance (SPR) to monitor the interactions of immobilized oligomeric recombinant αA subunit of human α-crystallin protein with bis-ANS and ATP. We assess the thermodynamic parameters and kinetics of such interactions at various temperatures. Our results indicate that bis-ANS binds to αA-crystallin with higher affinity when compared with ATP, although both αA-crystallin and αB-crystallin display fast interaction kinetics.

APA, Harvard, Vancouver, ISO, and other styles

17

KUMAR, M. Satish, P. Yadagiri REDDY, P. Anil KUMAR, Ira SUROLIA, and G. Bhanuprakash REDDY. "Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assays." Biochemical Journal 379, no. 2 (April 15, 2004): 273–82. http://dx.doi.org/10.1042/bj20031633.

Full text

Abstract:

α-Crystallin is a member of the small heat-shock protein family and functions like a molecular chaperone, and may thus help in maintaining the transparency of the eye lens by protecting the lens proteins from various stress conditions. Non-enzymic glycation of long-lived proteins has been implicated in several age- and diabetes-related complications, including cataract. Dicarbonyl compounds such as methylglyoxal and glyoxal have been identified as the predominant source for the formation of advanced glycation end-products in various tissues including the lens. We have investigated the effect of non-enzymic browning of α-crystallin by reactive dicarbonyls on its molecular chaperone-like function. Non-enzymic browning of bovine α-crystallin in vitro caused, along with altered secondary and tertiary structures, cross-linking and high-molecular-mass aggregation. Notwithstanding these structural changes, methylglyoxal- and glyoxal-modified α-crystallin showed enhanced anti-aggregation activity in various in vitro aggregation assays. Paradoxically, increased chaperone-like activity of modified α-crystallin was not associated with increased surface hydrophobicity and rather showed less 8-anilinonaphthalene-l-sulphonic acid binding. In contrast, the chaperone-like function of modified α-crystallin was found to be reduced in assays that monitor the prevention of enzyme inactivation by UV-B and heat. Moreover, incubation of bovine lens with methylglyoxal in organ culture resulted in cataract formation with accumulation of advanced glycation end-products and recovery of α-crystallin in high proportions in the insoluble fraction. Furthermore, soluble α-crystallin from methylglyoxal-treated lenses showed decreased chaperone-like activity. Thus, in addition to describing the effects of methylglyoxal and glyoxal on structure and chaperone-like activity, our studies also bring out an important caveat of aggregation assays in the context of the chaperone function of α-crystallin.

APA, Harvard, Vancouver, ISO, and other styles

18

Posner, Mason, Kelly L. Murray, Matthew S. McDonald, Hayden Eighinger, Brandon Andrew, Amy Drossman, Zachary Haley, Justin Nussbaum, Larry L. David, and Kirsten J. Lampi. "The zebrafish as a model system for analyzing mammalian and native α-crystallin promoter function." PeerJ 5 (November 27, 2017): e4093. http://dx.doi.org/10.7717/peerj.4093.

Full text

Abstract:

Previous studies have used the zebrafish to investigate the biology of lens crystallin proteins and their roles in development and disease. However, little is known about zebrafish α-crystallin promoter function, how it compares to that of mammals, or whether mammalian α-crystallin promoter activity can be assessed using zebrafish embryos. We injected a variety of α-crystallin promoter fragments from each species combined with the coding sequence for green fluorescent protein (GFP) into zebrafish zygotes to determine the resulting spatiotemporal expression patterns in the developing embryo. We also measured mRNA levels and protein abundance for all three zebrafish α-crystallins. Our data showed that mouse and zebrafish αA-crystallin promoters generated similar GFP expression in the lens, but with earlier onset when using mouse promoters. Expression was also found in notochord and skeletal muscle in a smaller percentage of embryos. Mouse αB-crystallin promoter fragments drove GFP expression primarily in zebrafish skeletal muscle, with less common expression in notochord, lens, heart and in extraocular regions of the eye. A short fragment containing only a lens-specific enhancer region increased lens and notochord GFP expression while decreasing muscle expression, suggesting that the influence of mouse promoter control regions carries over into zebrafish embryos. The two paralogous zebrafish αB-crystallin promoters produced subtly different expression profiles, with the aBa promoter driving expression equally in notochord and skeletal muscle while the αBb promoter resulted primarily in skeletal muscle expression. Messenger RNA for zebrafish αA increased between 1 and 2 days post fertilization (dpf), αBa increased between 4 and 5 dpf, but αBb remained at baseline levels through 5 dpf. Parallel reaction monitoring (PRM) mass spectrometry was used to detect αA, aBa, and αBb peptides in digests of zebrafish embryos. In whole embryos, αA-crystallin was first detected by 2 dpf, peaked in abundance by 4–5 dpf, and was localized to the eye. αBa was detected in whole embryo at nearly constant levels from 1–6 dpf, was also localized primarily to the eye, and its abundance in extraocular tissues decreased from 4–7 dpf. In contrast, due to its low abundance, no αBb protein could be detected in whole embryo, or dissected eye and extraocular tissues. Our results show that mammalian α-crystallin promoters can be efficiently screened in zebrafish embryos and that their controlling regions are well conserved. An ontogenetic shift in zebrafish aBa-crystallin promoter activity provides an interesting system for examining the evolution and control of tissue specificity. Future studies that combine these promoter based approaches with the expanding ability to engineer the zebrafish genome via techniques such as CRISPR/Cas9 will allow the manipulation of protein expression to test hypotheses about lens crystallin function and its relation to lens biology and disease.

APA, Harvard, Vancouver, ISO, and other styles

19

Kase, Satoru. "Expression of α-Crystallin in Retinoblastoma." Archives of Ophthalmology 127, no. 2 (February 9, 2009): 187. http://dx.doi.org/10.1001/archophthalmol.2008.580.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Wang, Xiaowei, and Frederick A. Bettelheim. "Second virial coefficient of α-crystallin." Proteins: Structure, Function, and Genetics 5, no. 2 (1989): 166–69. http://dx.doi.org/10.1002/prot.340050211.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Cherian, M., and E. C. Abraham. "Diabetes Affects α-Crystallin Chaperone Function." Biochemical and Biophysical Research Communications 212, no. 1 (July 1995): 184–89. http://dx.doi.org/10.1006/bbrc.1995.1954.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Horwitz, Joseph, Michael P. Bova, Lin Lin Ding, Dana A. Haley, and Phoebe L. Stewart. "Lens α-crystallin: Function and structure." Eye 13, no. 3 (May 1999): 403–8. http://dx.doi.org/10.1038/eye.1999.114.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Facchiano, Francesco, Teodosio Libondi, Paola Stiuso, Ciro Esposito, Raffaele Ragone, and Giovanni Colonna. "Effect of Galactose on α-Crystallin." Ophthalmic Research 28, no. 1 (1996): 97–100. http://dx.doi.org/10.1159/000267980.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Augusteyn, Robert C., and Jane F. Koretz. "A possible structure for α-crystallin." FEBS Letters 222, no. 1 (September 28, 1987): 1–5. http://dx.doi.org/10.1016/0014-5793(87)80180-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Tardieu, Annette, Dominique Laporte, Pedro Licinio, Brigitte Krop, and Mireille Delaye. "Calf lens α-crystallin quaternary structure." Journal of Molecular Biology 192, no. 4 (December 1986): 711–24. http://dx.doi.org/10.1016/0022-2836(86)90023-9.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Attanasio, Francesco, Claudia Cascio, Salvatore Fisichella, Vincenzo Giuseppe Nicoletti, Bruno Pignataro, Anna Savarino, and Enrico Rizzarelli. "Trehalose effects on α-crystallin aggregates." Biochemical and Biophysical Research Communications 354, no. 4 (March 2007): 899–905. http://dx.doi.org/10.1016/j.bbrc.2007.01.061.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

GANEA, Elena, and John J. HARDING. "α-Crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase." Biochemical Journal 345, no. 3 (January 25, 2000): 467–72. http://dx.doi.org/10.1042/bj3450467.

Full text

Abstract:

α-Crystallin, a major lens protein, has many of the properties of a molecular chaperone, but its ability to assist refolding of proteins has been less certain. In the present work it was shown that α-crystallin specifically increased the reactivation of guanidine-denatured glyceraldehyde-3-phosphate dehydrogenase with most of the activity being recovered. In the incubation mixture the recovered enzyme activity was partly free but mostly it appeared in a protective complex with α-crystallin. The aggregation of the denatured enzyme on dilution from the guanidine solution was prevented. Thus α-crystallin not only protects against aggregation and inactivation of enzymes during denaturation, but can also prevent aggregation and assist recovery of the native structure during renaturation.

APA, Harvard, Vancouver, ISO, and other styles

28

James, M., and C. Crabbe. "Partial sequence homologies between cytoskeletal proteins, c-myc, Rous sarcoma virus and adenovirus proteins, transducin, and β- and γ-crystallins." Bioscience Reports 5, no. 2 (February 1, 1985): 167–74. http://dx.doi.org/10.1007/bf01117063.

Full text

Abstract:

Computer based sequence comparisons indicate partial sequence homology between human c-myc, Rous sarcoma virus, adenovirus 7, and simian sarcoma virus proteins and the cytoskeletal proteins desmin, keratin and vimentin. In addition, sections of the oncogene proteins showed partial but significant homology to α and β subunits of transducin, γ-II and β-BP crystallins showed partial but significant homology to the cytoskeletal proteins keratin, vimentin, desmin, α and β-tubulin, and to adenovirus 7 and simian sarcoma virus transforming gene proteins. β-BP crystallin showed partial but significant homology to Rous sarcoma virus protein, and to α and y subunits of transducin. Both crystallins showed partial sequence homology to the GTP-binding protein elongation factor TU from Escherichia coli. These sequence homologies suggest a link between the mechanisms of normal lens cell differentiation, involving modifications to the cytoskeleton and subsequent changes to the pattern of protein synthesis, and mechanisms of neoplastic transformation. Furthermore the transducin-like region on β-crystallin may be important for its interaction with lens membranes and the maintenance of short-range order for lens transparency.

APA, Harvard, Vancouver, ISO, and other styles

29

Feil, Ingeborg K., Marc Malfois, Jörg Hendle, Hans van der Zandt, and Dmitri I. Svergun. "A Novel Quaternary Structure of the Dimeric α-Crystallin Domain with Chaperone-like Activity." Journal of Biological Chemistry 276, no. 15 (January 12, 2001): 12024–29. http://dx.doi.org/10.1074/jbc.m010856200.

Full text

Abstract:

αB-crystallin, a member of the small heat-shock protein family and a major eye lens protein, is a high molecular mass assembly and can act as a molecular chaperone. We report a synchrotron radiation x-ray solution scattering study of a truncation mutant from the human αB-crystallin (αB57–157), a dimeric protein that comprises the α-crystallin domain of the αB-crystallin and retains a significant chaperone-like activity. According to the sequence analysis (more than 23% identity), the monomeric fold of the α-crystallin domain should be close to that of the small heat-shock protein fromMethanococcusjannaschii(MjHSP16.5). The theoretical scattering pattern computed from the crystallographic model of the dimeric MjHSP16.5 deviates significantly from the experimental scattering by the α-crystallin domain, pointing to different quaternary structures of the two proteins. A rigid body modeling against the solution scattering data yields a model of the α-crystallin domain revealing a new dimerization interface. The latter consists of a strand-turn-strand motif contributed by each of the monomers, which form a four-stranded, antiparallel, intersubunit composite β-sheet. This model agrees with the recent spin labeling results and suggests that the αB-crystallin is composed by flexible building units with an extended surface area. This flexibility may be important for biological activity and for the formation of αB-crystallin complexes of variable sizes and compositions.

APA, Harvard, Vancouver, ISO, and other styles

30

Bagnéris, C., O. A. Bateman, C. E. Naylor, N. Cronin, W. C. Boelens, N. H. Keep, and C. Slingsby. "Crystal Structures of α-Crystallin Domain Dimers of αB-Crystallin and Hsp20." Journal of Molecular Biology 392, no. 5 (October 2009): 1242–52. http://dx.doi.org/10.1016/j.jmb.2009.07.069.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Raman, Bakthisaran, Tadato Ban, Miyo Sakai, Saloni Y. Pasta, Tangirala Ramakrishna, Hironobu Naiki, Yuji Goto, and Ch Mohan Rao. "αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β2-microglobulin." Biochemical Journal 392, no. 3 (December 6, 2005): 573–81. http://dx.doi.org/10.1042/bj20050339.

Full text

Abstract:

αB-crystallin, a small heat-shock protein, exhibits molecular chaperone activity. We have studied the effect of αB-crystallin on the fibril growth of the Aβ (amyloid β)-peptides Aβ-(1–40) and Aβ-(1–42). αB-crystallin, but not BSA or hen egg-white lysozyme, prevented the fibril growth of Aβ-(1–40), as revealed by thioflavin T binding, total internal reflection fluorescence microscopy and CD spectroscopy. Comparison of the activity of some mutants and chimaeric α-crystallins in preventing Aβ-(1–40) fibril growth with their previously reported chaperone ability in preventing dithiothreitol-induced aggregation of insulin suggests that there might be both common and distinct sites of interaction on α-crystallin involved in the prevention of amorphous aggregation of insulin and fibril growth of Aβ-(1–40). αB-crystallin also prevents the spontaneous fibril formation (without externally added seeds) of Aβ-(1–42), as well as the fibril growth of Aβ-(1–40) when seeded with the Aβ-(1–42) fibril seed. Sedimentation velocity measurements show that αB-crystallin does not form a stable complex with Aβ-(1–40). The mechanism by which it prevents the fibril growth differs from the known mechanism by which it prevents the amorphous aggregation of proteins. αB-crystallin binds to the amyloid fibrils of Aβ-(1–40), indicating that the preferential interaction of the chaperone with the fibril nucleus, which inhibits nucleation-dependent polymerization of amyloid fibrils, is the mechanism that is predominantly involved. We found that αB-crystallin prevents the fibril growth of β2-microglobulin under acidic conditions. It also retards the depolymerization of β2-microglobulin fibrils, indicating that it can interact with the fibrils. Our study sheds light on the role of small heat-shock proteins in protein conformational diseases, particularly in Alzheimer's disease.

APA, Harvard, Vancouver, ISO, and other styles

32

Biswas, Ashis, Benlian Wang, Masaru Miyagi, and Ram H. Nagaraj. "Effect of methylglyoxal modification on stress-induced aggregation of client proteins and their chaperoning by human αA-crystallin." Biochemical Journal 409, no. 3 (January 15, 2008): 771–77. http://dx.doi.org/10.1042/bj20071006.

Full text

Abstract:

α-Crystallin prevents protein aggregation under various stress conditions through its chaperone-like properties. Previously, we demonstrated that MGO (methylglyoxal) modification of αA-crystallin enhances its chaperone function and thus may affect transparency of the lens. During aging of the lens, not only αA-crystallin, but its client proteins are also likely to be modified by MGO. We have investigated the role of MGO modification of four model client proteins (insulin, α-lactalbumin, alcohol dehydrogenase and γ-crystallin) in their aggregation and structure and the ability of human αA-crystallin to chaperone them. We found that MGO modification (10–1000 μM) decreased the chemical aggregation of insulin and α-lactalbumin and thermal aggregation of alcohol dehydrogenase and γ-crystallin. Surface hydrophobicity in MGO-modified proteins decreased slightly relative to unmodified proteins. HPLC and MS analyses revealed argpyrimidine and hydroimidazolone in MGO-modified client proteins. The degree of chaperoning by αA-crystallin towards MGO-modified and unmodified client proteins was similar. Co-modification of client proteins and αA-crystallin by MGO completely inhibited stress-induced aggregation of client proteins. Our results indicate that minor modifications of client proteins and αA-crystallin by MGO might prevent protein aggregation and thus help maintain transparency of the aging lens.

APA, Harvard, Vancouver, ISO, and other styles

33

Piatigorsky, Joram. "Molecular biology: Recent studies on enzyme/crystallins and α-crystallin gene expression." Experimental Eye Research 50, no. 6 (June 1990): 725–27. http://dx.doi.org/10.1016/0014-4835(90)90121-a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Putilina, T., Z. W. Zhang, and R. C. Augusteyn. "The effects of sonication on α-crystallin." Current Eye Research 10, no. 2 (January 1991): 113–20. http://dx.doi.org/10.3109/02713689109001738.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Vanhoudt, Jos, Saïd Abgar, Tony Aerts, and Julius Clauwaert. "Native Quaternary Structure of Bovine α-Crystallin†." Biochemistry 39, no. 15 (April 2000): 4483–92. http://dx.doi.org/10.1021/bi990386u.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Cobb, Brian A., and J. Mark Petrash. "Characterization of α-crystallin-plasma membrane binding." Journal of Biological Chemistry 277, no. 2 (January 2002): 1628. http://dx.doi.org/10.1016/s0021-9258(20)87969-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Ho, Yuh, Ming-Ching Hsu, and Fu-Yung Huang. "Chaperone Function of Rat Lens α-Crystallin." Journal of the Chinese Chemical Society 45, no. 2 (April 1998): 285–92. http://dx.doi.org/10.1002/jccs.199800045.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Finley, Eric L., James Dillon, Rosalie K. Crouch, and Kevin L. Schey. "Radiolysis-Induced Oxidation of Bovine α-Crystallin." Photochemistry and Photobiology 68, no. 1 (July 1998): 9–15. http://dx.doi.org/10.1111/j.1751-1097.1998.tb03245.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Cobb, Brian A., and J. Mark Petrash. "Characterization of α-Crystallin-Plasma Membrane Binding." Journal of Biological Chemistry 275, no. 9 (February 25, 2000): 6664–72. http://dx.doi.org/10.1074/jbc.275.9.6664.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Groenen, Patricia J. T. A., Paul R. L. A. van den Ijssel, Christina E. M. Voorter, Hans Bloemendal, and Wilfried W. de Jong. "Site-specific racemization in aging α-crystallin." FEBS Letters 269, no. 1 (August 20, 1990): 109–12. http://dx.doi.org/10.1016/0014-5793(90)81131-7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Carver, John A., J. Andrew Aquilina, Philip G. Cooper, Gavin A. Williams, and Roger J. W. Truscott. "α-Crystallin: molecular chaperone and protein surfactant." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1204, no. 2 (February 1994): 195–206. http://dx.doi.org/10.1016/0167-4838(94)90009-4.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Tue, Nguyen Trong, Kouhei Shimaji, Naoki Tanaka, and Masamitsu Yamaguchi. "Effect ofαB-Crystallin on Protein Aggregation inDrosophila." Journal of Biomedicine and Biotechnology 2012 (2012): 1–7. http://dx.doi.org/10.1155/2012/252049.

Full text

Abstract:

Disorganisation and aggregation of proteins containing expanded polyglutamine (polyQ) repeats, or ectopic expression of α-synuclein, underlie neurodegenerative diseases including Alzheimer’s, Parkinson, Huntington, Creutzfeldt diseases. Small heat-shock proteins, such as αB-crystallin, act as chaperones to prevent protein aggregation and play a key role in the prevention of such protein disorganisation diseases. In this study, we have explored the potential for chaperone activity of αB-crystallin to suppress the formation of protein aggregates. We tested the ability of αB-crystallin to suppress the aggregation of a polyQ protein and α-synuclein inDrosophila. We found that αB-crystallin suppresses both the compound eye degeneration induced by polyQ and the α-synuclein-induced rough eye phenotype. Furthermore, by using histochemical staining we have determined that αB-crystallin inhibits the aggregation of polyQin vivo. These data provide a clue for the development of therapeutics for neurodegenerative diseases.

APA, Harvard, Vancouver, ISO, and other styles

43

Banerjee, Priya R., Ajay Pande, Alexander Shekhtman, and Jayanti Pande. "Molecular Mechanism of the Chaperone Function of Mini-α-Crystallin, a 19-Residue Peptide of Human α-Crystallin." Biochemistry 54, no. 2 (December 26, 2014): 505–15. http://dx.doi.org/10.1021/bi5014479.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Liu, Haiquan, Xin Du, Meng Wang, Qingling Huang, Linlin Ding, Hayes W. McDonald, John R. Yates, Bruce Beutler, Joseph Horwitz, and Xiaohua Gong. "Crystallin γB-I4F Mutant Protein Binds to α-Crystallin and Affects Lens Transparency." Journal of Biological Chemistry 280, no. 26 (May 4, 2005): 25071–78. http://dx.doi.org/10.1074/jbc.m502490200.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Michiel, Magalie, Elodie Duprat, Fériel Skouri-Panet, Jason A. Lampi, Annette Tardieu, Kirsten J. Lampi, and Stéphanie Finet. "Aggregation of deamidated human βB2-crystallin and incomplete rescue by α-crystallin chaperone." Experimental Eye Research 90, no. 6 (June 2010): 688–98. http://dx.doi.org/10.1016/j.exer.2010.02.007.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Muranov, K. O., N. B. Poliansky, N. A. Chebotareva, S. Yu Kleimenov, A. E. Bugrova, M. I. Indeykina, A. S. Kononikhin, E. N. Nikolaev, and M. A. Ostrovsky. "The mechanism of the interaction of α-crystallin and UV-damaged βL-crystallin." International Journal of Biological Macromolecules 140 (November 2019): 736–48. http://dx.doi.org/10.1016/j.ijbiomac.2019.08.178.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Roman, Svetlana G., Natalia A. Chebotareva, and Boris I. Kurganov. "Concentration dependence of chaperone-like activities of α-crystallin, αB-crystallin and proline." International Journal of Biological Macromolecules 50, no. 5 (June 2012): 1341–45. http://dx.doi.org/10.1016/j.ijbiomac.2012.03.015.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Maiti, Motilal, Masahiro Kono, and Bireswar Chakrabarti. "Heat-induced changes in the conformation of α- and β-crystalline: Unique thermal stability of α-crystallin." FEBS Letters 236, no. 1 (August 15, 1988): 109–14. http://dx.doi.org/10.1016/0014-5793(88)80295-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Kumar, M. Satish, Mili Kapoor, Sharmistha Sinha, and G. Bhanuprakash Reddy. "Insights into Hydrophobicity and the Chaperone-like Function of αA- and αB-crystallins." Journal of Biological Chemistry 280, no. 23 (April 6, 2005): 21726–30. http://dx.doi.org/10.1074/jbc.m500405200.

Full text

Abstract:

α-Crystallin, composed of two subunits, αA and αB, has been shown to function as a molecular chaperone that prevents aggregation of other proteins under stress conditions. The exposed hydrophobic surfaces of α-crystallins have been implicated in this process, but their exact role has not been elucidated. In this study, we quantify the hydrophobic surfaces of αA- and αB-crystallins by isothermal titration calorimetry using 8-anilino-1-napthalenesulfonic acid (ANS) as a hydrophobic probe and analyze its correlation to the chaperone potential of αA- and αB-crystallins under various conditions. Two ANS binding sites, one with low and another with high affinity, were clearly detected, with αB showing a higher number of sites than αA at 30 °C. In agreement with the higher number of hydrophobic sites, αB-crystallin demonstrated higher chaperone activity than αA at this temperature. Thermodynamic analysis of ANS binding to αA- and αB-crystallins indicates that high affinity binding is driven by both enthalpy and entropy changes, with entropy dominating the low affinity binding. Interestingly, although the number of ANS binding sites was similar for αA and αB at 15 °C, αA was more potent than αB in preventing aggregation of the insulin B-chain. Although there was no change in the number of high affinity binding sites of αA and αB for ANS upon preheating, there was an increase in the number of low affinity sites of αA and αB. Preheated αA, in contrast to αB, exhibited remarkably enhanced chaperone activity. Our results indicate that although hydrophobicity appears to be a factor in determining the chaperone-like activity of α-crystallins, it does not quantitatively correlate with the chaperone function of α-crystallins.

APA, Harvard, Vancouver, ISO, and other styles

50

Reddy, G. Bhanuprakash, P. Yadagiri Reddy, and Avadhesha Surolia. "Alzheimer’s and Danish dementia peptides induce cataract and perturb retinal architecture in rats." Biomolecular Concepts 8, no. 1 (March 1, 2017): 45–84. http://dx.doi.org/10.1515/bmc-2016-0025.

Full text

Abstract:

AbstractFamilial Danish dementias (FDDs) are autosomal dominant neurodegenerative disorders that are associated with visual defects. In some aspects, FDD is similar to Alzheimer’s disease (AD)– the amyloid deposits in FDD and AD are made of short peptides: amyloid β (Aβ) in AD and ADan in FDD. Previously, we demonstrated an interaction between the dementia peptides and α-crystallin leading to lens opacification in organ culture due to impaired chaperone activity of α-crystallin. Herein, we report the in vivo effects of ADan and Aβ on the eye. ADan [reduced (ADan-red) and oxidized (ADan-oxi)] and Aβ (Aβ1-40 and Aβ1-42) were injected intravitreally in rats. The onset of cataract was seen after injection of all the peptides, but the cataract matured by 2 weeks in the case of ADan-red, 5 weeks for ADan-oxi and 6 weeks for Aβ1-40, while Aβ1-42 had minimal effect on cataract progression. The severity of cataract is associated with insolubilization and alterations in crystallins and loss of chaperone activity of α-crystallin. Further, disruption of the architecture of the retina was evident from a loss of rhodopsin, increased gliosis, and the thinning of the retina. These results provide a basis for the dominant heredo-otoophthalmo-encephalopathy (HOOE)/FDD syndrome and indicate that ADan peptides are more potent than Aβpeptides in inflicting visual impairment.

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!