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Journal articles on the topic 'Α-crystallin'

Author: Grafiati

Published: 4 June 2021

Last updated: 24 July 2025

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1

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

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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, slight

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2

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

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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 th

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3

Chang, Yu-Yung, Meng-Hsuan Hsieh, Yen-Chieh Huang, Chun-Jung Chen та Ming-Tao Lee. "Conformational Changes of α-Crystallin Proteins Induced by Heat Stress". International Journal of Molecular Sciences 23, № 16 (2022): 9347. http://dx.doi.org/10.3390/ijms23169347.

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α-crystallin is a major structural protein in the eye lenses of vertebrates that is composed of two relative subunits, αA and αB crystallin, which function in maintaining lens transparency. As a member of the small heat-shock protein family (sHsp), α-crystallin exhibits chaperone-like activity to prevent the misfolding or aggregation of critical proteins in the lens, which is associated with cataract disease. In this study, high-purity αA and αB crystallin proteins were expressed from E. coli and purified by affinity and size-exclusion chromatography. The size-exclusion chromatography experime

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4

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

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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

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5

Dominova, Irina N., and Valery V. Zhukov. "Mollusc Crystallins: Physical and Chemical Properties and Phylogenetic Analysis." Diversity 14, no. 10 (2022): 827. http://dx.doi.org/10.3390/d14100827.

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The purpose of the present study was to perform bioinformatic analysis of crystallin diversity in aquatic molluscs based on the sequences in the NCBI Protein database. The objectives were as follows: (1) analysis of some physical and chemical properties of mollusc crystallins, (2) comparison of mollusc crystallins with zebrafish and cubomedusa Tripedalia cystophora crystallins, and (3) determination of the most probable candidates for the role of gastropod eye crystallins. The calculated average GRAVY values revealed that the majority of the seven crystallin groups, except for μ- and ζ-crystal

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Muranov, Konstantin O., Nicolay B. Poliansky, Vera A. Borzova та Sergey Y. Kleimenov. "Refolding Increases the Chaperone-like Activity of αH-Crystallin and Reduces Its Hydrodynamic Diameter to That of α-Crystallin". International Journal of Molecular Sciences 24, № 17 (2023): 13473. http://dx.doi.org/10.3390/ijms241713473.

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αH-Crystallin, a high molecular weight form of α-crystallin, is one of the major proteins in the lens nucleus. This high molecular weight aggregate (HMWA) plays an important role in the pathogenesis of cataracts. We have shown that the chaperone-like activity of HMWA is 40% of that of α-crystallin from the lens cortex. Refolding with urea significantly increased—up to 260%—the chaperone-like activity of α-crystallin and slightly reduced its hydrodynamic diameter (Dh). HMWA refolding resulted in an increase in chaperone-like activity up to 120% and a significant reduction of Dh of protein parti

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7

Timsina, Raju, Samantha Wellisch, Dieter Haemmerle, and Laxman Mainali. "Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens." International Journal of Molecular Sciences 23, no. 19 (2022): 11295. http://dx.doi.org/10.3390/ijms231911295.

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Several studies reported that α-crystallin concentrations in the eye lens cytoplasm decrease with a corresponding increase in membrane-bound α-crystallin with age and cataracts. The influence of the lipid and cholesterol composition difference between cortical membrane (CM) and nuclear membrane (NM) on α-crystallin binding to membranes is still unclear. This study uses the electron paramagnetic resonance (EPR) spin-labeling method to investigate the α-crystallin binding to bovine CM and NM derived from the total lipids extracted from a single lens. Compared to CMs, NMs have a higher percentage

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8

Besirli, Cagri G., Madhu Nath, Jingyu Yao, et al. "HSPB4/CRYAA Protect Photoreceptors during Retinal Detachment in Part through FAIM2 Regulation." Neurology International 16, no. 5 (2024): 905–17. http://dx.doi.org/10.3390/neurolint16050068.

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Our previous study discussed crystallin family induction in an experimental rat model of retinal detachment. Therefore, we attempted to evaluate the role of α-crystallin in photoreceptor survival in an experimental model of retinal detachment, as well as its association with the intrinsically neuroprotective protein Fas-apoptotic inhibitory molecule 2 (FAIM2). Separation of retina and RPE was induced in rat and mouse eyes by subretinal injection of hyaluronic acid. Retinas were subsequently analyzed for the presence αA-crystallin (HSPB4) and αB-crystallin (HSPB5) proteins using immunohistochem

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9

LINDNER, Robyn A., Teresa M. TREWEEK та 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, № 1 (2001): 79–87. http://dx.doi.org/10.1042/bj3540079.

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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-Crystal

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10

Khadka, Nawal K., Raju Timsina та Laxman Mainali. "An AFM Approach Applied in a Study of α-Crystallin Membrane Association: New Insights into Lens Hardening and Presbyopia Development". Membranes 12, № 5 (2022): 522. http://dx.doi.org/10.3390/membranes12050522.

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The lens of the eye loses elasticity with age, while α-crystallin association with the lens membrane increases with age. It is unclear whether there is any correlation between α-crystallin association with the lens membrane and loss in lens elasticity. This research investigated α-crystallin membrane association using atomic force microscopy (AFM) for the first time to study topographical images and mechanical properties (breakthrough force and membrane area compressibility modulus (KA), as measures of elasticity) of the membrane. α-Crystallin extracted from the bovine lens cortex was incubate

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11

Chakraborty, Aparajita. "Study on the Effects of different methods of Delaying Ripening in Avocado Pear and Banana Fruits." Bulletin of Scientific Research 4, no. 2 (2022): 9–14. http://dx.doi.org/10.54392/bsr2222.

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Crystallins are the predominant proteins of the eye lens which prevent the heat and oxidative-induced stress-induced aggregation of other proteins. They may be classified into two superfamilies, the α- and βγ- crystallins. The βγ- crystallins are long-lived structural proteins which refract light onto the retina. The microbial crystallins can not only bind to calcium ions, but even able to coordinate other ions such as Mg2+, Sr2+, Co2+, Mn2+, Ni2+, Zn2+ etc. Such metal ions may influence the stability and aggregation propensity of human γS- crystallin as well. Previous studies had even reveale

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12

Serebryany, Eugene, Rachel W. Martin та Gemma R. Takahashi. "The Functional Significance of High Cysteine Content in Eye Lens γ-Crystallins". Biomolecules 14, № 5 (2024): 594. http://dx.doi.org/10.3390/biom14050594.

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Cataract disease is strongly associated with progressively accumulating oxidative damage to the extremely long-lived crystallin proteins of the lens. Cysteine oxidation affects crystallin folding, interactions, and light-scattering aggregation especially strongly due to the formation of disulfide bridges. Minimizing crystallin aggregation is crucial for lifelong lens transparency, so one might expect the ubiquitous lens crystallin superfamilies (α and βγ) to contain little cysteine. Yet, the Cys content of γ-crystallins is well above the average for human proteins. We review literature relevan

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13

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

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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 induc

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14

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

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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 significa

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15

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

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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

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16

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

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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 w

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17

Trossi-Torres, Geraline, Raju Timsina, and Laxman Mainali. "Alpha-Crystallin-Membrane Association Modulated by Phospholipid Acyl Chain Length and Degree of Unsaturation." Membranes 12, no. 5 (2022): 455. http://dx.doi.org/10.3390/membranes12050455.

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α-crystallin-membrane association increases with age and cataracts, with the primary association site of α-crystallin being phospholipids. However, it is unclear if phospholipids’ acyl chain length and degree of unsaturation influence α-crystallin association. We used the electron paramagnetic resonance approach to investigate the association of α-crystallin with phosphatidylcholine (PC) membranes of different acyl chain lengths and degrees of unsaturation and with and without cholesterol (Chol). The association constant (Ka) of α-crystallin follows the trends, i.e., Ka (14:0–14:0 PC) > Ka

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18

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 (2021): 447. http://dx.doi.org/10.3390/membranes11060447.

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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 me

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Karmakar, Srabani, Shrutidhara Biswas, Kali P. Das та 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, № 6 (2019): 504–11. http://dx.doi.org/10.1139/cjc-2018-0412.

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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 funct

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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 (2004): 273–82. http://dx.doi.org/10.1042/bj20031633.

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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 o

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21

Chakraborty, Aparajita. "Role of α-Crystallin protein-protein interactions in disorders of the system and its therapeutic approaches: a new study". Bulletin of Scientific Research 5, № 1 (2023): 15–19. http://dx.doi.org/10.54392/bsr2312.

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α- Crystallin, a major eye lens protein with chaperone activity is vital in cataract development. As a member of the small heat shock protein superfamily, α-Crystallin is able to recognise and bind denatured or unfolded proteins, thereby preventing their aggregation. An important constituent of eye drops and artificial tears is polyethylene glycol-400(PEG-400) which can interact with α- Crystallin and lead to alterations in its tertiary structure, namely the global transition to a non-native form. Another protein, which is characterised by its presence in the insoluble fraction of vertebrate n

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

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23

Khan, Shabnam, Bushra Wasim Khan, Madeeha Sadiq, Fawad Rizvi, Faraz Ahmed Baig та Rehan Ahmed Siddiqui. "Immunohistochemical Expression of Alpha (Α) A Crystallin in Senile Degenerative and Non-Cataract Lenses". Pakistan Journal of Medical and Health Sciences 15, № 10 (2021): 2643–46. http://dx.doi.org/10.53350/pjmhs2115102643.

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Aim: Comparative immunohistochemical study of expression of α A Crystallin in non-cataract lenses and age-related cataract lenses in humans. Methodology: This was an observational cross sectional study. There are two groups in this study. Group A comprised of 121 senile degenerative cataract lenses from diagnosed patients. Group B included of 10 non-cataract lenses from patients who underwent surgeries for enucleation due to trauma and retinoblastoma. Lenses were fixed in 10% Buffered Neutral Formalin and processed to make paraffin blocks. Immunohistochemistry (IHC) staining was performed on s

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

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Posner, Mason, Kelly L. Murray, Matthew S. McDonald та ін. "The zebrafish as a model system for analyzing mammalian and native α-crystallin promoter function". PeerJ 5 (27 листопада 2017): e4093. http://dx.doi.org/10.7717/peerj.4093.

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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

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

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

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

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

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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-cr

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

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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 fromMethanoco

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James, M., та 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, № 2 (1985): 167–74. http://dx.doi.org/10.1007/bf01117063.

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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

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Malik, Ajamaluddin, Hajar Ahmed Almaharfi, Javed Masood Khan та ін. "Protection of ζ-crystallin by α-crystallin under thermal stress". International Journal of Biological Macromolecules 167 (січень 2021): 289–98. http://dx.doi.org/10.1016/j.ijbiomac.2020.11.183.

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

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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-cryst

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Raman, Bakthisaran, Tadato Ban, Miyo Sakai та ін. "αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β2-microglobulin". Biochemical Journal 392, № 3 (2005): 573–81. http://dx.doi.org/10.1042/bj20050339.

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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-induce

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Tue, Nguyen Trong, Kouhei Shimaji, Naoki Tanaka та 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.

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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 suppres

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

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

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

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

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

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

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

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Attanasio, Francesco, Claudia Cascio, Salvatore Fisichella та ін. "Trehalose effects on α-crystallin aggregates". Biochemical and Biophysical Research Communications 354, № 4 (2007): 899–905. http://dx.doi.org/10.1016/j.bbrc.2007.01.061.

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DERHAM, Barry K., та John J. HARDING. "Enzyme activity after resealing within ghost erythrocyte cells, and protection by α-crystallin against fructose-induced inactivation". Biochemical Journal 368, № 3 (2002): 865–74. http://dx.doi.org/10.1042/bj20020924.

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The role of α-crystallin as a molecular chaperone has been shown in many in vitro studies. In the present paper, we report on the chaperone function of α-crystallin within resealed erythrocyte ghosts. Eight enzymes were individually resealed within erythrocyte ghosts and assayed at zero time and at 24h. The ghost cell suspension was separated into soluble and membrane fractions. Five of the enzymes had significantly greater enzyme activity after 24h than the control within the soluble fractions. Fructation caused a decrease in enzyme activity (relative to the control). Resealing of α-crystalli

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Sarnat, Harvey B., та Laura Flores-Sarnat. "α-B-Crystallin as a Tissue Marker of Epileptic Foci in Paediatric Resections". Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 36, № 5 (2009): 566–74. http://dx.doi.org/10.1017/s0317167100008052.

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Background:We studied α-B-crystallin, a small heat shock chaperone protein upregulated by various “stresses”, as an immunocytochemical tissue marker of epileptic foci.Methods:We examined 45 resected brain tissues of epileptic patients, 16 months to 23 years. Postmortem brains of 2 epileptic children and 20 normal fetuses and neonates of 10-41 weeks gestation similarly were studied. Immunocytochemical demonstration of α-B-crystallin was supplemented by neuronal, glial and inflammatory cell markers and electron microscopy (EM) in surgical cases. Autopsy brain tissue of children without epilepsy

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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 (2017): 45–84. http://dx.doi.org/10.1515/bmc-2016-0025.

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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)] a

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Hazen, Preston, Geraline Trossi-Torres, Raju Timsina, Nawal K. Khadka, and Laxman Mainali. "Association of Alpha-Crystallin with Human Cortical and Nuclear Lens Lipid Membrane Increases with the Grade of Cortical and Nuclear Cataract." International Journal of Molecular Sciences 25, no. 3 (2024): 1936. http://dx.doi.org/10.3390/ijms25031936.

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Eye lens α-crystallin has been shown to become increasingly membrane-bound with age and cataract formation; however, to our knowledge, no studies have investigated the membrane interactions of α-crystallin throughout the development of cataracts in separated cortical membrane (CM) and nuclear membrane (NM) from single human lenses. In this study, four pairs of human lenses from age-matched male and female donors and one pair of male lenses ranging in age from 64 to 73 years old (yo) were obtained to investigate the interactions of α-crystallin with the NM and CM throughout the progression of c

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

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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. Tw

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Kulig, Melissa, та Heath Ecroyd. "The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin". Biochemical Journal 448, № 3 (2012): 343–52. http://dx.doi.org/10.1042/bj20121187.

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Stress conditions can destabilize proteins, promoting them to unfold and adopt intermediately folded states. Partially folded protein intermediates are unstable and prone to aggregation down off-folding pathways leading to the formation of either amorphous or amyloid fibril aggregates. The sHsp (small heat-shock protein) αB-crystallin acts as a molecular chaperone to prevent both amorphous and fibrillar protein aggregation; however, the precise molecular mechanisms behind its chaperone action are incompletely understood. To investigate whether the chaperone activity of αB-crystallin is depende

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TAKEUCHI, Satoru, Yumi MANDAI, Akiko OTSU, Taro SHIRAKAWA, Katsuyoshi MASUDA та Masanobu CHINAMI. "Differences in properties between human αA- and αB-crystallin proteins expressed in Escherichia coli cells in response to cold and extreme pH". Biochemical Journal 375, № 2 (2003): 471–75. http://dx.doi.org/10.1042/bj20030748.

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It has been reported that αA-crystallin has greater protective effects against apoptosis in lens epithelial cells than αB-crystallin [Andley, Song, Wawrousek, Fleming and Bassnett (2000) J. Biol. Chem. 275, 36823–36831]. Because the αA-crystallin proteins are specifically expressed in the vertebrate lens, we examine the non-specific properties of both αA- and αB-crystallins in an Escherichia coli system. E. coli cells were transformed with the inducible protein expression vector pET-11a, harbouring the gene for either human αA- or αB-crystallin, and two other control plasmids, pET-1la vector a

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