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Journal articles on the topic 'Β-crystallin'

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Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

Belisle, E. H., S. W. Su, B. W. Lubit, and S. C. J. Fu. "Homology among β-crystallins: Monoclonal antibodies to β-heavy crystallin." Current Eye Research 6, no. 8 (January 1987): 951–57. http://dx.doi.org/10.3109/02713688709034866.

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2

Hejtmancik, J. F., P. T. Wingfield, and Y. V. Sergeev. "β-Crystallin association." Experimental Eye Research 79, no. 3 (September 2004): 377–83. http://dx.doi.org/10.1016/j.exer.2004.06.011.

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3

Song, In-Kang, Seungjin Na, Eunok Paek, and Kong-Joo Lee. "Cataract-Associated New Mutants S175G/H181Q of βΒ2-Crystallin and P24S/S31G of γD-Crystallin Are Involved in Protein Aggregation by Structural Changes." International Journal of Molecular Sciences 21, no. 18 (September 5, 2020): 6504. http://dx.doi.org/10.3390/ijms21186504.

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β/γ-Crystallins, the main structural protein in human lenses, have highly stable structure for keeping the lens transparent. Their mutations have been linked to cataracts. In this study, we identified 10 new mutations of β/γ-crystallins in lens proteomic dataset of cataract patients using bioinformatics tools. Of these, two double mutants, S175G/H181Q of βΒ2-crystallin and P24S/S31G of γD-crystallin, were found mutations occurred in the largest loop linking the distant β-sheets in the Greek key motif. We selected these double mutants for identifying the properties of these mutations, employing biochemical assay, the identification of protein modifications with nanoUPLC-ESI-TOF tandem MS and examining their structural dynamics with hydrogen/deuterium exchange-mass spectrometry (HDX-MS). We found that both double mutations decrease protein stability and induce the aggregation of β/γ-crystallin, possibly causing cataracts. This finding suggests that both the double mutants can serve as biomarkers of cataracts.

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4

Feng, Jinhua, David L. Smith, and Jean B. Smith. "Human Lens β-Crystallin Solubility." Journal of Biological Chemistry 275, no. 16 (April 14, 2000): 11585–90. http://dx.doi.org/10.1074/jbc.275.16.11585.

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5

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.

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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 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.

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6

Pan, F. M., W. C. Chang, S. F. Lu, A. L. Hsu, and S. H. Chiou. "Sequence Analysis of One Major Basic β-Crystallin (β-Bp) of Amphibian Lenses - Evolutionary Comparison and Phylogenetic Relatedness Between β-Crystallin and γ-Crystallin." Biochemical and Biophysical Research Communications 217, no. 3 (December 1995): 940–49. http://dx.doi.org/10.1006/bbrc.1995.2861.

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7

Leng, Xiao-Yao, Sha Wang, Ni-Qian Cao, Liang-Bo Qi, and Yong-Bin Yan. "The N-Terminal Extension of βB1-Crystallin Chaperones β-Crystallin Folding and Cooperates with αA-Crystallin." Biochemistry 53, no. 15 (April 8, 2014): 2464–73. http://dx.doi.org/10.1021/bi500146d.

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8

Leng, Xiao-Yao, Hai-Yun Li, Jing Wang, Liang-Bo Qi, Yi-Bo Xi, and Yong-Bin Yan. "Congenital microcornea-cataract syndrome-causing mutation X253R increases βB1-crystallin hydrophobicity to promote aggregate formation." Biochemical Journal 473, no. 14 (July 12, 2016): 2087–96. http://dx.doi.org/10.1042/bcj20160247.

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The high solubility and lifelong stability of crystallins are crucial to the maintenance of lens transparency and optical properties. Numerous crystallin mutations have been linked to congenital cataract, which is one of the leading causes of newborn blindness. Besides cataract, several crystallin mutations have also been linked to syndromes such as congenital microcornea-cataract syndrome (CMCC). However, the molecular mechanism of CMCC caused by crystallin mutations remains elusive. In the present study, we investigated the mechanism of CMCC caused by the X253R mutation in βB1-crystallin. The exogenously expressed X253R proteins were prone to form p62-negative aggregates in HeLa cells, strongly inhibited cell proliferation and induced cell apoptosis. The intracellular X253R aggregates could be successfully redissolved by lanosterol but not cholesterol. The extra 26 residues at the C-terminus of βB1-crystallin introduced by the X253R mutation had little impact on βB1-crystallin structure and stability, but increased βB1-crystallin hydrophobicity and decreased its solubility. Interestingly, the X253R mutant fully abolished the aggregatory propensity of βB1- and βA3/βB1-crystallins at high temperatures, suggesting that X253R was an aggregation-inhibition mutation of β-crystallin homomers and heteromers in dilute solutions. Our results suggest that an increase in hydrophobicity and a decrease in solubility might be responsible for cataractogenesis induced by the X253R mutation, while the cytotoxic effect of X253R aggregates might contribute to the defects in ocular development. Our results also highlight that, at least in some cases, the aggregatory propensity in dilute solutions could not fully mimic the behaviours of mutated proteins in the crowded cytoplasm of the cells.

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9

Wang, Sha, Xiao-Yao Leng, and Yong-Bin Yan. "The Benefits of Being β-Crystallin Heteromers: βB1-Crystallin Protects βA3-Crystallin against Aggregation during Co-refolding." Biochemistry 50, no. 48 (December 6, 2011): 10451–61. http://dx.doi.org/10.1021/bi201375p.

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10

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.

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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-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.

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11

Jiang, Y. J., S. H. Chiou, and W. C. Chang. "Lens crystallin changes associated with amphibian metamorphosis: Involvement of a β-crystallin polypeptide." Biochemical and Biophysical Research Communications 164, no. 3 (November 1989): 1423–30. http://dx.doi.org/10.1016/0006-291x(89)91829-9.

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12

Lu, Shao-Fan, Fu-Ming Pan, and Shyh-Horng Chiou. "Sequence Analysis of Four Acidic β-Crystallin Subunits of Amphibian Lenses: Phylogenetic Comparison between β- and γ-Crystallins." Biochemical and Biophysical Research Communications 221, no. 2 (April 1996): 219–28. http://dx.doi.org/10.1006/bbrc.1996.0577.

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13

Liang, Jack J. N. "Interaction between β-amyloid and lens αB-crystallin." FEBS Letters 484, no. 2 (October 31, 2000): 98–101. http://dx.doi.org/10.1016/s0014-5793(00)02136-0.

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14

Stege, G. J. J., K. Renkawek, P. S. G. Overkamp, P. Verschuure, A. F. van Rijk, A. Reijnen-Aalbers, W. C. Boelens, G. J. C. G. M. Bosman, and W. W. de Jong. "The Molecular Chaperone αB-crystallin Enhances Amyloid β Neurotoxicity." Biochemical and Biophysical Research Communications 262, no. 1 (August 1999): 152–56. http://dx.doi.org/10.1006/bbrc.1999.1167.

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15

Shinkai, Yasuhiro, Yunjie Ding, Takashi Miura, and Yoshito Kumagai. "Aggregation of β-crystallin through covalent binding to 1,2-naphthoquinone is rescued by α-crystallin chaperone." Journal of Toxicological Sciences 45, no. 1 (2020): 37–43. http://dx.doi.org/10.2131/jts.45.37.

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16

Kase, Satoru, Shikun He, Shozo Sonoda, Mizuki Kitamura, Christine Spee, Eric Wawrousek, Stephen J. Ryan, Ram Kannan, and David R. Hinton. "αB-crystallin regulation of angiogenesis by modulation of VEGF." Blood 115, no. 16 (April 22, 2010): 3398–406. http://dx.doi.org/10.1182/blood-2009-01-197095.

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Abstract αB-crystallin is a chaperone belonging to the small heat shock protein family. Herein we show attenuation of intraocular angiogenesis in αB-crystallin knockout (αB-crystallin−/−) mice in 2 models of intraocular disease: oxygen-induced retinopathy and laser-induced choroidal neovascularization. Vascular endothelial growth factor A (VEGF-A) mRNA and hypoxia inducible factor-1α protein expression were induced during retinal angiogenesis, but VEGF-A protein expression remained low in αB-crystallin−/− retina versus wild-type mice, whereas VEGF-R2 expression was not affected. Both αB-crystallin and its phosphorylated serine59 formwere expressed, and immunoprecipitation revealed αB-crystallin binding to VEGF-A but not transforming growth factor-β in cultured retinal pigment epithelial (RPE) cells. αB-crystallin and VEGF-A are colocalized in the endoplasmic reticulum in RPE cells under chemical hypoxia. αB-crystallin−/− RPE showed low VEGF-A secretion under serum-starved conditions compared with wild-type cells. VEGF-A is polyubiquitinated in control and αB-crystallin siRNA treated RPE; however, mono-tetra ubiquitinated VEGF-A increases with αB-crystallin knockdown. Endothelial cell apoptosis in newly formed vessels was greater in αB-crystallin−/− than wild-type mice. Proteasomal inhibition in αB-crystallin−/− mice partially restores VEGF-A secretion and angiogenic phenotype in choroidal neovascularization. Our studies indicate an important role for αB-crystallin as a chaperone for VEGF-A in angiogenesis and its potential as a therapeutic target.

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17

Chen, Jyh-Yih, Bei-En Chang, Yi-Hsuan Chen, Cliff Ji-Fan Lin, Jen-Leih Wu, and Ching-Ming Kuo. "Molecular Cloning, Developmental Expression, and Hormonal Regulation of Zebrafish (Danio rerio) β Crystallin B1, a Member of the Superfamily of β Crystallin Proteins." Biochemical and Biophysical Research Communications 285, no. 1 (July 2001): 105–10. http://dx.doi.org/10.1006/bbrc.2001.5099.

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18

YAN, Hong, Antony C. WILLIS, and John J. HARDING. "γIII-Crystallin is the primary target of glycation in the bovine lens incubated under physiological conditions." Biochemical Journal 374, no. 3 (September 15, 2003): 677–85. http://dx.doi.org/10.1042/bj20030542.

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Several mechanisms have been proposed for the way in which glucose and its metabolites cause cataract, retinopathy and other complications of diabetes, the most convincing being glycation. Glycation, the reaction of sugars with free amino groups of proteins, is one of a variety of non-enzymic post-translational modifications. The aim of the present study was to identify some of the most reactive proteins in the lens when incubated under physiological conditions. Fresh intact bovine lenses were incubated with [14C]glucose in a conventional tissue-culture medium with added antibiotics. After 3 and 6 days of incubation, the water-soluble proteins were separated by size-exclusion chromatography. Glycated proteins from the water-soluble fractions were separated by using a sugar affinity column (Affi-Gel 601). Then the radioactive fractions were identified on SDS/polyacrylamide gels. In addition, the whole bovine lenses were incubated with 10 mM fructose and glucose for 3 and 6 days. The glycated proteins from the water-soluble fractions in parallel with the radioactive fractions were separated by affinity chromatography, and were identified further by amino-acid sequencing. A progressive uptake of radioactive label showed that the majority of proteins incorporating both glucose and fructose were water-soluble fractions. Chromatography and SDS/polyacrylamide gel results showed that α- and γ-crystallin and some proteins of a mean molecular mass of 36–37 kDa incorporated sugars early during incubation. After 6 days of incubation, more crystallins were glycated compared with 3 days, in particular β-crystallin. Affinity-chromatography results indicated that proteins with subunit masses of 36 kDa and 20 kDa were possibly radiolabelled at an early stage. The purified glycated proteins following incubation with both glucose and fructose, which corresponded to 20 kDa and 36 kDa bands on SDS/polyacrylamide gels, were sequenced by Edman degradation. N-terminal sequences of both 20 kDa bands were Gly-Lys-Ile-Thr, characteristic of γ-crystallins, but the N-termini of both 36 kDa bands were blocked. Further sequencing after digestion of 36 kDa bands with trypsin and running on HPLC revealed that the glucose sample gave the peptide sequences as Gly-Glu-Tyr-Pro-Asp-Tyr-Gln-Gln and Tyr-Glu-Leu-Pro-Asn-Tyr-Arg, which match with bovine γIIIb-crystallin. The peptide sequence Tyr-Glu-Leu-Pro-Asn-Tyr-Arg is only present in the published sequence of bovine γIIIb-crystallin and not in any other type of γ-crystallin. The fructose sample gave the peptide sequences Ile-Thr-Phe-Tyr-Glu-Asp-Arg, Arg-Gly-Asp-Tyr-Pro-Asp-Tyr-Gln-Gln-Trp, Gln-Tyr-Leu-Leu-Arg and Val-Val-Asp-Leu-Tyr, which all matched with bovine γIIIa-crystallin. The sequence Val-Val-Asp-Leu-Tyr only appears in the sequence of bovine γIIIa-crystallin. γIII-Crystallin is the most susceptible lens protein to glycation. The primary target of glucose is γIIIb-crystallin, whereas that of fructose is γIIIa-crystallin. The early glycation of γIII-crystallin by glucose and fructose could result in structural alterations, leading to aggregation of crystallin and eventually cataract formation.

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19

Hejtmancik, J. F., P. T. Wingfield, and Y. V. Sergeev. "β-Crystallin association [Experimental Eye Research 79 (2004) 377–383]." Experimental Eye Research 79, no. 6 (December 2004): 785. http://dx.doi.org/10.1016/s0014-4835(04)00303-3.

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20

Siezen, Roland J., Robert D. Anello, and John A. Thomson. "Interactions of lens proteins. Concentration dependence of β-crystallin aggregation." Experimental Eye Research 43, no. 3 (September 1986): 293–303. http://dx.doi.org/10.1016/s0014-4835(86)80067-7.

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21

Kroone, R. C., G. S. Elliott, A. Ferszt, C. Slingsby, N. H. Lubsen, and J. G. G. Schoenmakers. "The role of the sequence extensions in β-crystallin assembly." "Protein Engineering, Design and Selection" 7, no. 11 (1994): 1395–99. http://dx.doi.org/10.1093/protein/7.11.1395.

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22

Lapatto, R., V. Nalini, B. Bax, H. Driessen, P. F. Lindley, T. L. Blundell, and C. Slingsby. "High resolution structure of an oligomeric eye lens β-crystallin." Journal of Molecular Biology 222, no. 4 (December 1991): 1067–83. http://dx.doi.org/10.1016/0022-2836(91)90594-v.

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23

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.

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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 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.

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24

Wu, Fang, Liangkai Cheng, Qi Yu, Lin Zhang, Hong Li, and Caiyan Wang. "Purification and Functional Characterization of the C-Terminal Domain of the β-Actin-Binding Protein AIM1 In Vitro." Molecules 23, no. 12 (December 11, 2018): 3281. http://dx.doi.org/10.3390/molecules23123281.

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The protein absent in melanoma 1 (AIM1) is a member of the βγ-crystal lens superfamily that is associated with the development of multiple cancers. The binding of AIM1 to β-actin affects the migration and invasion of prostate cancer epithelial cells. The C-terminus of AIM1 is required for the β-actin interaction. However, the characteristics of AIM1 in vitro and the interaction mode between AIM1 and β-actin remain unknown. We describe novel methods to prepare pure recombinant AIM1 and identify possible binding modes between AIM1 and β-actin; we also obtain the crystal of the first two βγ-crystallin domains of AIM1 (g1g2) for future structural biology research. We first express and purify AIM1 after cloning the sequence into a modified pET-28a_psp expression vector. Next, we define the minimum unit formed by the βγ-crystallin domain repeats that bound to β-actin and perform its physiological function. Finally, we made the structural model of the AIM1 g1g2 that can be used to guide future biomedical investigations and prostate cancer research.

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25

Duncan, Melinda K., John I. Haynes, Ales Cvekl, and Joram Piatigorsky. "Dual Roles for Pax-6: a Transcriptional Repressor of Lens Fiber Cell-Specific β-Crystallin Genes." Molecular and Cellular Biology 18, no. 9 (September 1, 1998): 5579–86. http://dx.doi.org/10.1128/mcb.18.9.5579.

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ABSTRACT It has been demonstrated previously that Pax-6, a paired domain (PD)/homeodomain (HD) transcription factor critical for eye development, contributes to the activation of the αB-, αA-, δ1-, and ζ-crystallin genes in the lens. Here we have examined the possibility that the inverse relationship between the expression of Pax-6 and β-crystallin genes within the developing chicken lens reflects a negative regulatory role of Pax-6. Cotransfection of a plasmid containing the βB1-crystallin promoter fused to the chloramphenicol acetyltransferase reporter gene and a plasmid containing the full-length mouse Pax-6 coding sequences into primary embryonic chicken lens epithelial cells or fibroblasts repressed the activity of this promoter by as much as 90%. Pax-6 constructs lacking the C-terminal activation domain repressed βB1-crystallin promoter activity as effectively as the full-length protein, but the PD alone or Pax-6 (5a), a splice variant with an altered PD affecting its DNA binding specificity, did not. DNase footprinting analysis revealed that truncated Pax-6 (PD+HD) binds to three regions (−183 to −152, −120 to −48, and −30 to +1) of the βB1-crystallin promoter. Earlier experiments showed that the βB1-crystallin promoter sequence from −120 to −48 contains a cis element (PL2 at −90 to −76) that stimulates the activity of a heterologous promoter in lens cells but not in fibroblasts. In the present study, we show by electrophoretic mobility shift assay and cotransfection that Pax-6 binds to PL2 and represses its ability to activate promoter activity; moreover, mutation of PL2 eliminated binding by Pax-6. Taken together, our data indicate that Pax-6 (via its PD and HD) represses the βB1-crystallin promoter by direct interaction with the PL2 element. We thus suggest that the relatively high concentration of Pax-6 contributes to the absence of βB1-crystallin gene expression in lens epithelial cells and that diminishing amounts of Pax-6 in lens fiber cells during development allow activation of this gene.

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26

CRAGHILL, Jane, Andrew D. CRONSHAW, and John J. HARDING. "The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens." Biochemical Journal 379, no. 3 (May 1, 2004): 595–600. http://dx.doi.org/10.1042/bj20031367.

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The glutathionylation of human lens proteins was examined by Western-blot analysis with an anti-GSH antibody and scanning. Several different glutathionylated proteins were observed, and a 47 kDa band was of particular interest. This band did not appear after SDS/PAGE under reducing conditions, suggesting that it was a glutathionylated fraction. The 47 kDa band was found principally in the outer part of the lens, the cortex, but not in the lens nucleus where older proteins are present. The 47 kDa component was composed of βB1-, βB2- and γS-crystallin, with the γS-crystallin having glutathione bound at Cys-82 and at Cys-22, Cys-24 or Cys-26. We conclude that when glutathione becomes bound to γS-crystallin, it causes it to bind in turn to the β-crystallin polypeptides to form a dimer.

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27

Kretschmar, M., E. M. Mayr, and R. Jaenicke. "Homo-Dimeric Spherulin 3a: A Single-Domain Member of the bg-Crystallin Superfamily." Biological Chemistry 380, no. 1 (January 4, 1999): 89–94. http://dx.doi.org/10.1515/bc.1999.012.

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Abstract The βγ-crystallin superfamily of eye lens proteins comprises a class of structurally related members with a wide variety of different functions. Common features of these proteins are 1. the Greek-key motif of antiparallel β-sheets, called the crystallin fold, and 2. the high intrinsic long-term stability. Spherulin 3a (S3a), a dormant protein from the spherules of Physarum polycephalum, is the only known single-domain protein within the βγ-crystallin family. Based on sequence homology and ‘domain swapping’, it has been proposed to represent an evolutionary ancestor of present-day eye lens crystallins. Since S3a is highly expressed in spherulating plasmodia of P. polycephalum under a variety of stress conditions, it can be assumed that the protein may serve as a compatible solute in the cytosol of the slime mold. In order to investigate the stability and other physicochemical properties of a single-domain all-β protein, we isolated natural S3a. For the large-scale purification, the recombinant protein was cloned and expressed in Escherichia coli. The detailed spectral and biochemical analysis proved the recombinant protein to be authentic. In its native form, S3a is dimeric. Due to its exposed cysteine residues (Cys4), in the absence of reducing agents intermolecular disulfide cross-linking leads to the formation of higher oligomers. In order to preserve the native quaternary structure without aggregation artifacts in denaturation/renaturation experiments, the Cys4→Ser mutant (S3a C4S) was produced. Both the wild-type protein and its mutant are indistinguishable in their physicochemical properties. At pH 3–4, both proteins form a stable compact intermediate (A-state). Concentration-dependent thermal and chemical denaturation showed that the equilibrium unfolding of S3a obeys the simple two-state model with no significant occurrence of folding intermediates.

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28

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.

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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)] 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.

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29

Chiou, Shyh-Horng, Fu-Ming Pan, Hsuan-Wan Peng, Yen-Kai Chao, and Wen-Chang Chang. "Characterization of γS-Crystallin Isoforms from a Catfish: Evolutionary Comparison of Various γ-, γS-, and β-Crystallins." Biochemical and Biophysical Research Communications 252, no. 2 (November 1998): 412–19. http://dx.doi.org/10.1006/bbrc.1998.9657.

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30

Macdonald, James T., Andrew G. Purkiss, Myron A. Smith, Paul Evans, Julia M. Goodfellow, and Christine Slingsby. "Unfolding crystallins: The destabilizing role of a β-hairpin cysteine in βB2-crystallin by simulation and experiment." Protein Science 14, no. 5 (May 2005): 1282–92. http://dx.doi.org/10.1110/ps.041227805.

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31

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.

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Coop, Audrey, Kirsten E. H. Wiesmann, and M. James C. Crabbe. "Translocation of β crystallin in neural cells in response to stress." FEBS Letters 431, no. 3 (July 24, 1998): 319–21. http://dx.doi.org/10.1016/s0014-5793(98)00783-2.

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33

Bateman, O. A., R. Sarra, S. T. van Genesen, G. Kappé, N. H. Lubsen, and C. Slingsby. "The stability of human acidic β-crystallin oligomers and hetero-oligomers." Experimental Eye Research 77, no. 4 (October 2003): 409–22. http://dx.doi.org/10.1016/s0014-4835(03)00173-8.

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34

Liedtke, Thomas, Jens Christian Schwamborn, Uwe Schröer, and Solon Thanos. "Elongation of Axons during Regeneration Involves Retinal Crystallin β b2 (crybb2)." Molecular & Cellular Proteomics 6, no. 5 (January 29, 2007): 895–907. http://dx.doi.org/10.1074/mcp.m600245-mcp200.

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35

Wang, Kai Jie. "Novel β-Crystallin Gene Mutations in Chinese Families With Nuclear Cataracts." Archives of Ophthalmology 129, no. 3 (March 1, 2011): 337. http://dx.doi.org/10.1001/archophthalmol.2011.11.

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36

Srinivas, P. N. B. S., P. Yadagiri Reddy, and G. Bhanuprakash Reddy. "Significance of α-crystallin heteropolymer with a 3:1 αA/αB ratio: chaperone-like activity, structure and hydrophobicity." Biochemical Journal 414, no. 3 (August 27, 2008): 453–60. http://dx.doi.org/10.1042/bj20080544.

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Abstract:

The small heat-shock protein α-crystallin isolated from the eye lens exists as a large (700 kDa) heteropolymer composed of two subunits, αA and αB, of 20 kDa each. Although trace amounts of αA-crystallin are found in other tissues, non-lenticular distribution of α-crystallin is dominated by the αB homopolymer. In most vertebrate lens, the molar ratio of αA to αB is generally 3:1. However, the importance of this ratio in the eye lens is not known. In the present study, we have investigated the physiological significance of the 3:1 ratio by determining the secondary/tertiary structure, hydrophobicity and chaperone-like activity of αA- and αB-homopolymers and heteropolymers with different ratios of αA to αB subunits. Although, under physiologically relevant conditions, the αB-homopolymer (37–40 °C) has shown relatively higher activity, the αA-homopolymer or the heteropolymer with a higher αA proportion (3:1 ratio) has shown greater chaperone-like activity at elevated temperatures (>50 °C) and also upon structural perturbation. Furthermore, higher chaperone activity at elevated temperatures as well as upon structural perturbation is mainly mediated through increased hydrophobicity of αA. Although homopolymers and heteropolymers of α-crystallin did not differ in their secondary structure, changes in tertiary structure due to structural perturbations upon pre-heating are mediated predominantly by αA. Interestingly, the heteropolymer with higher αA proportion (3:1) or the αA-homopolymer seems to be better chaperones in protecting lens β- and γ-crystallins at both normal and elevated temperatures. Thus lens might have favoured a combination of these qualities to achieve optimal protection under both native and stress (perturbed) conditions for which the heteropolymer with αA to αB in the 3:1 ratio appears to be better suited.

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Pan, Fu-Ming, Ming-Hong Chuang, and Shyh-Horng Chiou. "Characterization of γS-Crystallin Isoforms from Lip Shark (Chiloscyllium colax): Evolutionary Comparison between γS and β/γ Crystallins." Biochemical and Biophysical Research Communications 240, no. 1 (November 1997): 51–56. http://dx.doi.org/10.1006/bbrc.1997.7600.

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38

Kenworthy, Anne K., Alan D. Magid, Timothy N. Oliver, and Thomas J. McIntosh. "Colloid Osmotic Pressure of Steer and β-Crystallins: Possible Functional Roles for Lens Crystallin Distribution and Structural Diversity." Experimental Eye Research 59, no. 1 (July 1994): 11–30. http://dx.doi.org/10.1006/exer.1994.1077.

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39

David, Larry L., Jay W. Wright, and Thomas R. Shearer. "Calpain II induced insolubilization of lens β-crystallin polypeptides may induce cataract." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1139, no. 3 (July 1992): 210–16. http://dx.doi.org/10.1016/0925-4439(92)90136-b.

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40

Ghosh, Joy G., Denise Fabian, Ashley Mallat, Steve Ramirez, Mark Burton, Juliet Moncaster, Noel Casey, et al. "P2-145: The molecular chaperone human Aβ crystallin modulates amyloid-β neurotoxicity." Alzheimer's & Dementia 5, no. 4S_Part_10 (July 2009): P304. http://dx.doi.org/10.1016/j.jalz.2009.04.456.

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41

Cheeseman, Kevin H., Milfred Seccia, Olga Brossa, Trevor Slater, and Enrico Gravela. "Modification of β-crystallin by free radicals predisposes it to transglutaminase activity." Free Radical Biology and Medicine 9 (January 1990): 83. http://dx.doi.org/10.1016/0891-5849(90)90464-t.

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42

Herzog, Rebecca, Juan Manuel Sacnun, Guadalupe González-Mateo, Maria Bartosova, Katarzyna Bialas, Anja Wagner, Markus Unterwurzacher, et al. "Lithium preserves peritoneal membrane integrity by suppressing mesothelial cell αB-crystallin." Science Translational Medicine 13, no. 608 (August 25, 2021): eaaz9705. http://dx.doi.org/10.1126/scitranslmed.aaz9705.

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Abstract:

Life-saving renal replacement therapy by peritoneal dialysis (PD) is limited in use and duration by progressive impairment of peritoneal membrane integrity and homeostasis. Preservation of peritoneal membrane integrity during chronic PD remains an urgent but long unmet medical need. PD therapy failure results from peritoneal fibrosis and angiogenesis caused by hypertonic PD fluid (PDF)–induced mesothelial cytotoxicity. However, the pathophysiological mechanisms involved are incompletely understood, limiting identification of therapeutic targets. We report that addition of lithium chloride (LiCl) to PDF is a translatable intervention to counteract PDF-induced mesothelial cell death, peritoneal membrane fibrosis, and angiogenesis. LiCl improved mesothelial cell survival in a dose-dependent manner. Combined transcriptomic and proteomic characterization of icodextrin-based PDF-induced mesothelial cell injury identified αB-crystallin as the mesothelial cell protein most consistently counter-regulated by LiCl. In vitro and in vivo overexpression of αB-crystallin triggered a fibrotic phenotype and PDF-like up-regulation of vascular endothelial growth factor (VEGF), CD31-positive cells, and TGF-β–independent activation of TGF-β–regulated targets. In contrast, αB-crystallin knockdown decreased VEGF expression and early mesothelial-to-mesenchymal transition. LiCl reduced VEGF release and counteracted fibrosis- and angiogenesis-associated processes. αB-crystallin in patient-derived mesothelial cells was specifically up-regulated in response to PDF and increased in peritoneal mesothelial cells from biopsies from pediatric patients undergoing PD, correlating with markers of angiogenesis and fibrosis. LiCl-supplemented PDF promoted morphological preservation of mesothelial cells and the submesothelial zone in a mouse model of chronic PD. Thus, repurposing LiCl as a cytoprotective PDF additive may offer a translatable therapeutic strategy to combat peritoneal membrane deterioration during PD therapy.

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43

Aarts, Henk J. M., Johan T. Den Dunnen, Nicolette H. Lubsen, and John G. G. Schoenmakers. "Linkage between the βB2 and βB3 crystallin genes in man and rat: a remnant of an ancient β-crystallin gene cluster." Gene 59, no. 1 (January 1987): 127–35. http://dx.doi.org/10.1016/0378-1119(87)90273-3.

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44

Bruggink, Kim, H. Bea Kuiperij, Marcel M. Verbeek, and Wilbert Boelens. "P1-067: Complexes of amyloid β and Amyloid-β-crystallin as potential biomarkers for early stage Alzheimer's disease." Alzheimer's & Dementia 7 (July 2011): S131. http://dx.doi.org/10.1016/j.jalz.2011.05.346.

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45

Lubsen, N. H., H. J. M. Aarts, and J. G. G. Schoenmakers. "The evolution of lenticular proteins: The β- and γ-crystallin super gene family." Progress in Biophysics and Molecular Biology 51, no. 1 (January 1988): 47–76. http://dx.doi.org/10.1016/0079-6107(88)90010-7.

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46

Trivedi, Vishwa D., Bakthisaran Raman, Tangirala Ramakrishna, and Ch Mohan Rao. "Detection and assay of proteases using calf lens β-crystallin aggregate as substrate." Journal of Biochemical and Biophysical Methods 40, no. 1-2 (July 1999): 49–55. http://dx.doi.org/10.1016/s0165-022x(99)00021-4.

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47

BERBERS, Guy A. M., Otto C. BOERMAN, Hans BLOEMENDAL, and Wilfried W. JONG. "Primary Gene Products of Bovine β-Crystallin and Reassociation Behavior of Its Aggregates." European Journal of Biochemistry 128, no. 2-3 (March 3, 2005): 495–502. http://dx.doi.org/10.1111/j.1432-1033.1982.tb06992.x.

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48

Trifonova, N. "Anti-α, anti-β, and anti-γ-crystallin autoantibodies from patients with cataract." Vision Research 35, no. 1 (October 1995): S193. http://dx.doi.org/10.1016/0042-6989(95)98743-s.

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49

Lowe, James, Michael Landon, Ian Pike, Ian Spendlove, Helen Mcdermott, and R. John Mayer. "Dementia with β-amyloid deposition: involvement of αB-crystallin supports two main diseases." Lancet 336, no. 8713 (August 1990): 515–16. http://dx.doi.org/10.1016/0140-6736(90)92075-s.

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50

Slingsby, C., and O. A. Bateman. "Rapid separation of bovine β-crystallin subunits βB1, βB2, βB3, βA3 and βA4." Experimental Eye Research 51, no. 1 (July 1990): 21–26. http://dx.doi.org/10.1016/0014-4835(90)90165-q.

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