Regular articleMolecular Evidence for the Involvement of Alpha Crystallin in the Colouration/Crosslinking of Crystallins in Age-related Nuclear Cataract☆
References (26)
- Bleasby, A. J. Wootton, J. C. 1990, Construction of validated, non-redundant composite protein sequence database....
- Carver, J. A. Aquilina, J. A. Cooper, P. G. Williams, G. A. Truscott, R. J. W. 1994, α-Crystallin: molecular chaperone...
- David, L. L. Lampi, K. J. Lund, A. L. Smith, J. B. 1996, The sequence human βB1-crystallin cDNA allows mass...
- Dilley, K. J. Pirie, A. 1974, Changes to the proteins of the human lens nucleus in cataract. Exp. Eye Res. 19, 59,...
- Dillon, J. Garcia Castineiras, S. Santiago, M. A. Spector, A. 1984, The endopeptidase-resistant protein fraction from...
- Eng, J. K. McCormack, A. L. Yates, J. R. 1994, An approach to correlate tandem mass spectral data of peptides with...
- Garner, M. H. Spector, A. 1980, Selective oxidation of cysteine and methionine in normal and senile cataractous lenses....
- Harding, J. J. 1991, Cataract biochemistry and epidemiology and pharmacology. Chapman & Hall,...
- Harding, J. J. Crabbe, M. J. C. 1984, The lens: development, proteins, metabolism and cataract. The Eye: Vegetative...
- Horwitz, J. 1992, α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U.S.A. 89, 10449,...
Cited by (28)
Tools to fight the cataract epidemic: A review of experimental animal models that mimic age related nuclear cataract
2016, Experimental Eye ResearchCitation Excerpt :In more advanced stages of ARN cataract, proteins may still remain insoluble after treatment with urea/reducing agents (Truscott and Augusteyn, 1977a). The major component of the urea insoluble fraction from cataract lenses is α-crystallin (Chen et al., 1997). In addition to its structural role, α-crystallin also acts as a molecular chaperone preventing the aggregation and/or inactivation of lens proteins (Horwitz, 1992, 2003; Harding, 2002; Horwitz, 2003; Bloemendal et al., 2004).
Identification of kynoxazine, a novel fluorescent product of the reaction between 3-hydroxykynurenine and erythrulose in the human lens, and its role in protein modification
2016, Journal of Biological ChemistryCitation Excerpt :Covalent cross-linking of proteins occurs in aging lenses and strongly affects light scattering in age-related cataracts (1).
UVA light-excited kynurenines oxidize ascorbate and modify lens proteins through the formation of advanced glycation end products: Implications for human lens aging and cataract formation
2014, Journal of Biological ChemistryCitation Excerpt :Human lens proteins undergo numerous chemical changes with age, and this process is accelerated in cataractogenesis (1–3).
Chaperone-independent mitochondrial translocation and protection by αB-crystallin in RPE cells
2013, Experimental Eye ResearchCitation Excerpt :It is mainly found in the eye lens, retina, heart and neural tissues (Bhat and Nagineni, 1989; Dubin et al., 1989). Altered expression and/or accumulation of αB-crystallin are associated with the etiology of many diseases including mammary metaplastic carcinoma (Chan et al., 2011), hepatocellular carcinoma (Tang et al., 2009), and renal cell carcinoma (Shi et al., 2004), age-related macular degeneration (Nakata et al., 2005; Alge et al., 2002; De et al., 2007), age-related cataract (Chen et al., 1997; Truscott et al., 1998), Parkinson's disease (Braak et al., 2001), Alexander disease (Iwaki et al., 1989), Lewy body disease (Dabir et al., 2004), Alzheimer disease (Renkawek et al., 1994), Creutzfeldt–Jakob disease (Renkawek et al., 1992), multiple sclerosis (Ousman et al., 2007), congestive heart failure (Dohke et al., 2006) and Huntington's disease (Iwaki et al., 1992; Zabel et al., 2002; Dabir et al., 2004). αB-crystallin protects multiple cell types against a variety of environmental stresses.
αb-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cells
2012, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :It has also been shown to protect tissues against peroxide-induced damage [18], UV-light damage [38] and damage due to ischemic-reperfusion damage [47]. The importance of αB-crystallin/sHSP for oxidative stress defense is underscored by its highly altered expression patterns in a multitude of oxidative stress-associated diseases including Parkinson's disease [48], Alexander's Brain disease [49], Lewy Body disease [50,51], Alzheimer's disease [52,50], Huntington's disease [53], Creutzfeldt–Jakob disease [54], Desmin-related myopathy [29], age-related macular degeneration [16,55,56], and age-related cataract [57,58]. Despite its ability to confer oxidative stress protection to cells the cellular targets and functions protected by αB-crystallin/sHSP under oxidative stress conditions have not been entirely established.
Conformational diseases: Looking into the eyes
2010, Brain Research BulletinCitation Excerpt :Cataract is opacity of the lens due to the accumulation of insoluble proteins that obstructs the passage of light through the lens, thereby blocking light from reaching the photoreceptors in the retina. A major component of this insoluble protein is α-crystallin and βγ-crystallins [18]. Cataracts removed from the human eye lens are composed of different species of aggregated crystallins.
- ☆
Davson, H.
- f1
Address for correspondence: Roger J. W. Truscott, Australian Cataract Research Foundation, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia.