Calcium-induced aggregation of the urea-deaggregated human lens insoluble protein. 1990

K Satoh, and H Adachi, and S Yamashita, and H Hirano, and P Yasin, and Y Ueda
Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, Noda, Japan.

Calcium-induced aggregation of the urea-deaggregated insoluble protein (US-fraction) derived from human lens was investigated by use of a simple light scattering method. The initial rate of aggregation was shown to increase with progress of senescence of the lens, and to be much higher in the nucleus as compared to the cortex. The aggregation was found to be more active in the US-fraction from cataractous lens than in that of normal lens at same age. A calcium sensitive polypeptide (CSP) was isolated from the US-fraction from cataractous human lenses by gel filtration followed by DEAE-cellulose column chromatography in the presence of 7 M urea. The molecular size of the CSP in the dissociated state was assessed to be 4.2 kDa by urea-SDS-PAGE, and the size in the associated state to be 450 kDa by thin layer gel filtration. With addition of calcium ion to the latter, it aggregates rapidly to form much larger aggregates and eventually precipitates out. The aggregation rate of the CSP is shown to increase exponentially with an increase in the concentration of both CSP and calcium ion, indicating the involvement of complicated mechanisms in the aggregation process. Effects of divalent ions other than calcium ion on the aggregation process were also examined. It is revealed that the effect of manganese ion is little less than that of calcium ion, whereas magnesium and strontium ions are much less effective as compared to the former two ions.

UI MeSH Term Description Entries
D007908 Lens, Crystalline A transparent, biconvex structure of the EYE, enclosed in a capsule and situated behind the IRIS and in front of the vitreous humor (VITREOUS BODY). It is slightly overlapped at its margin by the ciliary processes. Adaptation by the CILIARY BODY is crucial for OCULAR ACCOMMODATION. Eye Lens,Lens, Eye,Crystalline Lens
D002122 Calcium Chloride A salt used to replenish calcium levels, as an acid-producing diuretic, and as an antidote for magnesium poisoning. Calcium Chloride Dihydrate,Calcium Chloride, Anhydrous
D003459 Crystallins A heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. The presence of these proteins accounts for the transparency of the lens. The family is composed of four major groups, alpha, beta, gamma, and delta, and several minor groups, which are classed on the basis of size, charge, immunological properties, and vertebrate source. Alpha, beta, and delta crystallins occur in avian and reptilian lenses, while alpha, beta, and gamma crystallins occur in all other lenses. Lens Proteins,Crystallin,Eye Lens Protein,Lens Protein, Eye,Protein, Eye Lens,Proteins, Lens
D005136 Eye Proteins PROTEINS derived from TISSUES of the EYE. Proteins, Eye
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012995 Solubility The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Solubilities
D014508 Urea A compound formed in the liver from ammonia produced by the deamination of amino acids. It is the principal end product of protein catabolism and constitutes about one half of the total urinary solids. Basodexan,Carbamide,Carmol
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

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