Cataract incidence and analysis of lens crystallins in the water-, urea- and SDS-soluble fractions of Emory mice fed a diet restricted by 40% in calories.

Restriction of dietary calorie intake is associated with life extension and with the delay of age-related disorders. Preliminary studies demonstrated that by feeding the Emory mouse a diet restricted by 21% in calories cataract and insolubilization of protein could also be delayed. To observe the effects of calorie restriction over prolonged portions of adulthood, Emory mice were fed the control diet (C) or a diet restricted by 40% in calories (R). Feeding the R diet was associated with delayed formation or progress of cataract over virtually the entire second half of life. At 11 months of age, bilateral grade 5 cataracts were present in 17% and 2% of C and R lenses, respectively. At 22 months of age, bilateral grade 5 cataracts were present in 90% and 18% of C and R lenses, respectively. The distribution of alpha-, beta-, and gamma- crystallins in the water-soluble, urea-soluble, and SDS-soluble fractions indicates more similarities than differences between C and R lenses with a specific grade of cataract or of a given age. However, there were significant and abrupt (after grade 4 cataract) losses of particular gamma-crystallins; gamma-crystallins which were not prominent at earlier stages became the major gamma-crystallin moieties. Losses of alpha-crystallins were also noted upon cataract formation or aging in most of the fractions. Aggregates including gamma- and alpha-crystallins also accumulate faster in the C group.

[1]  S. Lerman,et al.  Studies on the structural proteins of the human lens. , 1969, Experimental eye research.

[2]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[3]  M. BradfordM たんぱく質‐色素結合の原理を用いるμg量のたんぱく質の定量のための迅速,高感度法 , 1976 .

[4]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[5]  Howard M. Goodman,et al.  High resolution two-dimensional electrophoresis of basic as well as acidic proteins , 1977, Cell.

[6]  A. Spector,et al.  Human insoluble lens protein. I. Separation and partial characterization of polypeptides. , 1978, Experimental eye research.

[7]  J. Piatigorsky,et al.  Differential metabolism and leakage of protein in an inherited cataract and a normal lens cultured with ouabain , 1978, Nature.

[8]  H. Towbin,et al.  Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[9]  J. Bours Species specificity of the crystallins and the albuminoid of the ageing lens , 1980 .

[10]  Propagation failure of antidromic action potentials in crab motor neurons , 1980 .

[11]  J. Piatigorsky,et al.  Differential synthesis and degradation of protein in the hereditary Philly mouse cataract. , 1980, Experimental eye research.

[12]  J. Kuck,et al.  The Emory mouse cataract: an animal model for human senile cataract. , 1981, Current eye research.

[13]  B. Stollar,et al.  Serological detection of homologies of H1o with H5 and H1 histones. , 1981, The Journal of biological chemistry.

[14]  R. Gold,et al.  Comparative two-dimensional electrophoretic analysis of water soluble proteins from bovine and murine lenses. , 1982, Experimental eye research.

[15]  H. Bloemendal,et al.  Effect of aging on the water-soluble and water-insoluble protein pattern in normal human lens. , 1982, Experimental eye research.

[16]  O. Hockwin,et al.  Biochemistry of the ageing rat lens. II. Isoelectric focusing of water-soluble crystallins. , 1983, Ophthalmic research.

[17]  R. Siezen,et al.  Physicochemical characterization of high-molecular-weight alpha-crystallin subpopulations from the calf lens nucleus. , 1983, Biochimica et biophysica acta.

[18]  J. Kuck,et al.  The Emory mouse cataract: Changes in the β and γ-crystallins during aging and cataractogenesis as revealed by isoelectric focusing of the native soluble proteins , 1984 .

[19]  R. Weindruch,et al.  Dietary restriction retards age-related loss of gamma crystallins in the mouse lens. , 1984, Science.

[20]  M. Crabbe,et al.  Chapter 3 – The Lens: Development, Proteins, Metabolism and Cataract , 1984 .

[21]  J. Piatigorsky,et al.  Selective loss of a family of gene transcripts in a hereditary murine cataract. , 1985, Science.

[22]  J. Sredy,et al.  cAMP-dependent phosphorylation of bovine lens alpha-crystallin. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[23]  T. Shearer,et al.  Origin of urea-soluble protein in the selenite cataract. Role of beta-crystallin proteolysis and calpain II. , 1987, Investigative ophthalmology & visual science.

[24]  E. Abraham,et al.  Lens protein composition, glycation and high molecular weight aggregation in aging rats. , 1987, Investigative ophthalmology & visual science.

[25]  L. Takemoto,et al.  Immunochemical characterization of the major low molecular weight polypeptide (10K) from human cataractous lenses. , 1989, Experimental eye research.

[26]  G E Dallal,et al.  Moderate caloric restriction delays cataract formation in the Emory mouse , 1989, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[27]  The fate of γL crystallins in rat lens during diabetic cataractogenesis as determined by a monoclonal antibody. , 1989, Current eye research.

[28]  C. R. Middaugh,et al.  Inhibition of alpha-crystallin aggregation by gamma-crystallin. , 1990, The Journal of biological chemistry.

[29]  J. Zigler Animal models for the study of maturity-onset and hereditary cataract. , 1990, Experimental eye research.

[30]  J. Kuck Late onset hereditary cataract of the emory mouse. A model for human senile cataract. , 1990, Experimental eye research.

[31]  R. Augusteyn,et al.  On the composition and origin of the urea-soluble polypeptides of the U18666A cataract. , 1990, Current eye research.

[32]  Walford Rl The clinical promise of diet restriction. , 1990 .

[33]  J. Blumberg,et al.  Dietary energy restriction decreases ex vivo spleen prostaglandin E2 synthesis in Emory mice. , 1990, The Journal of nutrition.

[34]  P. Russell,et al.  Interaction of an altered beta-crystallin with other proteins in the Philly mouse lens. , 1990, Experimental eye research.

[35]  A. Kamei Characterization of water-insoluble proteins in normal and cataractous human lens. , 1990, Japanese journal of ophthalmology.

[36]  R. Weindruch,et al.  Influences of dietary restriction on immunity to influenza in aged mice. , 1991, Journal of gerontology.

[37]  R. Schäfer,et al.  Alpha B-crystallin is a small heat shock protein. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[38]  R. Bronson,et al.  Reduction in rate of occurrence of age related lesions in dietary restricted laboratory mice. , 1991, Growth, development, and aging : GDA.

[39]  R. Walford,et al.  The calorically restricted low-fat nutrient-dense diet in Biosphere 2 significantly lowers blood glucose, total leukocyte count, cholesterol, and blood pressure in humans. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[40]  B. Ames,et al.  Protein oxidation associated with aging is reduced by dietary restriction of protein or calories. , 1992, Proceedings of the National Academy of Sciences of the United States of America.