caa a22 4500 463185404 CHVBK 20180406164851.0 cr unu---uuuuu 170326e20070101xx s 000 0 eng 10.1007/s00726-006-0303-4 doi (NATIONALLICENCE)springer-10.1007/s00726-006-0303-4 Age-related changes of alpha-crystallin aggregate in human lens [Elektronische Daten] [N. Fujii, Y. Shimmyo, M. Sakai, Y. Sadakane, T. Nakamura, Y. Morimoto, T. Kinouchi, Y. Goto, K. Lampi] Summary.: Lens alpha-crystallin, composed of two subunits alpha A- and alpha B-crystallin, forms large aggregates in the lens of the eye. The present study investigated the aggregate of human lens alpha-crystallin from elderly and young donors. Recombinant alpha A- and alpha B-crystallins in molar ratios of alpha A to alpha B at 1:1, corresponding to the aged sample, were also studied in detail. We found by ultra-centrifugation analysis that the alpha-crystallin aggregate from elderly donors was large and heterogeneous with an average sedimentation coefficient of 30 S and a range of 20-60 S at 37 °C. This was higher compared to the young samples that had an average sedimentation coefficient of 17 S. The sedimentation coefficients of recombinant alpha A- and alpha B-crystallins were approximately 12 S and 15 S, respectively. Even when recombinant alpha-crystallins were mixed in molar ratios equivalent to those found in vivo, similar S values as the native aged alpha-crystallin aggregates were not obtained. Changes in the self-association of alpha-crystallin aggregate were correlated to changes in chaperone activity. Alpha-crystallin from young donors, and recombinant alpha A- and alpha B-crystallin and their mixtures showed chaperone activity, which was markedly lost in samples from the aged alpha-crystallin aggregates. Springer-Verlag, 2006 Keywords: Aging - Aggregation - Analytical ultracentrifugation - Lens alpha-crystallin nationallicence Fujii N. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut Shimmyo Y. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut Sakai M. Institute for Protein Research, Osaka University, Osaka, Japan aut Sadakane Y. Kyushu University of Health and Welfare, Miyazaki, Japan aut Nakamura T. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut Morimoto Y. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut Kinouchi T. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut Goto Y. Institute for Protein Research, Osaka University, Osaka, Japan aut Lampi K. Oregon Health & Science University, Portland, Oregon, U.S.A. aut Amino Acids Springer-Verlag 32/1(2007-01-01), 87-94 0939-4451 32:1<87 2007 32 726 https://doi.org/10.1007/s00726-006-0303-4 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-006-0303-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Fujii N. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut NATIONALLICENCE 700 1- Shimmyo Y. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut NATIONALLICENCE 700 1- Sakai M. Institute for Protein Research, Osaka University, Osaka, Japan aut NATIONALLICENCE 700 1- Sadakane Y. Kyushu University of Health and Welfare, Miyazaki, Japan aut NATIONALLICENCE 700 1- Nakamura T. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut NATIONALLICENCE 700 1- Morimoto Y. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut NATIONALLICENCE 700 1- Kinouchi T. Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka, Japan aut NATIONALLICENCE 700 1- Goto Y. Institute for Protein Research, Osaka University, Osaka, Japan aut NATIONALLICENCE 700 1- Lampi K. Oregon Health & Science University, Portland, Oregon, U.S.A aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 32/1(2007-01-01), 87-94 0939-4451 32:1<87 2007 32 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer