Abstract：
:Alpha-crystallin high-molecular-weight (HMW) aggregates can be formed in vitro by many mechanisms, but the mechanism of in vivo aggregation has not been clearly established. HMW and LMW (low-molecular-weight) alpha-crystallins were isolated from human lenses 50-60 years of age and some spectroscopic measurements were performed. Conformational differences were suggested based on data of increased bis-ANS (4,4'-dianilino-1,1'-binaphthalene-5, 5'-disulfonic acid) and ThT (thioflavin T) fluorescence as well as increased far-UV and decreased near-UV circular dichroism (CD). These results indicated that HMW alpha-crystallin was more hydrophobic than LMW alpha-crystallin, possibly resulting from partial unfolding of alpha-crystallin. On the other hand, the increased ThT fluorescence and far-UV CD intensities indicate that an increased amount of beta-sheet conformation was involved in aggregation. These data, along with little difference in chaperone-like activity between the LMW and HMW alpha-crystallins, strongly suggest that HMW alpha-crystallin aggregates resulted from partial unfolding and disassembling-reassembling of LMW alpha-crystallin caused by posttranslational modification rather than chaperone complex formation.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Liang JJ,Akhtar NJdoi
10.1006/bbrc.2000.3306subject
Has Abstractpub_date
2000-08-28 00:00:00pages
354-9issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(00)93306-0journal_volume
275pub_type
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