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Full-Text Articles in Social and Behavioral Sciences
Truncation, Cross-Linking And Interaction Of Crystallins And Intermediate Filament Proteins In The Aging Human Lens, Roger Truscott, Jason Mcarthur, Andrew Aquilina, Shi-Ping (Jim) Su
Truncation, Cross-Linking And Interaction Of Crystallins And Intermediate Filament Proteins In The Aging Human Lens, Roger Truscott, Jason Mcarthur, Andrew Aquilina, Shi-Ping (Jim) Su
J. A. Aquilina
The optical properties of the lens are dependent upon the integrity of proteins within the fiber cells. During aging, crystallins, the major intra-cellular structural proteins of the lens, aggregate and become water-insoluble. Modifications to crystallins and the lens intermediate filaments have been implicated in this phenomenon. In this study, we examined changes to, and interactions between, human lens crystallins and intermediate filament proteins in lenses from a variety of age groups (0-86 years). Among the lens-specific intermediate filament proteins, filensin was extensively cleaved in all postnatal lenses, with truncated products of various sizes being found in both the lens cortical …
Chemical Cross-Linking Of The Chloroplast Localized Small Heat-Shock Protein, Hsp21, And The Model Substrate Citrate Synthase, Emma Ahrman, W Lambert, Andrew Aquilina, C V Robinson, Cs Emanuelsson
Chemical Cross-Linking Of The Chloroplast Localized Small Heat-Shock Protein, Hsp21, And The Model Substrate Citrate Synthase, Emma Ahrman, W Lambert, Andrew Aquilina, C V Robinson, Cs Emanuelsson
J. A. Aquilina
The molecular mechanism whereby the small heat-shock protein (sHsp) chaperones interact with and prevent aggregation of other proteins is not fully understood. We have characterized the sHsp-substrate protein interaction at normal and increased temperatures utilizing a model substrate protein, citrate synthase (CS), widely used in chaperone assays, and a dodecameric plant sHsp, Hsp21, by chemical cross-linking with 3,3'-Dithiobis[sulfosuccinimidylpropionate] (DTSSP) and mass spectrometric peptide mapping. In the absence of CS, the cross-linker captured Hsp21 in dodecameric form, even at increased temperature (47 degrees C). In the presence of equimolar amounts of CS, no Hsp21 dodecamer was captured, indicating a substrate-induced Hsp21 …