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Full-Text Articles in Social and Behavioral Sciences
Subunit Exchange Of Polydisperse Proteins: Mass Spectrometry Reveals Consequences Of Αa-Crystallin Truncation, J. Andrew Aquilina, Justin Benesch, Lin Lin Ding, Orna Yaron, Joseph Horwitz, Carol Robinson
Subunit Exchange Of Polydisperse Proteins: Mass Spectrometry Reveals Consequences Of Αa-Crystallin Truncation, J. Andrew Aquilina, Justin Benesch, Lin Lin Ding, Orna Yaron, Joseph Horwitz, Carol Robinson
J. A. Aquilina
The small heat shock protein, α-crystallin, plays a key role in maintaining lens transparency by chaperoning structurally compromised proteins. This is of particular importance in the human lens, where proteins are exposed to post-translational modifications over the life-time of an individual. Here, we examine the structural and functional consequences of one particular modification of αA-crystallin involving the truncation of 5 C-terminal residues (αA1–168). Using novel mass spectrometry approaches and established biophysical techniques, we show that αA1–168 forms oligomeric assemblies with a lower average molecular mass than wild-type αA-crystallin (αAWT). Also apparent from the mass spectra of both αAWT and αA1–168 …
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 …