Project Details
Description
Alpha crystallin, alpha, is a major protein of the lens contributing to
the transparency of the organ by its known structural and putative
chaperone like characteristics. It is known that alpha is phosphorylated
to a significant extent on both of its subunits alphaA and alphaB. Since
phosphorylation required a considerable amount of energy, it is apparent
that these are important reactions. My work has shown that with oxidative
stress, phosphorylation of alpha is significantly increased. However, it
is clear that phosphorylation does not effect the known chaperone activity
of alpha or significantly change its physical structure. Therefore, the
objective of this grant is to define the biological roles of
phosphorylation of alphaA and alphaB, especially its possible contribution
to the prevention of the development of maturity onset cataract. The
effect of a variety of stresses, which are believed to contribute to the
development of cataract, on the phosphorylation of alphaA and alphaB in
rat lenses in normal and transfected lens epithelial cells will be studied
to determine the function of phosphorylation of alphaA and alphaB. The
distribution of alphaA or alphaB within the cell will be examined before
and after such stresses to determine changes in cellular localization and
binding sites of the alpha macromolecule. The sites of the oxidative
stress-induced phosphorylation will also be determined. The binding of
phosphorylated and nonphosphorylated alphaA and alphaB to a variety of
biomolecules and cell structures will be studied to determine whether
alpha is involved in reactions with cell matrix modeling plasma membrane,
nuclear membrane structure, and proteolytic pathways. This work is a
logical extension of my previous studies. The project should
significantly increase our understanding of alpha-crystallin function.
Status | Finished |
---|---|
Effective start/end date | 6/1/96 → 5/31/01 |
Funding
- National Eye Institute: US$126,232.00
ASJC Scopus Subject Areas
- Ophthalmology
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