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Journal of Undergraduate Research

Keywords

direct inhibition, phosphorylation, sodium-potassium, ATPase, cataract formation

College

Physical and Mathematical Sciences

Department

Chemistry and Biochemistry

Abstract

Preliminary data suggested that bovine lens epithelial cells (BLEC) are able to increase the amount of sodium-potassium ATPase (sodium pump or SP) in the plasma membrane. I set out to accomplish three objectives: (1) to continue ongoing ouabain inhibition experiments in order to confirm the preliminary data; (2) to examine BLEC’s response to peptide hormones (in other tissues the peptide hormone induced phosphorylation of SP is followed by an observable removal of SP from the membrane); and (3) to confirm our hypothesis that observations of SP redistribution are a manifestation of BLEC’s ability to compensate for the inhibitory effect of ouabain on membrane-bound SP. I expected to report that although the distribution and location of SP fluctuates in response to differing inhibitory treatments, the net SP activity remains unchanged after the cell is allowed sufficient time to shuffle the distribution of its SPs, thereby compensating for the loss of ion exchange activity. My overarching intent was to determine whether two methods of reducing SP activity, ie. via direct inhibition or phosphorylation, went uncompensated by BLEC (further confirming their candidacy for cataract-causing agents) or whether other mechanisms, e.g., genetic regulation, most likely explain the reduced SP activity characteristic of cataracts.

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