MassIVE MSV000084566

Complete Public PXD016212

Long-lived Metabolic Enzymes in the Crystallin Lens Identified by Pulse-labeling of Mice and Mass Spectrometry

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Description

The lenticular fiber cells are comprised of extremely long-lived proteins while still maintaining an active biochemical state. Dysregulation of these activities has been implicated in age-related cataracts, and other lens diseases. However, the lenticular protein dynamics underlying health and disease is unclear. We sought to measure the global protein turnover rates in the eye using dietary nitrogen-15 (15N)-labeling of mice between 3 and 15 weeks of age. By performing mass spectrometry we measured the 14N- to 15N-peptide ratios of hundreds of lens proteins, including Crystallin, Aquaporin, Collagen and Laminin of the lens capsule, and enzymes that catalyze glycolysis as well as oxidation and reduction reactions. Direct comparison of lens cortex versus nucleus longevity revealed little or no 15N-protein contents in most proteins in the lens nucleus, while there were a broad range of 14N/15N ratios of proteins in the cortex, including crystallin isoforms. Unexpectedly, like the crystallin proteins, many enzymes were also exceedingly long-lived, including those present at relatively high abundance in the nucleus. The slow replacement of these enzymes in spite of young age of the mice suggests their potential roles in age-related metabolic changes in the lens. [doi:10.25345/C5H09K] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Lens Proteomics ; 15N labeling ; Protein Turnover

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Principal Investigators:
(in alphabetical order) 		Jeffrey N. Savas, PhD, Department of Neurology Northwestern University, USA
Jing Jin, Northwestern University, United States
Submitting User: jeffsavas
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