Quantitative peptidomics of Purkinje cell degeneration mice.
Cytosolic carboxypeptidase 1 (CCP1) is a metallopeptidase that removes C-terminal and side-chain glutamates from tubulin. The Purkinje cell degeneration (pcd) mouse lacks CCP1 due to a mutation. Previously, elevated levels of peptides derived from cytosolic and mitochondrial proteins were found in a...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3620535?pdf=render |
| _version_ | 1828371360118734848 |
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| author | Iryna Berezniuk Juan J Sironi Jonathan Wardman Raymond C Pasek Nicolas F Berbari Bradley K Yoder Lloyd D Fricker |
| author_facet | Iryna Berezniuk Juan J Sironi Jonathan Wardman Raymond C Pasek Nicolas F Berbari Bradley K Yoder Lloyd D Fricker |
| author_sort | Iryna Berezniuk |
| collection | DOAJ |
| description | Cytosolic carboxypeptidase 1 (CCP1) is a metallopeptidase that removes C-terminal and side-chain glutamates from tubulin. The Purkinje cell degeneration (pcd) mouse lacks CCP1 due to a mutation. Previously, elevated levels of peptides derived from cytosolic and mitochondrial proteins were found in adult pcd mouse brain, raising the possibility that CCP1 functions in the degradation of intracellular peptides. To test this hypothesis, we used a quantitative peptidomics technique to compare peptide levels in wild-type and pcd mice, examining adult heart, spleen, and brain, and presymptomatic 3 week-old amygdala and cerebellum. Contrary to adult mouse brain, young pcd brain and adult heart and spleen did not show a large increase in levels of intracellular peptides. Unexpectedly, levels of peptides derived from secretory pathway proteins were altered in adult pcd mouse brain. The pattern of changes for the intracellular and secretory pathway peptides in pcd mice was generally similar to the pattern observed in mice lacking primary cilia. Collectively, these results suggest that intracellular peptide accumulation in adult pcd mouse brain is a secondary effect and is not due to a role of CCP1 in peptide turnover. |
| first_indexed | 2024-04-14T06:48:51Z |
| format | Article |
| id | doaj.art-c4248ff8dab04f3297ae00a74b8414f5 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-14T06:48:51Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-c4248ff8dab04f3297ae00a74b8414f52022-12-22T02:07:05ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0184e6098110.1371/journal.pone.0060981Quantitative peptidomics of Purkinje cell degeneration mice.Iryna BerezniukJuan J SironiJonathan WardmanRaymond C PasekNicolas F BerbariBradley K YoderLloyd D FrickerCytosolic carboxypeptidase 1 (CCP1) is a metallopeptidase that removes C-terminal and side-chain glutamates from tubulin. The Purkinje cell degeneration (pcd) mouse lacks CCP1 due to a mutation. Previously, elevated levels of peptides derived from cytosolic and mitochondrial proteins were found in adult pcd mouse brain, raising the possibility that CCP1 functions in the degradation of intracellular peptides. To test this hypothesis, we used a quantitative peptidomics technique to compare peptide levels in wild-type and pcd mice, examining adult heart, spleen, and brain, and presymptomatic 3 week-old amygdala and cerebellum. Contrary to adult mouse brain, young pcd brain and adult heart and spleen did not show a large increase in levels of intracellular peptides. Unexpectedly, levels of peptides derived from secretory pathway proteins were altered in adult pcd mouse brain. The pattern of changes for the intracellular and secretory pathway peptides in pcd mice was generally similar to the pattern observed in mice lacking primary cilia. Collectively, these results suggest that intracellular peptide accumulation in adult pcd mouse brain is a secondary effect and is not due to a role of CCP1 in peptide turnover.http://europepmc.org/articles/PMC3620535?pdf=render |
| spellingShingle | Iryna Berezniuk Juan J Sironi Jonathan Wardman Raymond C Pasek Nicolas F Berbari Bradley K Yoder Lloyd D Fricker Quantitative peptidomics of Purkinje cell degeneration mice. PLoS ONE |
| title | Quantitative peptidomics of Purkinje cell degeneration mice. |
| title_full | Quantitative peptidomics of Purkinje cell degeneration mice. |
| title_fullStr | Quantitative peptidomics of Purkinje cell degeneration mice. |
| title_full_unstemmed | Quantitative peptidomics of Purkinje cell degeneration mice. |
| title_short | Quantitative peptidomics of Purkinje cell degeneration mice. |
| title_sort | quantitative peptidomics of purkinje cell degeneration mice |
| url | http://europepmc.org/articles/PMC3620535?pdf=render |
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