Imaging Cataract-Specific Peptides in Human Lenses
Age-related protein truncation is a common process in long-lived proteins such as proteins found in the ocular lens. Major truncation products have been reported for soluble and membrane proteins of the lens, including small peptides that can accelerate protein aggregation. However, the spatial loca...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-12-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/11/24/4042 |
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| author | Kevin L. Schey Zhen Wang Kristie L. Rose David M. G. Anderson |
| author_facet | Kevin L. Schey Zhen Wang Kristie L. Rose David M. G. Anderson |
| author_sort | Kevin L. Schey |
| collection | DOAJ |
| description | Age-related protein truncation is a common process in long-lived proteins such as proteins found in the ocular lens. Major truncation products have been reported for soluble and membrane proteins of the lens, including small peptides that can accelerate protein aggregation. However, the spatial localization of age-related protein fragments in the lens has received only limited study. Imaging mass spectrometry (IMS) is an ideal tool for examining the spatial localization of protein products in tissues. In this study we used IMS to determine the spatial localization of small crystallin fragments in aged and cataractous lenses. Consistent with previous reports, the pro-aggregatory αA-crystallin 66–80 peptide as well as αA-crystallin 67–80 and γS-crystallin 167–178 were detected in normal lenses, but found to be increased in nuclear cataract regions. In addition, a series of γS-crystallin C-terminal peptides were observed to be mainly localized to cataractous regions and barely detected in transparent lenses. Other peptides, including abundant αA3-crystallin peptides were present in both normal and cataract lenses. The functional properties of these crystallin peptides remain unstudied; however, their cataract-specific localization suggests further studies are warranted. |
| first_indexed | 2024-03-09T17:12:40Z |
| format | Article |
| id | doaj.art-c46b74946ace4d03beb30e20a7bc6873 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-09T17:12:40Z |
| publishDate | 2022-12-01 |
| publisher | MDPI AG |
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| series | Cells |
| spelling | doaj.art-c46b74946ace4d03beb30e20a7bc68732023-11-24T13:54:50ZengMDPI AGCells2073-44092022-12-011124404210.3390/cells11244042Imaging Cataract-Specific Peptides in Human LensesKevin L. Schey0Zhen Wang1Kristie L. Rose2David M. G. Anderson3Department of Biochemistry and Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USADepartment of Biochemistry and Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USADepartment of Biochemistry and Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USADepartment of Biochemistry and Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USAAge-related protein truncation is a common process in long-lived proteins such as proteins found in the ocular lens. Major truncation products have been reported for soluble and membrane proteins of the lens, including small peptides that can accelerate protein aggregation. However, the spatial localization of age-related protein fragments in the lens has received only limited study. Imaging mass spectrometry (IMS) is an ideal tool for examining the spatial localization of protein products in tissues. In this study we used IMS to determine the spatial localization of small crystallin fragments in aged and cataractous lenses. Consistent with previous reports, the pro-aggregatory αA-crystallin 66–80 peptide as well as αA-crystallin 67–80 and γS-crystallin 167–178 were detected in normal lenses, but found to be increased in nuclear cataract regions. In addition, a series of γS-crystallin C-terminal peptides were observed to be mainly localized to cataractous regions and barely detected in transparent lenses. Other peptides, including abundant αA3-crystallin peptides were present in both normal and cataract lenses. The functional properties of these crystallin peptides remain unstudied; however, their cataract-specific localization suggests further studies are warranted.https://www.mdpi.com/2073-4409/11/24/4042imaging mass spectrometryocular lensprotein degradationcataract |
| spellingShingle | Kevin L. Schey Zhen Wang Kristie L. Rose David M. G. Anderson Imaging Cataract-Specific Peptides in Human Lenses Cells imaging mass spectrometry ocular lens protein degradation cataract |
| title | Imaging Cataract-Specific Peptides in Human Lenses |
| title_full | Imaging Cataract-Specific Peptides in Human Lenses |
| title_fullStr | Imaging Cataract-Specific Peptides in Human Lenses |
| title_full_unstemmed | Imaging Cataract-Specific Peptides in Human Lenses |
| title_short | Imaging Cataract-Specific Peptides in Human Lenses |
| title_sort | imaging cataract specific peptides in human lenses |
| topic | imaging mass spectrometry ocular lens protein degradation cataract |
| url | https://www.mdpi.com/2073-4409/11/24/4042 |
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