Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation
α-crystallin is a major protein found in the mammalian eye lens that works as a molecular chaperone by preventing the aggregation of proteins and providing tolerance to stress in the eye lens. These functions of α-crystallin are significant for maintaining lens transparency. However, with age and ca...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-06-01
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| Series: | Membranes |
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| Online Access: | https://www.mdpi.com/2077-0375/11/6/447 |
| _version_ | 1797530072285970432 |
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| author | Raju Timsina Laxman Mainali |
| author_facet | Raju Timsina Laxman Mainali |
| author_sort | Raju Timsina |
| collection | DOAJ |
| description | α-crystallin is a major protein found in the mammalian eye lens that works as a molecular chaperone by preventing the aggregation of proteins and providing tolerance to stress in the eye lens. These functions of α-crystallin are significant for maintaining lens transparency. However, with age and cataract formation, the concentration of α-crystallin in the eye lens cytoplasm decreases with a corresponding increase in the membrane-bound α-crystallin, accompanied by increased light scattering. The purpose of this review is to summarize previous and recent findings of the role of the: (1) lens membrane components, i.e., the major phospholipids (PLs) and sphingolipids, cholesterol (Chol), cholesterol bilayer domains (CBDs), and the integral membrane proteins aquaporin-0 (AQP0; formally MIP26) and connexins, and (2) α-crystallin mutations and post-translational modifications (PTMs) in the association of α-crystallin to the eye lens’s fiber cell plasma membrane, providing thorough insights into a molecular basis of such an association. Furthermore, this review highlights the current knowledge and need for further studies to understand the fundamental molecular processes involved in the association of α-crystallin to the lens membrane, potentially leading to new avenues for preventing cataract formation and progression. |
| first_indexed | 2024-03-10T10:23:44Z |
| format | Article |
| id | doaj.art-b078c3ac603947839afa637015e9f3ce |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-10T10:23:44Z |
| publishDate | 2021-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-b078c3ac603947839afa637015e9f3ce2023-11-22T00:12:37ZengMDPI AGMembranes2077-03752021-06-0111644710.3390/membranes11060447Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract FormationRaju Timsina0Laxman Mainali1Department of Physics, Boise State University, Boise, ID 83725, USADepartment of Physics, Boise State University, Boise, ID 83725, USAα-crystallin is a major protein found in the mammalian eye lens that works as a molecular chaperone by preventing the aggregation of proteins and providing tolerance to stress in the eye lens. These functions of α-crystallin are significant for maintaining lens transparency. However, with age and cataract formation, the concentration of α-crystallin in the eye lens cytoplasm decreases with a corresponding increase in the membrane-bound α-crystallin, accompanied by increased light scattering. The purpose of this review is to summarize previous and recent findings of the role of the: (1) lens membrane components, i.e., the major phospholipids (PLs) and sphingolipids, cholesterol (Chol), cholesterol bilayer domains (CBDs), and the integral membrane proteins aquaporin-0 (AQP0; formally MIP26) and connexins, and (2) α-crystallin mutations and post-translational modifications (PTMs) in the association of α-crystallin to the eye lens’s fiber cell plasma membrane, providing thorough insights into a molecular basis of such an association. Furthermore, this review highlights the current knowledge and need for further studies to understand the fundamental molecular processes involved in the association of α-crystallin to the lens membrane, potentially leading to new avenues for preventing cataract formation and progression.https://www.mdpi.com/2077-0375/11/6/447α-crystallinfiber cell plasma membranelipidscholesterolcholesterol bilayer domainsintegral membrane protein |
| spellingShingle | Raju Timsina Laxman Mainali Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation Membranes α-crystallin fiber cell plasma membrane lipids cholesterol cholesterol bilayer domains integral membrane protein |
| title | Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation |
| title_full | Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation |
| title_fullStr | Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation |
| title_full_unstemmed | Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation |
| title_short | Association of Alpha-Crystallin with Fiber Cell Plasma Membrane of the Eye Lens Accompanied by Light Scattering and Cataract Formation |
| title_sort | association of alpha crystallin with fiber cell plasma membrane of the eye lens accompanied by light scattering and cataract formation |
| topic | α-crystallin fiber cell plasma membrane lipids cholesterol cholesterol bilayer domains integral membrane protein |
| url | https://www.mdpi.com/2077-0375/11/6/447 |
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