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Full-Text Articles in Physics
Association Of Alpha-Crystallin With Human Cortical And Nuclear Lens Lipid Membrane Increases With The Grade Of Cortical And Nuclear Cataract, Preston Hazen, Geraline Trossi-Torres, Raju Timsina, Nawal K. Khadka, Laxman Mainali
Association Of Alpha-Crystallin With Human Cortical And Nuclear Lens Lipid Membrane Increases With The Grade Of Cortical And Nuclear Cataract, Preston Hazen, Geraline Trossi-Torres, Raju Timsina, Nawal K. Khadka, Laxman Mainali
Physics Faculty Publications and Presentations
Eye lens α-crystallin has been shown to become increasingly membrane-bound with age and cataract formation; however, to our knowledge, no studies have investigated the membrane interactions of α-crystallin throughout the development of cataracts in separated cortical membrane (CM) and nuclear membrane (NM) from single human lenses. In this study, four pairs of human lenses from age-matched male and female donors and one pair of male lenses ranging in age from 64 to 73 years old (yo) were obtained to investigate the interactions of α-crystallin with the NM and CM throughout the progression of cortical cataract (CC) and nuclear cataract (NC) …
Cholesterol Content Regulates The Interaction Of Αa-, Αb-, And Α-Crystallin With The Model Of Human Lens-Lipid Membranes, Raju Timsina, Preston Hazen, Geraline Trossi-Torres, Nawal K. Khadka, Navdeep Kalkat, Laxman Mainali
Cholesterol Content Regulates The Interaction Of Αa-, Αb-, And Α-Crystallin With The Model Of Human Lens-Lipid Membranes, Raju Timsina, Preston Hazen, Geraline Trossi-Torres, Nawal K. Khadka, Navdeep Kalkat, Laxman Mainali
Physics Faculty Publications and Presentations
α-Crystallin (αABc) is a major protein comprised of αA-crystallin (αAc) and αB-crystallin (αBc) that is found in the human eye lens and works as a molecular chaperone by preventing the aggregation of proteins and providing tolerance to stress. However, with age and cataract formation, the concentration of αABc in the eye lens cytoplasm decreases, with a corresponding increase in the membrane-bound αABc. This study uses the electron paramagnetic resonance (EPR) spin-labeling method to investigate the role of cholesterol (Chol) and Chol bilayer domains (CBDs) in the binding of αAc, αBc, and αABc to the Chol/model of human lens-lipid (Chol/MHLL) membranes. …
Binding Of ΒL-Crystallin With Models Of Animal And Human Eye Lens-Lipid Membrane, Preston Hazen, Geraline Trossi-Torres, Nawal K. Khadka, Raju Timsina, Laxman Mainali
Binding Of ΒL-Crystallin With Models Of Animal And Human Eye Lens-Lipid Membrane, Preston Hazen, Geraline Trossi-Torres, Nawal K. Khadka, Raju Timsina, Laxman Mainali
Physics Faculty Publications and Presentations
Several discoveries show that with age and cataract formation, β-crystallin binds with the lens membrane or associates with other lens proteins, which bind with the fiber cell plasma membrane, accompanied by light scattering and cataract formation. However, how lipids (phospholipids and sphingolipids) and cholesterol (Chol) influence β-crystallin binding to the membrane is unclear. This research aims to elucidate the role of lipids and Chol in the binding of β-crystallin to the membrane and the membrane’s physical properties (mobility, order, and hydrophobicity) with β-crystallin binding. We used electron paramagnetic resonance (EPR) spin-labeling methods to investigate the binding of βL-crystallin …
Binding Of Alpha-Crystallin To Cortical And Nuclear Lens Lipid Membranes Derived From A Single Lens, Raju Timsina, Samantha Wellisch, Dieter Haemmerle, Laxman Mainali
Binding Of Alpha-Crystallin To Cortical And Nuclear Lens Lipid Membranes Derived From A Single Lens, Raju Timsina, Samantha Wellisch, Dieter Haemmerle, Laxman Mainali
Physics Faculty Publications and Presentations
Several studies reported that α-crystallin concentrations in the eye lens cytoplasm decrease with a corresponding increase in membrane-bound α-crystallin with age and cataracts. The influence of the lipid and cholesterol composition difference between cortical membrane (CM) and nuclear membrane (NM) on α-crystallin binding to membranes is still unclear. This study uses the electron paramagnetic resonance (EPR) spin-labeling method to investigate the α-crystallin binding to bovine CM and NM derived from the total lipids extracted from a single lens. Compared to CMs, NMs have a higher percentage of membrane surface occupied by α-crystallin and binding affinity, correlating with less mobility and …