Manipulating polydispersity of lens β-crystallins using divalent cations demonstrates evidence of calcium regulation.

ABSTRACT: Crystallins comprise the protein-rich tissue of the eye lens. Of the three most common vertebrate subtypes, β-crystallins exhibit the widest degree of polydispersity due to their complex multimerization properties in situ. While polydispersity enables precise packing densities across the concentration gradient of the lens for vision, it is unclear why there is such a high degree of structural complexity within the β-crystallin subtype and what the role of this feature is in the lens. To investigate this, we first characterized β-crystallin polydispersity and then established a method to dynamically disrupt it in a process that is dependent on isoform composition and the presence of divalent cationic salts (CaCl₂ or MgCl₂). We used size-exclusion chromatography togethe

SUBMITTER: Bergman MR 

PROVIDER: S-EPMC9860307 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature