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- Title
Refolding Increases the Chaperone-like Activity of α H -Crystallin and Reduces Its Hydrodynamic Diameter to That of α-Crystallin.
- Authors
Muranov, Konstantin O.; Poliansky, Nicolay B.; Borzova, Vera A.; Kleimenov, Sergey Y.
- Abstract
αH-Crystallin, a high molecular weight form of α-crystallin, is one of the major proteins in the lens nucleus. This high molecular weight aggregate (HMWA) plays an important role in the pathogenesis of cataracts. We have shown that the chaperone-like activity of HMWA is 40% of that of α-crystallin from the lens cortex. Refolding with urea significantly increased—up to 260%—the chaperone-like activity of α-crystallin and slightly reduced its hydrodynamic diameter (Dh). HMWA refolding resulted in an increase in chaperone-like activity up to 120% and a significant reduction of Dh of protein particles compared with that of α-crystallin. It was shown that the chaperone-like activity of HMWA, α-crystallin, and refolded α-crystallin but not refolded HMWA was strongly correlated with the denaturation enthalpy measured with differential scanning calorimetry (DSC). The DSC data demonstrated a significant increase in the native protein portion of refolded α-crystallin in comparison with authentic α-crystallin; however, the denaturation enthalpy of refolded HMWA was significantly decreased in comparison with authentic HMWA. The authors suggested that the increase in the chaperone-like activity of both α-crystallin and HMWA could be the result of the correction of misfolded proteins during renaturation and the rearrangement of protein supramolecular structures.
- Subjects
CRYSTALLINE lens; DIFFERENTIAL scanning calorimetry; PROTEIN structure; MOLECULAR weights; DIAMETER
- Publication
International Journal of Molecular Sciences, 2023, Vol 24, Issue 17, p13473
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms241713473