Mechanism of aggregation of UV-irradiated βL-crystallin

Quantification of anti-aggregation activity of UV-irradiated α-crystallin

“…The position of the maximum of tryptophan fluorescence remained unchanged when the irradiation dose increased (λ max = 335 nm). The same situation was observed by us earlier upon irradiation of β L -crystallin [12] and glyceraldehyde-3-phosphate dehydrogenase [64].…”

“…UV irradiation results in oxidative damage of lens proteins, especially γ-and β-crystallins, and the formation of insoluble aggregates of high molecular weight, whereas UV irradiation of α-crystallin does not cause significant rearrangement of protein quaternary structure, aggregation of oligomers or loss of solubility [9][10][11][12][13]. However, UV irradiation brings about oxidative modification of α-crystallin [14][15][16].…”

Congenital Cataract-Causing Mutation G129C in γC-Crystallin Promotes the Accumulation of Two Distinct Unfolding Intermediates That Form Highly Toxic Aggregates

“…Many efforts have been devoted in recent years to elucidate the molecular mechanism of cataract caused by mutations or environmental factors [3,[13][14][15][16][17][18][19][20][21][22]. The most widely understood mechanism is the disruption of crystallin solubility and/or stability directly by mutations/modifications or indirectly by changes in cellular homeostasis.…”

Effect of crowding on several stages of protein aggregation in test systems in the presence of α-crystallin

“…Such a complexation modifies subsequent stages of nucleation and start aggregates formation. As for the test systems of the second type, the protein molecules denatured by UV-irradiation are assembled into smallsized primary aggregates [15,17]. Thus, in this case the nucleation stage is lacking, and the effect of chaperone on the aggregation process is determined by interaction of chaperone with primary aggregates.…”