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

Selection of Test Systems for Estimation of Anti-aggregation Activity of Molecular Chaperones

“…The value of n for the aggregation process was found to be 2.5 ± 0.2 (80 mM Hepes buffer, рН 6.8, containing 0.1 M NaCl; 37°C) [17]. The data obtained in our earlier works are consistent with this conclusion [10,18,19]. In Table 1 It should be noted that in the case thermal aggregation of target proteins elevation of temperature can result in the change in the kinetic regime of the aggregation process with realization of the kinetic regime of type B at high temperatures [20,21].…”

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

“…It is well known that ␣-crystallin suppresses DTT-induced aggregation of ␣-lactalbumin [2,5,7,[44][45][46][47]. To elucidate the sensitivity of the rate-limiting stages of the general processes of ␣-lactalbumin aggregation in the presence of ␣-crystallin to crowding, we studied the aggregation kinetics in the presence of PEG.…”

Differential phosphorylation-based regulation of αB-crystallin chaperone activity for multipass transmembrane proteins

“…The protein consists of an N-terminal domain, a conserved central α-crystallin domain and a short C-terminal domain [4] , [7] . It forms soluble complexes with partially unfolded proteins preventing them from irreversible aggregation (“holdase” activity) and keeping them ready for the function of other chaperones that assist in the folding [8] . Besides the crucial role made in the lens in association with αA-crystallin [3] , CRYAB is an extensively expressed sHsp that play a role in a variety of cellular functions such as cell cycle, differentiation, apoptosis, gene expression and has been associated with several pathological conditions [9] , [10] , [11] , [12] , [13] , [14] .…”