Concentration dependence of chaperone-like activities of α-crystallin, αB-crystallin and proline

Roman, Svetlana G.; Chebotareva, Natalia A.; Bi, Kurganov

doi:10.1016/j.ijbiomac.2012.03.015

Cited by 17 publications

(24 citation statements)

References 28 publications

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“…Ample evidence demonstrates the complexation of α-crystallin with nonnative proteins [1], [14]–[18]. The formation of complexes between dissociated forms of α-crystallin and target substrates, muscle glyceraldehyde 3-phosphate dehydrogenase (GAPDH) or glycogen phosphorylase b (Ph b ), at elevated temperatures has been demonstrated in our studies [19]–[22].…”

Section: Introductionsupporting

confidence: 56%

“…When analyzing the shape of the kinetic curves of aggregation of Ph b denatured by UV radiation [22], we observed that Eq. (3) is not fulfilled and, to characterize the initial rate of aggregation, we proposed to use the time interval ( t 2I ) over which the initial value of the light scattering intensity is doubled.…”

Section: Theory Quantification Of the Chaperone-like Activitymentioning

confidence: 99%

“…Consider the dependence of the initial rate of aggregation of UV-irradiated Ph b on the αB-crystallin concentration obtained in [22] (37°C; pH 6.8). The v value was calculated using Eq.…”

Section: Theory Quantification Of the Chaperone-like Activitymentioning

confidence: 99%

“…Anti-aggregation activity of proline (Pro), one of the osmolytes behaving as a chemical chaperone, was demonstrated in in vivo and in vitro experiments [22], [42]–[45]. Pro is found to prevent aggregation during protein refolding [42], [43], [46], [47].…”

Section: Introductionmentioning

confidence: 99%

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Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

et al. 2013

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The methodology for quantification of the anti-aggregation activity of protein and chemical chaperones has been elaborated. The applicability of this methodology was demonstrated using a test-system based on dithiothreitol-induced aggregation of bovine serum albumin at 45°C as an example. Methods for calculating the initial rate of bovine serum albumin aggregation (v agg) have been discussed. The comparison of the dependences of v agg on concentrations of intact and cross-linked α-crystallin allowed us to make a conclusion that a non-linear character of the dependence of v agg on concentration of intact α-crystallin was due to the dynamic mobility of the quaternary structure of α-crystallin and polydispersity of the α-crystallin–target protein complexes. To characterize the anti-aggregation activity of the chemical chaperones (arginine, arginine ethyl ester, arginine amide and proline), the semi-saturation concentration [L]0.5 was used. Among the chemical chaperones studied, arginine ethyl ester and arginine amide reveal the highest anti-aggregation activity ([L]0.5 = 53 and 58 mM, respectively).

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Section: Introductionsupporting

confidence: 56%

Section: Theory Quantification Of the Chaperone-like Activitymentioning

confidence: 99%

“…Consider the dependence of the initial rate of aggregation of UV-irradiated Ph b on the αB-crystallin concentration obtained in [22] (37°C; pH 6.8). The v value was calculated using Eq.…”

Section: Theory Quantification Of the Chaperone-like Activitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

et al. 2013

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“…Multiple data demonstrate that under conditions of heat denaturation of protein the mechanism of antiaggregation activity of α-crystallin involves formation of chaperone complexes with destabilized proteins [17,36,[42][43][44]. The formation of complexes between dissociated forms of α-crystallin and target substrates, muscle glyceraldehyde-3-phosphate dehydrogenase or glycogen phosphorylase b, at elevated temperatures was demonstrated in our earlier studies [32,45,46].…”

Section: Introductionmentioning

confidence: 55%

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

Borzova

Markossian

Muranov

et al. 2015

International Journal of Biological Macromolecules

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Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. Effect of crowding agents and chaperones

et al. 2014

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The effect of protein and chemical chaperones and crowders on thermal stability and aggregation of apoform of rabbit muscle glycogen phosphorylase b (apoPhb) has been studied at 37°C. Proline suppressed heat-induced loss in ability of apoPhb to reconstitution at 37°C, whereas α-crystallin did not reveal a protective action. To compare the antiaggregation activity of intact and crosslinked α-crystallins, an adsorption capacity (AC) of a protein chaperone with respect to a target protein was estimated. This parameter is a measure of the antiaggregation activity. Crosslinking of α-crystallin results in 11-fold decrease in the initial AC. The nonlinear character of the relative initial rate of apoPhb aggregation versus the [intact α-crystallin]/[apoPhb] ratio plot is indicative of the decrease in the AC of α-crystallin with increasing the [α-crystallin]/[apoPhb] ratio and can be interpreted as an evidence for dynamic chaperone structure and polydispersity of α-crystallin-target protein complexes. As for chemical chaperones, a semisaturation concentration of the latter was used as a characteristic of the antiaggregation activity. A decrease in the semisaturation concentration for proline was observed in the presence of the crowders (polyethylene glycol and Ficoll-70).

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Concentration dependence of chaperone-like activities of α-crystallin, αB-crystallin and proline

Cited by 17 publications

References 28 publications

Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

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

Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. Effect of crowding agents and chaperones

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