The effect of dextran on subunit exchange of the molecular chaperone αA-crystallin

Ghahghaei, Arezou; Rekas, Agata; Price, William E.; Carver, John A.

doi:10.1016/j.bbapap.2006.10.002

Cited by 27 publications

(21 citation statements)

References 49 publications

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“…Furthermore, the chaperone ability of alpha-crystallin increased with increasing pH. This is consistent with other data showing that the chaperone ability of alpha-crystallin is less efficient for rapidly aggregating target protein [24,25] .…”

Section: Resultssupporting

confidence: 91%

“…Increased aggregation of heated betalactoglobulin in the presence of DTT showed that aggregation of beta-lactoglobulin occurs both via intramolecular and intermolecular disulphide bond formation (hydrophobic interactions and a nucleationdependent). Under these conditions beta-lactoglobulin aggregates much faster and alpha-crystallin is not a good chaperone [25] to prevent its aggregation. At room temperature and physiological pH, betalactoglobulin exists as a dimer in which the monomers are noncovalently linked but dissociates into monomers upon heating [33] .…”

Section: Discussionmentioning

confidence: 99%

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The Effect of Molecular Chaperone, Alpha-Crystallin, on the Heat-Induced Aggregation of Beta-lactoglobulin

Ghahghaei¹

2008

American J. of Biochemistry and Biotechnology

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Aggregation of beta-lactoglobulin occurs mainly via intermolecular disulphide bond exchange. Upon heating, beta-lactoglobulin aggregated which increased with increasing pH. The presence of DTT led to more rapid aggregation and precipitation of beta-lactoglobulin. AlphaCrystallin prevented the aggregation of heat-stressed beta-lactoglobulin and was a more efficient chaperone at higher pH values. In the presence of DTT, however, alpha-crystallin was a less efficient chaperone due to faster aggregation of heated and reduced beta-lactoglobulin.

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Section: Resultssupporting

confidence: 91%

Section: Discussionmentioning

confidence: 99%

The Effect of Molecular Chaperone, Alpha-Crystallin, on the Heat-Induced Aggregation of Beta-lactoglobulin

Ghahghaei¹

2008

American J. of Biochemistry and Biotechnology

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“…␣-Crystallin particles possess dynamic structure and show a capacity for intermolecular exchange of subunits and partial dissociation into suboligomeric forms when interacting with target protein [9,15,[48][49][50][51][52][53][54][55][56]. Carver and coworkers showed that the rate of subunit exchange of ␣A-crystallin decreased under crowding conditions [57]. Thus, one can expect that crowding will affect the rate of the nucleation stages preceding the formation of start aggregates in the presence of ␣-crystallin.…”

Section: Methodsmentioning

confidence: 95%

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

Chebotareva

Filippov

2015

International Journal of Biological Macromolecules

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“…sHsps are most effective against slowly-aggregating target proteins undergoing amorphous aggregation [3,36,108]. This is because sHsps interact with intermediately folded states of target proteins and thus the longer these states persist, the better the ability of sHsps to interact with them.…”

Section: Shsps and The Aβ Peptidesmentioning

confidence: 99%

Crystallin proteins and amyloid fibrils

Ecroyd

Carver

2008

Cell. Mol. Life Sci.

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220

234

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Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates. The major lens protein, alpha-crystallin, is a member of the small heat-shock protein (sHsp) family of intracellular molecular chaperone proteins that prevent protein aggregation. Whilst the chaperone activity of sHsps against amorphously aggregating proteins has been well studied, its action against fibril-forming proteins has received less attention despite the presence of sHsps in deposits found in fibril-associated diseases (e.g. Alzheimer's and Parkinson's). In this review, the literature on the interaction of alpha B-crystallin and other sHsps with fibril-forming proteins is summarized. In particular, the ability of sHsps to prevent fibril formation, their mechanisms of action and the possible in vivo consequences of such associations are discussed. Finally, the fibril-forming propensity of the crystallin proteins and its implications for cataract formation are described along with the potential use of fibrillar crystallin proteins as bionanomaterials. Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates. The major lens protein, α-crystallin, is a member of the small heat-shock protein (sHsp) family of intracellular molecular chaperone proteins that prevent protein aggregation. Whilst the chaperone activity of sHsps against amorphously aggregating proteins has been well studied, its action against fibril-forming proteins has received less attention despite the presence of sHsps in deposits found in fibril-associated diseases (e.g. Alzheimer's and Parkinson's). In this review, the literature on the interaction of αB-crystallin and other sHsps with fibril-forming proteins is summarized. In particular, the ability of sHsps to prevent fibril formation, their mechanisms of action and the possible in vivo consequences of such associations are discussed. Finally, the fibril-forming propensity of the crystallin proteins and its implications for cataract formation are described along with the potential use of fibrillar crystallin proteins as bionanomaterials.

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The effect of dextran on subunit exchange of the molecular chaperone αA-crystallin

Cited by 27 publications

References 49 publications

The Effect of Molecular Chaperone, Alpha-Crystallin, on the Heat-Induced Aggregation of Beta-lactoglobulin

The Effect of Molecular Chaperone, Alpha-Crystallin, on the Heat-Induced Aggregation of Beta-lactoglobulin

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

Crystallin proteins and amyloid fibrils

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