ArticleCellular and molecular life sciences : CMLS2005
Alpha-crystallin: an ATP-independent complete molecular chaperone toward sorbitol dehydrogenase.
Article in Cellular and molecular life sciences : CMLS, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- Modulation of the Structure and Stability of Novel Camel Lens Alpha-Crystallin by pH and Thermal Stress.Gels (Basel, Switzerland) · 2022Article
- Lens Biology and Biochemistry.Progress in molecular biology and translational science · 2015Review
- The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation.Molecular vision · 2010Article
- The endoplasmic reticulum chaperone Cosmc directly promotes in vitro folding of T-synthase.The Journal of biological chemistry · 2010Article
- Gene duplication and separation of functions in alphaB-crystallin from zebrafish (Danio rerio).The FEBS journal · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
alpha-Crystallin, the major component of the vertebrate lens, is known to interact with proteins undergoing denaturation and to protect them from aggregation phenomena. Bovine lens sorbitol dehydrogenase (SDH) was previously shown to be completely protected by alpha-crystallin from thermally induced aggregation and inactivation. Here we report that alpha-crystallin, in the presence of the SDH pyridine cofactor NAD(H), can exert a remarkable chaperone action by favoring the recovery of the enzyme activity from chemically denaturated SDH up to 77%. Indeed, even in the absence of the cofactor, alpha-crystallin present at a ratio with SDH of 20:1 (w:w) allows a recovery of 35% of the enzyme activity. The effect of ATP in enhancing alpha-crystallin-promoted SDH renaturation appears to be both nonspecific and to not involve hydrolysis phenomena, thus confirming that the chaperone action of alpha-crystallin is not dependent on ATP as energy donor.
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Registered trials
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