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Small changes lead to increased protective ability in disease-related protein; Study involved fish from the Antarctic to the tropics
The small heat shock protein (sHsp) alpha A-crystallin plays a role in the prevention of human diseases such as Alzheimer's, lens cataracts and cancer. By comparing the alpha A-crystallins from six different fish species living at temperatures from -2 to 40 degrees Celsius, the researchers were able to identify two small changes in the protein's structure that affected its stability and ability to buffer other proteins from stress.
After cloning the gene for alpha A-crystallin from the six different fish species, the study authors discovered that the protective function and stability of the resulting proteins correlated with the temperature of each fish. Using amino acid sequence and structural modeling analysis they identified specific amino acid differences between the warm adapted zebrafish and the cold adapted Antarctic toothfish.
By genetically engineering zebrafish alpha A-crystallins with amino acid substitutions found in the Antarctic toothfish the authors were able to show that two of these three changes alter alpha A-crystallin protective function in a predictable way.
“Not only does this add to our basic understanding of how small heat shock proteins work, but it validates a technique for identifying small heat shock protein modifications that could have therapeutic applications,” say Kiss and Mason Posner, professor of biology at Ashland University and lead study author.
Andor Kiss contributed to this article.