Sandbox Reserved 200: Difference between revisions

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==Medical Relevance==
==Medical Relevance==
[http://en.wikipedia.org/wiki/Alzheimer%27s_disease Alzheimer’s disease] is a terminal disease that slowly degenerates the brain.  One of the possible causes of Alzheimer’s is [http://en.wikipedia.org/wiki/Amyloid amyloid] deposits throughout the brain.  Though RNase A oligomers are not the amyloid deposits that cause Alzheimer’s, the folding of these oligomers gives clues towards the formation of amyloid deposits responsible for Alzheimer’s.
[http://en.wikipedia.org/wiki/Alzheimer%27s_disease Alzheimer’s disease] is a terminal disease that slowly degenerates the brain.  One of the possible causes of Alzheimer’s is [http://en.wikipedia.org/wiki/Amyloid amyloid] deposits throughout the brain.  Though RNase A oligomers are not the amyloid deposits that cause Alzheimer’s, the folding of these oligomers gives clues about the formation of the amyloid deposits responsible for Alzheimer’s.




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The RNase A 3D domain swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity.  In antitumor activity, the oligomers degrade dsRNA, but they are also capable of degrading DNA and RNA hybrids which can be found during the translation of genes.<ref name="tumor"/>  This same activity has not been observed in the monomer and the non-3D domain swapped oligomers .<ref name="liu98">PMID:9520384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref >   
The RNase A 3D domain swapped oligomers show significant biological activity including allostery, antitumor, and immunosupressive activity.  In antitumor activity, the oligomers degrade dsRNA, but they are also capable of degrading DNA and RNA hybrids which can be found during the translation of genes.<ref name="tumor"/>  This same activity has not been observed in the monomer and the non-3D domain swapped oligomers .<ref name="liu98">PMID:9520384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref >   




All oligomers of RNase A have antitumor activity, but the higher ordered oligomers show greater activity. <ref name="tumor"/>  Though the higher ordered oligomers are more active, they are also much more unstable when ''in vivo''.  The pathway of the oligomer once it is inside the cell is unknown, but the activity seems to be unregulated.  <ref name="tumor"/>  In cancer cells the movement of proteins through nuclear pores is unregulated, therefore oligomers can sometimes enter into the nucleus.  Once the oligomer is in the nucleus, it is able to degrade RNA and DNA hybrids.<ref name="tumor"/>  This will eventually prevent the cell from dividing and decrease the tumor size.  Before oligomers can be used as an antitumor drug, the pathway of high ordered oligomers into the cell needs to be monitored, as well as their function within the cell.  This needs to occur to prevent the degradation of dsRNA in healthy cells.
All oligomers of RNase A have antitumor activity, but the higher ordered oligomers show greater activity. <ref name="tumor"/>  Though the higher ordered oligomers are more active, they are also much more unstable ''in vivo'', and the pathway inside the cell is unknown.  Before oligomers can be used as an antitumor drug and to prevent the degradation of dsRNA in healthy cells, the pathway of high ordered oligomers into the cell needs to be monitored, as well as their function within the cell.   


==Literature Cited==
==Literature Cited==