Sandbox Reserved 192: Difference between revisions
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=='''Medical Implications'''== | =='''Medical Implications'''== | ||
''Inhibition of Metastasis'': A recent study published in 2010 discusses the possibility of using the degradation capabilities of RNase A and a similar protein DNase I to treat tumors. Tumor propagation is associated with an imbalance in the level of nucleic acid degradation | ''Inhibition of Metastasis'': A recent study published in 2010 discusses the possibility of using the degradation capabilities of RNase A and a similar protein DNase I to treat tumors. Tumor propagation is associated with an imbalance in the level of nucleic acid degradation. This is shown by increased levels of nucleic acids and decreased levels of nuclease activity in the blood of patients. The high levels of nucleic acids are caused by the unregulated expression and the secretion of a specific tumor-derived miRNA and DNA. It was found that the combined treatment with the RNase A and the DNase produced the best results by slowing the growth rate of the tumor. But both the ribonucleases are toxic at high levels; thus, only low levels can be administered to prevent adverse effects. | ||
''Radicalization of RNase A'': Tandem radical damage is a degenerative process where the radicalization of one molecule leads to a number of adverse biological effects. Methionine (Met) residues are transformed to alpha-aminobutyric acid (Aba) with a methanethiyl radical byproduct when bombarded with H*. When cysteine residues are radicalized, they are transformed to Alanine releasing sulfur radicals. This byproduct radical interact with the cis double bond in phospholipid fatty acids causing the conformational shift to the trans isomer. This switch from cis to trans causes many serious unfavorable biological diseases. Further studies into radical stresses on RNase A will help to better understand cellular degradation associated with aging and such degenerative pathologies. | ''Radicalization of RNase A'': Tandem radical damage is a degenerative process where the radicalization of one molecule leads to a number of adverse biological effects. Methionine (Met) residues are transformed to alpha-aminobutyric acid (Aba) with a methanethiyl radical byproduct when bombarded with H*. When cysteine residues are radicalized, they are transformed to Alanine releasing sulfur radicals. This byproduct radical interact with the cis double bond in phospholipid fatty acids causing the conformational shift to the trans isomer. This switch from cis to trans causes many serious unfavorable biological diseases. Further studies into radical stresses on RNase A will help to better understand cellular degradation associated with aging and such degenerative pathologies. | ||