Insilico Approach to Inhibit Over Expression of CaSm Gene to Arrest Over Expressed Human LSm1 Protein in Pancreatic Carcinoma Cell
Abstract
Small nuclear ribonucleoproteins (snRNPs) are particles that are found in the nucleus of eukaryotic cells. They consist of one RNA (snRNA) associated with one or more proteins. snRNPs are involved in a wide variety of functions including pre-mRNA splicing (e.g., U1, U2, U4–6, U11, U12, U4ATAC, U6ATAC snRNPs and transspliced leader RNPs), histone mRNA 39 end processing (U7 snRNP). The snRNA U6 (unlike U1, U2, U4 and U5) does not associate with the Sm proteins. In 1999 heteromer protein was identified that binds only to U6, and made up of seven proteins which are homologous to the Sm proteins. These proteins were denoted LSm (like Sm) proteins (LSm1, LSm2, LSm3, LSm4, LSm5, LSm6, and LSm7), LSm8 protein identified after that. The cancer associated Sm-like protooncogene mRNA has been found to be overexpressed in the majority of pancreatic adenocarcinomas and is necessary for the transformed phenotype in pancreatic cancer cell lines. Human Lsm1, also called CaSm (cancer-associated Sm-like) was originally identified based on elevated expression in pancreatic cancer, in several cancer-derived cell lines as well as in metastatic tumors. CaSm is also required to maintain the transformed phenotype of prostate cancer cells and it can function as a oncogene in that over-expression of this gene. In this present study some of cancer drugs like S-adenosyl-L-Homocystein, S-adenosyl-L-Homoselenocystein, Adenosyl-ornithine and S-adenosylmethionine were tested through bioinformatics tools to check whether they could suppress the overexpression of LSm1 protein.
Keywords: Protooncogene, spliceosome, CaSm, human LSm, adenocarcinomas, ribonucleoproteins
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