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• W2143657633 endingPage "431" @default.
• W2143657633 startingPage "423" @default.
• W2143657633 abstract "Interaction of two members of the heterogeneous nuclear ribonucleoprotein (hnRNP) family with the 3'untranslated region (UTR) of the murine inducible nitric-oxide synthase (iNOS) mRNA is demonstrated in this study. An iNOS RNA-protein complex is formed using protein extracts from untreated and septic shock treated mouse liver. UV cross-linking reveals that the complex consists of at least two proteins, with apparent molecular masses of 60 and 70 kDa, respectively. The 60-kDa protein binding site lies within a 112-nt pyrimidine-rich sequence, approximately 160 nt from the coding sequence, and the RNA-protein complex can be precipitated by a monoclonal antibody directed against hnRNP I [also named polypyrimidine tract binding protein (PTB)]. The 70-kDa protein binds a 43-nt sequence near the 3'end of the 3'UTR and is immunoprecipitated by a monoclonal antibody against hnRNP L. A computer-simulated conformation of the 3'UTR suggests that both binding sites reside in regions easily accessible for a protein. Supershifts of the native RNA-protein complex could only be achieved with anti-hnRNP L, suggesting that within this multiprotein RNA complex, only hnRNP L is exposed to the antibodies, whereas the hnRNP I/PTB is mainly responsible for its interaction with the mRNA. Up-regulation of iNOS by septic shock reduces the RNA-protein complex formation, thus showing that hnRNP I/PTB and hnRNP L binding to the iNOS mRNA is modulated by inflammation. This suggests a novel function for the two previously described proteins as regulators of the iNOS gene." @default.
• W2143657633 created "2016-06-24" @default.
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• W2143657633 date "2002-08-01" @default.
• W2143657633 modified "2023-10-16" @default.
• W2143657633 title "Inflammation Modulates the Interaction of Heterogeneous Nuclear Ribonucleoprotein (hnRNP) I/Polypyrimidine Tract Binding Protein and hnRNP L with the 3′Untranslated Region of the Murine Inducible Nitric-Oxide Synthase mRNA" @default.
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• W2143657633 doi "https://doi.org/10.1124/mol.62.2.423" @default.
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