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In human cells, the heterogeneous nuclear ribonucleoproteins (hnRNP) are represented by a group of polypeptides, with various molecular properties, comprizing the most abundant constituents of the cell nucleus. Autoantibodies to hnRNPs have been reported in patients suffering from different rheumatic dieseases since 1980s. Experimental evidence indicates that hnRNP complexes undergo substantial structural changes during mRNA formation and export. However, how this contributes to disease development still has to be elucidated. Here some preliminary physicochemical features of RNA-protein folding and stability patterns of newly characterized hnRNP A3 with further functional implications in development of systemic human autoimmune states are reported.
In human cells, the heterogeneous nuclear ribonucleoproteins (hnRNP) are represented by a group of polypeptides, with various molecular properties, comprizing the most abundant constituents of the cell nucleus. Autoantibodies to hnRNPs have been reported in patients suffering from different rheumatic dieseases since 1980s. Yet some how physinochemical features of RNA-protein folding and stability patterns of newly hnRNP A3 with further functional implications in development of systemic human autoimmune states are reported.