| http://purl.uniprot.org/citations/19441079 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19441079 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19441079 | http://www.w3.org/2000/01/rdf-schema#comment | "The matrix protein thrombospondin-4 has an acidic amphipathic C-terminal peptide (C21) which stimulates erythroid cell proliferation. Here we show that C21 stimulates red cell formation in anemic mice in vivo. In vitro experiments indicated that the peptide-mediated increase of erythroid colony formation in cultures of human CD34+ hematopoietic progenitor cells was possible only under continuous presence of erythropoietin. In the absence of this cytokine, C21 stimulated exclusively myeloid colony formation. Therefore, the peptide is not a specific erythroid differentiation factor. In fact, it is mitogenic in non-erythroid cells, such as skin fibroblasts and kidney epithelial cells. In erythroleukemic TF-1 cells, it actually decreased the production of the erythroid differentiation marker glycophorin A. C21-affinity chromatography revealed regulator of differentiation 1 (ROD1) as a major C21-binding protein. ROD1 is the hematopoietic cell paralog of polypyrimidine tract binding proteins (PTBs), RNA splice regulators which regulate differentiation by repressing tissue-specific exons. ROD1 binding to C21 was strongly inhibited by synthetic RNAs in the order poly A > poly U > poly G = poly C and was weakly inhibited by a synthetic phosphorylated peptide mimicking the C-terminal domain of RNA polymerase II. Cellular overexpression or knockdown experiments of ROD1 suggest a role for this protein in the mitogenic activity of C21. Since the nuclear proteins ROD1 and PTBs regulate differentiation at a posttranscriptional level and there is a fast nuclear uptake of C21, we put forward the idea that the peptide is internalized, goes to the nucleus and maintains cells in a proliferative state by supporting ROD1-mediated inhibition of differentiation."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.org/dc/terms/identifier | "doi:10.1002/jcp.21817"xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.org/dc/terms/identifier | "doi:10.1002/jcp.21817"xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/author | "Congote L.F."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/author | "Congote L.F."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/author | "Difalco M.R."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/author | "Difalco M.R."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/author | "Dobocan M.C."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/author | "Dobocan M.C."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/author | "Sadvakassova G."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/author | "Sadvakassova G."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/name | "J. Cell. Physiol."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/name | "J. Cell. Physiol."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/pages | "672-679"xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/pages | "672-679"xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/title | "Regulator of differentiation 1 (ROD1) binds to the amphipathic C-terminal peptide of thrombospondin-4 and is involved in its mitogenic activity."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/title | "Regulator of differentiation 1 (ROD1) binds to the amphipathic C-terminal peptide of thrombospondin-4 and is involved in its mitogenic activity."xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/volume | "220"xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://purl.uniprot.org/core/volume | "220"xsd:string |
| http://purl.uniprot.org/citations/19441079 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19441079 |
| http://purl.uniprot.org/citations/19441079 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19441079 |