Phosphoinositide signalling in nuclei of Friend cells: DMSO-induced differentiation reduces the association of phosphatidylinositol-transfer protein with the nucleus
| Autor: | Alessandro Matteucci, Joyce Lutterman, Anna Maria Billi, Karel W. A. Wirtz, Lucio Cocco, Silvia Rubbini, Lucia Manzoli |
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| Rok vydání: | 1997 |
| Předmět: |
Gene isoform
Biophysics Phospholipase C beta Biology Phospholipase Phosphatidylinositols Biochemistry Cell Line chemistry.chemical_compound Mice medicine Animals Dimethyl Sulfoxide Phosphatidylinositol Phospholipid Transfer Proteins Fluorescent Antibody Technique Indirect Molecular Biology Phosphatidylinositol transfer protein Cell Nucleus Cell growth Membrane Proteins Cell Differentiation Cell Biology Molecular biology Cell biology Blot Isoenzymes Microscopy Electron medicine.anatomical_structure chemistry Type C Phospholipases Leukemia Erythroblastic Acute Bacterial outer membrane Carrier Proteins Nucleus Signal Transduction |
| Zdroj: | Biochemical and biophysical research communications. 230(2) |
| ISSN: | 0006-291X |
| Popis: | Friend erythroleukemia cells have a nuclear phosphoinositide cycle which is related to both mitogen-stimulated cell growth and erythorid differentiation. Because of the important role of the phosphatidylinositol-transfer protein (PI-TP) in phosphatidylinositol 4,5-bisphosphate (PtdInsP2) synthesis, we have analysed nuclei isolated from Friend cells for the presence of PI-TP. By Western Blotting it was demonstrated that both intact nuclei and nuclei deprived of the outer membrane contained the PI-TP alpha isoform. Upon induction of erythroid differentiation by DMSO, the amount of nuclear PI-TP alpha was greatly diminished. As shown previously, under these same conditions, nuclear phospholipase C beta1 (PLC beta1) is down-regulated as well. |
| Databáze: | OpenAIRE |
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