Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1997-1-23
|
| pubmed:abstractText |
The effect of the CSF-1 receptor, cFMS, on the phosphorylation of the retinoblastoma (RB) tumor suppressor protein and on the cell cycle and cell differentiation was analyzed in a cultured promyelocytic leukemia cell capable of induced myelomonocytic differentiation. A series of cFMS-transfected HL-60 sublines with progressively higher cell surface FMS expression was derived by flow cytometric cell sorting. Overexpression of FMS increased the duration of the cell cycle, prolonging all cell cycle phases especially S phase, which doubled. The increased cell cycle generation times occurred without any detectable changes in RB expression level or phosphorylation. For retinoic acid (RA)-induced myeloid differentiation, progressive overexpression of FMS caused a greater fraction of cells to differentiate and G1/0 arrest compared to wild-type cells after the same number of cell cycle generation times. FMS overexpression also progressively increased the relative amount of dephosphorylated RB protein induced, while reducing the total amount of RB protein. The inducer-originated and FMS-driven changes in RB hypophosphorylation were not effected through changes in p21/WAF1/CIP1 in this p53-negative cell. Similar effects on differentiation and G0 arrest occurred with 1,25-dihydroxy vitamin D3 (D3)-induced monocytic differentiation. FMS did not significantly affect myeloid differentiation induced by DMSO, which does not target steroid-thyroid hormone receptors like RA and D3. While differentiation is typically associated with hypophosphorylated RB in all these cases, the kinetics indicate that the FMS-induced changes in cell cycle and cell differentiation do not depend in a direct causal fashion on the interconversion between hyperphosphorylated and hypophosphorylated RB.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CDKN1A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcitriol,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase Inhibitor...,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Macrophage...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retinoblastoma Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0014-4827
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
25
|
| pubmed:volume |
229
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
111-25
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:8940255-Calcitriol,
pubmed-meshheading:8940255-Cell Cycle,
pubmed-meshheading:8940255-Cell Differentiation,
pubmed-meshheading:8940255-Cell Division,
pubmed-meshheading:8940255-Cyclin-Dependent Kinase Inhibitor p21,
pubmed-meshheading:8940255-Cyclins,
pubmed-meshheading:8940255-Enzyme Inhibitors,
pubmed-meshheading:8940255-G1 Phase,
pubmed-meshheading:8940255-Gene Expression,
pubmed-meshheading:8940255-HL-60 Cells,
pubmed-meshheading:8940255-Humans,
pubmed-meshheading:8940255-Kinetics,
pubmed-meshheading:8940255-Monocytes,
pubmed-meshheading:8940255-Phosphorylation,
pubmed-meshheading:8940255-Receptor, Macrophage Colony-Stimulating Factor,
pubmed-meshheading:8940255-Recombinant Proteins,
pubmed-meshheading:8940255-Retinoblastoma Protein,
pubmed-meshheading:8940255-Transfection,
pubmed-meshheading:8940255-Tretinoin
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
FMS (CSF-1 receptor) prolongs cell cycle and promotes retinoic acid-induced hypophosphorylation of retinoblastoma protein, G1 arrest, and cell differentiation.
|
| pubmed:affiliation |
Department of Pathology, College of Veterinary Medicine, Cornell University, Ithaca, New York 14853, USA.
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| pubmed:publicationType |
Journal Article
|