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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0007589,
umls-concept:C0007600,
umls-concept:C0007610,
umls-concept:C0018183,
umls-concept:C0032214,
umls-concept:C0035820,
umls-concept:C0040845,
umls-concept:C0127400,
umls-concept:C0205177,
umls-concept:C0205263,
umls-concept:C0282549,
umls-concept:C0600138,
umls-concept:C1511938,
umls-concept:C1554080,
umls-concept:C1706198
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pubmed:issue |
3
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pubmed:dateCreated |
1998-3-27
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pubmed:abstractText |
The effect of differentiating doses of all-trans retinoic acid (ATRA, 10(-6) M) and vitamin D3 (10(-7) M) was investigated on the nuclear levels of endogenous ceramide and protein kinase C-zeta (PKC-zeta) catalytic activity in HL-60 myeloid cells. ATRA induced a parallel increase of ceramide and catalytically active PKC-zeta into the nuclear compartment of HL-60 cells (peak at 72 h). On the other hand, vitamin D3 increased the levels of nuclear ceramide and PKC-zeta activity to a lesser extent and with a delayed kinetics compared to ATRA (peak at 96 h). Pretreatment of HL-60 cells with high pharmacological concentrations of exogenously-added C2-ceramide (10(-6) M) completely blocked the ATRA-mediated activation of nuclear PKC-zeta. Exogenous C2-ceramide (10(-6) M) also inhibited the granulocytic differentiation induced by ATRA, whereas it did not affect monocytic differentiation mediated by vitamin D3. Transient transfection experiments performed with a plasmid construct containing a constitutively active mutated form of the PKC-zeta cDNA fused in 3' to a fluorescent tag protein (pEGFP-PKC-zeta) demonstrated that the overexpression of catalytically active PKC-zeta was not accompanied by the appearance of a differentiated morphology. These findings suggest that nuclear PKC-zeta is necessary but not sufficient to induce granulocytic differentiation of HL-60 myeloid malignant cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ceramides,
http://linkedlifedata.com/resource/pubmed/chemical/Cholecalciferol,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin,
http://linkedlifedata.com/resource/pubmed/chemical/protein kinase C zeta
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0007-1048
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
100
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
541-9
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pubmed:dateRevised |
2009-4-7
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pubmed:meshHeading |
pubmed-meshheading:9504637-Blotting, Western,
pubmed-meshheading:9504637-Cell Differentiation,
pubmed-meshheading:9504637-Cell Nucleus,
pubmed-meshheading:9504637-Ceramides,
pubmed-meshheading:9504637-Cholecalciferol,
pubmed-meshheading:9504637-Granulocytes,
pubmed-meshheading:9504637-HL-60 Cells,
pubmed-meshheading:9504637-Humans,
pubmed-meshheading:9504637-Protein Kinase C,
pubmed-meshheading:9504637-Tretinoin
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pubmed:year |
1998
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pubmed:articleTitle |
Accumulation of catalytically active PKC-zeta into the nucleus of HL-60 cell line plays a key role in the induction of granulocytic differentiation mediated by all-trans retinoic acid.
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pubmed:affiliation |
Institute of Human Anatomy, University of Ferrara, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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