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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0006674,
umls-concept:C0007634,
umls-concept:C0017262,
umls-concept:C0031715,
umls-concept:C0033684,
umls-concept:C0040715,
umls-concept:C0185117,
umls-concept:C0205178,
umls-concept:C0205263,
umls-concept:C0256371,
umls-concept:C0441712,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C1414481,
umls-concept:C1522702,
umls-concept:C1637379,
umls-concept:C2911684
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pubmed:issue |
27
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pubmed:dateCreated |
1996-8-29
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pubmed:abstractText |
1,25-Dihydroxyvitamin D3 (1,25-(OH)2D3) primes NB4 cells for 12-O-tetradecanoylphorbol-13-acetate-induced monocytic differentiation in a dose- and sequence-dependent fashion. Experiments utilizing 1,25-(OH)2D3 analogues and kinase/phosphatase inhibitors suggested that tyrosine kinase and serine/threonine phosphorylation cascades, rather than vitamin D3 receptor-mediated signals, were involved in 1,25-(OH)2D3 action. Here we show that NB4 cells express the alpha and delta (but not the beta, epsilon, and theta) isoforms of protein kinase C (PKC). Both authentic 1, 25-(OH)2D3 and the nongenomic analogue 1alpha,25-dihydroxyprevitamin D3 (HF) increased expression of PKCalpha and PKCdelta. PKCalpha and PKCdelta were translocated to the nucleus of the cell in response to 1,25-(OH)2D3 or HF. The effects of HF were attenuated by the nongenomic antagonist 1beta,25-dihydroxyvitamin D3, suggesting that changes in PKC expression are mediated by a nongenomic signaling pathway. Consistent with the involvement of serine, threonine, and tyrosine phosphorylation cascades mediating 1,25-(OH)2D3 action, enhanced phosphorylation of a variety of cellular proteins at serine and threonine residues and the specific enhanced phosphotyrosyl content of a 33-kDa protein (vdrp33) were observed immediately after 1,25-(OH)2D3 addition. We propose that 1,25-(OH)2D3 primes NB4 cells for 12-O-tetradecanoylphorbol-13-acetate-induced monocytic differentiation by increasing the expression of specific PKC isoforms and inducing the specific phosphorylation of key protein signaling intermediates.
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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/Calcitriol,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/PRKCA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PRKCD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-delta,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16090-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8663234-Blotting, Western,
pubmed-meshheading:8663234-Calcitriol,
pubmed-meshheading:8663234-Cell Line,
pubmed-meshheading:8663234-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8663234-Gene Expression,
pubmed-meshheading:8663234-Humans,
pubmed-meshheading:8663234-Isoenzymes,
pubmed-meshheading:8663234-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:8663234-Molecular Weight,
pubmed-meshheading:8663234-Phosphoproteins,
pubmed-meshheading:8663234-Phosphorylation,
pubmed-meshheading:8663234-Protein Kinase C,
pubmed-meshheading:8663234-Protein Kinase C-alpha,
pubmed-meshheading:8663234-Protein Kinase C-delta,
pubmed-meshheading:8663234-Tetradecanoylphorbol Acetate,
pubmed-meshheading:8663234-Tumor Cells, Cultured
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pubmed:year |
1996
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pubmed:articleTitle |
1,25-Dihydroxyvitamin D3 stimulates expression and translocation of protein kinase Calpha and Cdelta via a nongenomic mechanism and rapidly induces phosphorylation of a 33-kDa protein in acute promyelocytic NB4 cells.
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pubmed:affiliation |
Department of Human Biology and Nutritional Sciences, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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