Abstract |
Phorbol diesters induce macrophage-like differentiation in KG-1 and HL-60 human acute myelogenous leukemia cell lines. We developed a cloned subline of KG-1, known as KG-1a, that does not differentiate when exposed to phorbol diesters. Both KG-1 and KG-1a cells have a single class of specific high-affinity receptors for labeled phorbol-12,13-dibutyrate with a mean Kd of 1.47 +/- 0.10 (S.E.) X 10(-8) M and 0.85 +/- 0.20 X 10(-8) M for the sensitive parental KG-1 line and the resistant KG-1a subline, respectively (p less than 0.025). The number of [3H] phorbol-12,13-dibutyrate binding sites (mean +/- S.E.) per cell was 3.85 +/- 0.98 X 10(5) and 3.94 +/- 0.31 X 10(5) on KG-1 and resistant KG-1a cells, respectively. We observed no significant decrease of specific binding with time (down regulation) in either KG-1, KG-1a, or HL-60 cells, suggesting that down regulation of specific phorbol-12,13-dibutyrate binding is not critical to induction of differentiation. Our data also confirm that the presence of specific high-affinity phorbol receptors on leukemic cells does not assure that phorbol diesters can trigger their differentiation.
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Authors | R I Lehrer, L E Cohen, H P Koeffler |
Journal | Cancer research
(Cancer Res)
Vol. 43
Issue 8
Pg. 3563-6
(Aug 1983)
ISSN: 0008-5472 [Print] United States |
PMID | 6574815
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Phorbol Esters
- Phorbols
- Phorbol 12,13-Dibutyrate
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Topics |
- Cell Differentiation
(drug effects)
- Cell Line
- Clone Cells
(metabolism)
- Humans
- Leukemia, Myeloid, Acute
(metabolism)
- Phorbol 12,13-Dibutyrate
- Phorbol Esters
(metabolism, pharmacology)
- Phorbols
(metabolism, pharmacology)
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