These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Specific binding of [3H]phorbol dibutyrate to phorbol diester-responsive and -resistant clones of a human myeloid leukemia (KG-1) line 1.
    Author: Lehrer RI, Cohen LE, Koeffler HP.
    Journal: Cancer Res; 1983 Aug; 43(8):3563-6. PubMed ID: 6574815.
    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.
    [Abstract] [Full Text] [Related] [New Search]