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Title: Heterogeneity of (TH)phorbol 12,13-dibutyrate binding in primary mouse keratinocytes at different stages of maturation

Abstract

Mouse keratinocytes respond heterogeneously to phorbol esters with distinct subpopulations stimulated to proliferate or induced to differentiate. The maturation state of the epidermal cell at the time of exposure may determine its response. The binding of phorbol esters to primary mouse keratinocytes was studied under culture conditions selecting for proliferating cells or differentiating cells. (20-TH)-12-Deoxyphorbol 13-isobutyrate ((TH)-DPB) bound to both types of cells at one class of binding sites. The dissociation constant (Kd) for (TH)DPB in the proliferative cells was 69 nM and the binding at saturation (Bmax) was 1.3 pmol/mg of protein. The corresponding values in the differentiative cells were 96 nM and 1.5 pmol/mg of protein, respectively. In contrast to the results obtained with (TH)DPB, (20-TH)phorbol 12,13-dibutyrate ((TH)PDBU) bound to both cell types in a heterogeneous fashion. The site for (TH)DPB binding seemed to correspond to the higher affinity (TH)PDBU binding site. The major difference in the cells grown in the medium containing 1.2 mM CaCl2 was an increase in the Bmax of the lower affinity binding site with the other three parameters remaining similar. The state of epidermal differentiation thus appears to modulate the amount of the lower affinity binding sites for phorbol esters.

Authors:
; ; ;
Publication Date:
Research Org.:
National Cancer Institute, Bethesda, MD
OSTI Identifier:
6297673
Resource Type:
Journal Article
Journal Name:
Cancer Res.; (United States)
Additional Journal Information:
Journal Name: Cancer Res.; (United States)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ANIMAL CELLS; CONFIGURATION INTERACTION; PHORBOL ESTERS; CALCIUM; CELL DIFFERENTIATION; KERATIN; KINETICS; MICE; SKIN; TRITIUM COMPOUNDS; ALKALINE EARTH METALS; ANIMALS; BODY; CARCINOGENS; ELEMENTS; ESTERS; LABELLED COMPOUNDS; MAMMALS; METALS; ORGANIC COMPOUNDS; ORGANS; PROTEINS; RODENTS; SCLEROPROTEINS; VERTEBRATES; 550301* - Cytology- Tracer Techniques

Citation Formats

Dunn, J A, Jeng, A Y, Yuspa, S H, and Blumberg, P M. Heterogeneity of (TH)phorbol 12,13-dibutyrate binding in primary mouse keratinocytes at different stages of maturation. United States: N. p., 1985. Web.
Dunn, J A, Jeng, A Y, Yuspa, S H, & Blumberg, P M. Heterogeneity of (TH)phorbol 12,13-dibutyrate binding in primary mouse keratinocytes at different stages of maturation. United States.
Dunn, J A, Jeng, A Y, Yuspa, S H, and Blumberg, P M. 1985. "Heterogeneity of (TH)phorbol 12,13-dibutyrate binding in primary mouse keratinocytes at different stages of maturation". United States.
@article{osti_6297673,
title = {Heterogeneity of (TH)phorbol 12,13-dibutyrate binding in primary mouse keratinocytes at different stages of maturation},
author = {Dunn, J A and Jeng, A Y and Yuspa, S H and Blumberg, P M},
abstractNote = {Mouse keratinocytes respond heterogeneously to phorbol esters with distinct subpopulations stimulated to proliferate or induced to differentiate. The maturation state of the epidermal cell at the time of exposure may determine its response. The binding of phorbol esters to primary mouse keratinocytes was studied under culture conditions selecting for proliferating cells or differentiating cells. (20-TH)-12-Deoxyphorbol 13-isobutyrate ((TH)-DPB) bound to both types of cells at one class of binding sites. The dissociation constant (Kd) for (TH)DPB in the proliferative cells was 69 nM and the binding at saturation (Bmax) was 1.3 pmol/mg of protein. The corresponding values in the differentiative cells were 96 nM and 1.5 pmol/mg of protein, respectively. In contrast to the results obtained with (TH)DPB, (20-TH)phorbol 12,13-dibutyrate ((TH)PDBU) bound to both cell types in a heterogeneous fashion. The site for (TH)DPB binding seemed to correspond to the higher affinity (TH)PDBU binding site. The major difference in the cells grown in the medium containing 1.2 mM CaCl2 was an increase in the Bmax of the lower affinity binding site with the other three parameters remaining similar. The state of epidermal differentiation thus appears to modulate the amount of the lower affinity binding sites for phorbol esters.},
doi = {},
url = {https://www.osti.gov/biblio/6297673}, journal = {Cancer Res.; (United States)},
number = ,
volume = ,
place = {United States},
year = {Fri Nov 01 00:00:00 EST 1985},
month = {Fri Nov 01 00:00:00 EST 1985}
}