Identification of the phorbol ester receptor in human and avian erythrocytes
The ability of phorbol esters to inhibit the uptake of a fluorescent glucose analogue in goose but not human erythrocytes is consistent with earlier reports that the human red blood cell lacks the phorbol ester receptor. However, they have located specific phorbol 12,13-dibutyrate binding sites in both human and goose erythrocytes. Human and goose red blood cells contain 2 classes of phorbol ester receptors with similar affinities, however the human erythrocyte contains 1/3 as many phorbol ester receptors as does the goose red blood cell. An additional contrast in the binding of phorbol esters to human and goose red blood cells is the temperature-induced enhancement of binding to goose, but not human erythrocytes. Equilibrium phorbol ester binding to goose red blood cells at 37/sup 0/C is enhanced 3.3 +/- 0.4 times that amount bound at 4/sup 0/C. Equilibrium binding of phorbol esters to human erythrocytes is identical at both temperatures. In vivo and in vitro phosphorylation profiles of C-kinase substrates also differ between the human and goose erythrocyte.
- Research Organization:
- Univ. of Virginia, Charlottesville
- OSTI ID:
- 6984912
- Report Number(s):
- CONF-8606151-
- Journal Information:
- Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 45:6; Conference: 76. annual meeting of the Federation of American Society for Experimental Biology, Washington, DC, USA, 8 Jun 1986
- Country of Publication:
- United States
- Language:
- English
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59 BASIC BIOLOGICAL SCIENCES
PHORBOL ESTERS
BIOCHEMICAL REACTION KINETICS
RECEPTORS
AFFINITY
EQUILIBRIUM
ERYTHROCYTES
GEESE
MAN
ANIMALS
BIOLOGICAL MATERIALS
BIRDS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARCINOGENS
ESTERS
FOWL
KINETICS
MAMMALS
MATERIALS
MEMBRANE PROTEINS
ORGANIC COMPOUNDS
PRIMATES
PROTEINS
REACTION KINETICS
VERTEBRATES
560300* - Chemicals Metabolism & Toxicology
550200 - Biochemistry