TY - JOUR
T1 - Specific binding of phorbol esters to nuclei of human promyelocytic leukemia cells
AU - Kraft, A. S.
AU - Appling, C.
AU - Berkow, R. L.
N1 - Funding Information:
ACKNOWLEDGMENTS: This work was supported by the American Cancer Society BC 522 and National Institutes of Health Grants CA 42533 and AI 22048 (to A.S.K. and R.L.B.). Financial support for the purification of bryostatin at the Arizona State University Cancer Research Institute was provided by the F.E. Rippel Foundation, the Arizona Disease Control Commission, the R.B. Dalton Endowment Fund, and National Institutes of Health Grants CA 16049.
PY - 1987/4/14
Y1 - 1987/4/14
N2 - In this report, we demonstrate that HL-60 nuclei isolated in calcium but not EGTA containing buffers specifically bind PE and express approximately 37,000 receptor sites/nucleus. Nuclear phorbol ester binding is lost by isolation in the absence of calcium, but can be repleted by the addition of partially purified protein kinase C and calcium. When HL-60 cells are treated with bryostatin 1, a compound which activates protein kinase C in a similar fashion to phorbol esters but does not induce differentiation of HL-60 cells, and nuclei are isolated in the presence of EGTA, these nuclei continue to bind phorbol esters. These experiments suggest that HL-60 nuclei bind PE in vitro, and that comments that activate protein kinase C may increase nuclear binding of PE in situ.
AB - In this report, we demonstrate that HL-60 nuclei isolated in calcium but not EGTA containing buffers specifically bind PE and express approximately 37,000 receptor sites/nucleus. Nuclear phorbol ester binding is lost by isolation in the absence of calcium, but can be repleted by the addition of partially purified protein kinase C and calcium. When HL-60 cells are treated with bryostatin 1, a compound which activates protein kinase C in a similar fashion to phorbol esters but does not induce differentiation of HL-60 cells, and nuclei are isolated in the presence of EGTA, these nuclei continue to bind phorbol esters. These experiments suggest that HL-60 nuclei bind PE in vitro, and that comments that activate protein kinase C may increase nuclear binding of PE in situ.
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U2 - 10.1016/S0006-291X(87)80523-5
DO - 10.1016/S0006-291X(87)80523-5
M3 - Article
C2 - 3472520
AN - SCOPUS:0023216265
SN - 0006-291X
VL - 144
SP - 393
EP - 401
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -