Cytosolic calcium regulates phorbol diester binding affinity in intact phagocytes.
نویسندگان
چکیده
منابع مشابه
Effect of cellular phospholipid modification on phorbol diester binding.
The influence of cellular lipid composition on the specific binding of [20-3H]phorbol-12,13-dibutyrate to intact human promyelocytic leukemia cells was investigated. Cellular phospholipid composition could be manipulated by culturing cells in serum-free, chemically defined media containing base analogues of phospholipid polar head groups. Human promyelocytic leukemia cells grown in the presence...
متن کاملPhorbol diester receptor copurifies with protein kinase C.
The phorbol diester receptor present in the particulate fraction of rat brain was solubilized by divalent ion chelation in the absence of detergents. The soluble receptor was partially purified by (NH4)2SO4 precipitation, DEAE-cellulose, and gel filtration chromatography. The purified receptor required exogenous phospholipid for activity and displayed a Kd of 7 nM for [3H]phorbol 12, 13-dibutyr...
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Activation of cellular protein kinase C appears to be involved in the mechanism by which phorbol diesters induce differentiation of human myeloid leukemia cells (HL-60). Protein kinase C is thought to be physiologically activated by diacylglycerol derived from receptor-mediated phosphatidylinositol hydrolysis. sn-1,2-diacylglycerols with short saturated acyl side chains (C4-C10) were synthesize...
متن کاملEffect of Cellular Phospholipid Modification on Phorbol Diester Binding1
The influence of cellular lipid composition on the specific binding of [20-3H]phorbol-12,13-dibutyrate to intact human promyelocytic leukemia cells was investigated. Cellular phospholipid composition could be manipulated by culturing cells in serumfree, chemically defined media containing base analogues of phospholipid polar head groups. Human promyelocytic leukemia cells grown in the presence ...
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The sarcoplasmic calcium-binding protein (SCP) from crayfish has in its dimer form two calcium-specific and four Ca-Mg sites. The conformations of this protein in the calcium(SCP2 *Cas), magnesium(SCP2 -Mg4), and metal-free forms as well as in intermediary states have been studied by circular dichroism (CD) in the far and near-ultraviolet regions, tryptophan fluorescence, sulfhydryl reactivity,...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)35628-4