Partial purification and characterization of a binding protein for biologically active phorbol and ingenol esters from murine sera
We have purified a protein (Mr approximately 71,000) from murine sera 104-fold which directly binds biologically active phorbol esters, ingenol esters, and mezerein in a specific, reversible, and saturable manner. The binding of labeled phorbol-12,13-dibutyrate (PDBu) to the purified protein is rapi...
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Published in | The Journal of biological chemistry Vol. 257; no. 1; pp. 439 - 445 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
American Society for Biochemistry and Molecular Biology
01.01.1982
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Abstract | We have purified a protein (Mr approximately 71,000) from murine sera 104-fold which directly binds biologically active phorbol
esters, ingenol esters, and mezerein in a specific, reversible, and saturable manner. The binding of labeled phorbol-12,13-dibutyrate
(PDBu) to the purified protein is rapid and dose-dependent. Those phorbol and ingenol esters which stimulate cell growth in
culture and have tumor-promoting activity in vivo inhibit the binding of labeled PDBu, while the biologically inactive derivatives
fail to do so. Other nonditerpene tumor promoters, retinoids, steroids, and prostaglandins do not interfere with PDBu-protein
interaction. Epidermal growth factor, insulin, bovine serum albumin, hemoglobin, ovalbumin, ferritin, myoglobin, fetuin, and
lipase do not interact directly with PDBu. The purified binding protein competitively inhibits the binding of PDBu to its
specific receptors. It is nonglycosylated and slightly hydrophobic. The protein is heat- and acid-labile and is present in
sera of various mammalian species. Its concentration in murine sera is age-, sex-, and strain-independent. |
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AbstractList | We have purified a protein (Mr approximately 71,000) from murine sera 104-fold which directly binds biologically active phorbol
esters, ingenol esters, and mezerein in a specific, reversible, and saturable manner. The binding of labeled phorbol-12,13-dibutyrate
(PDBu) to the purified protein is rapid and dose-dependent. Those phorbol and ingenol esters which stimulate cell growth in
culture and have tumor-promoting activity in vivo inhibit the binding of labeled PDBu, while the biologically inactive derivatives
fail to do so. Other nonditerpene tumor promoters, retinoids, steroids, and prostaglandins do not interfere with PDBu-protein
interaction. Epidermal growth factor, insulin, bovine serum albumin, hemoglobin, ovalbumin, ferritin, myoglobin, fetuin, and
lipase do not interact directly with PDBu. The purified binding protein competitively inhibits the binding of PDBu to its
specific receptors. It is nonglycosylated and slightly hydrophobic. The protein is heat- and acid-labile and is present in
sera of various mammalian species. Its concentration in murine sera is age-, sex-, and strain-independent. The authors have purified a protein (Mr similar to 71,000) from murine sera 104-fold which directly binds biologically active phorbol esters, ingenol esters and mezerein in a specific, reversible, and saturable manner. The binding of labeled phorbol-12,13-dibutyrate (PDBu) to the purified protein is rapid and dose-dependent. Those phorbol and ingenol esters which stimulate cell growth in culture and have tumor-promoting activity in vivo inhibit the binding of labeled PDBu, while the biologically inactive derivatives fail to do so. Other nonditerpene tumor promoters, retinoids, steroids, and prostaglandins do not interfere with PDBu-protein interaction. Epidermal growth factor, insulin, bovine serum albumin, hemoglobin, ovalbumin, ferritin, myoglobin, fetuin, and lipase do not interact directly with PDBu. The purified binding protein competitively inhibits the binding of PDBu to its specific receptors. It is nonglycosylated and slightly hydrophobic. The protein is heat and acid-labile and is present in sera of various mammalian species. Its concentration in murine sera is age-, sex-, and strain-independent. We have purified a protein (Mr approximately 71,000) from murine sera 104-fold which directly binds biologically active phorbol esters, ingenol esters, and mezerein in a specific, reversible, and saturable manner. The binding of labeled phorbol-12,13-dibutyrate (PDBu) to the purified protein is rapid and dose-dependent. Those phorbol and ingenol esters which stimulate cell growth in culture and have tumor-promoting activity in vivo inhibit the binding of labeled PDBu, while the biologically inactive derivatives fail to do so. Other nonditerpene tumor promoters, retinoids, steroids, and prostaglandins do not interfere with PDBu-protein interaction. Epidermal growth factor, insulin, bovine serum albumin, hemoglobin, ovalbumin, ferritin, myoglobin, fetuin, and lipase do not interact directly with PDBu. The purified binding protein competitively inhibits the binding of PDBu to its specific receptors. It is nonglycosylated and slightly hydrophobic. The protein is heat- and acid-labile and is present in sera of various mammalian species. Its concentration in murine sera is age-, sex-, and strain-independent. |
Author | G J Todaro M Shoyab |
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Cites_doi | 10.1038/279387a0 10.1016/S0021-9258(19)52451-6 10.1007/BF02137733 10.1007/BF00525517 10.1111/1523-1747.ep12513451 10.1016/0003-9861(81)90084-9 10.1038/264446a0 10.1038/288451a0 10.1038/newbio243212a0 10.1073/pnas.74.2.657 10.1126/science.286421 10.1038/262402a0 10.3109/10408447309025704 10.1126/science.308698 10.1016/0006-291X(79)90221-3 10.1126/science.177.4053.949 10.1002/jcp.1040800203 10.1016/0009-2797(71)90001-9 10.1111/j.1749-6632.1977.tb41848.x 10.1073/pnas.75.8.4001 10.1016/S0006-291X(72)80182-7 10.1016/S0021-9258(18)43561-2 10.1159/000391388 10.1007/BF00531226 10.1016/0005-2760(72)90212-3 10.1002/jcp.1040870105 10.1002/jcp.1040820203 10.1038/259232a0 10.1073/pnas.77.1.567 10.1016/S0021-9258(17)30458-1 |
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Snippet | We have purified a protein (Mr approximately 71,000) from murine sera 104-fold which directly binds biologically active phorbol
esters, ingenol esters, and... We have purified a protein (Mr approximately 71,000) from murine sera 104-fold which directly binds biologically active phorbol esters, ingenol esters, and... The authors have purified a protein (Mr similar to 71,000) from murine sera 104-fold which directly binds biologically active phorbol esters, ingenol esters... |
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SubjectTerms | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Brain - metabolism Caenorhabditis elegans Proteins Carcinogens - metabolism Carrier Proteins Cell Membrane - metabolism Diterpenes - metabolism Fundamental and applied biological sciences. Psychology Humans Kinetics Mice Phorbol 12,13-Dibutyrate Phorbol Esters - metabolism phorbol-binding protein Phorbols - metabolism Protein Kinase C Proteins purification Receptors, Drug - isolation & purification Receptors, Drug - metabolism Species Specificity |
Title | Partial purification and characterization of a binding protein for biologically active phorbol and ingenol esters from murine sera |
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