A High Molecular Weight Component of the Human Tumor Necrosis Factor Receptor is Associated with Cytotoxicity
We compared the molecular structure of the receptor to human recombinant tumor necrosis factor (HurTNF) on cells of different tissue origin that differ in their response to one of the known activities of TNF. We studied (i) tumor cell lines that respond to the cytotoxic action of TNF and resistant v...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 84; no. 10; pp. 3293 - 3297 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
National Academy of Sciences of the United States of America
01.05.1987
National Acad Sciences |
Subjects | |
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Abstract | We compared the molecular structure of the receptor to human recombinant tumor necrosis factor (HurTNF) on cells of different tissue origin that differ in their response to one of the known activities of TNF. We studied (i) tumor cell lines that respond to the cytotoxic action of TNF and resistant variants that bind TNF, (ii) normal cell lines that are stimulated to proliferate by TNF and those that are not affected by TNF, and (iii) peripheral blood granulocytes whose activation is also augmented by TNF. Using125I-labeled HurTNF, we found that it bound mainly to four cellular polypeptides (138, 90, 75, and 54 kDa), three of which were found in every cell type examined and one (138 kDa) that was observed only in a human breast carcinoma cell line (MCF-7) that is highly responsive to the cytotoxic action of TNF. The 138-kDa polypeptide was not found in resistant variants of MCF-7 that bind TNF. In contrast to the other polypeptides, the 138-kDa protein was detected 30 min after incubation at 4 degrees C, as compared to 5 min. Scatchard analysis and cross-linking data suggest a model for the TNF receptor structure whereby the receptor is composed of noncovalently linked membrane-bound polypeptides that bind TNF with high affinity (Kd, 0.05-0.8 × 10-9M) with the 138-kDa protein being the least abundant and/or even absent in most cells. |
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AbstractList | We compared the molecular structure of the receptor to human recombinant tumor necrosis factor (HurTNF) on cells of different tissue origin that differ in their response to one of the known activities of TNF. We studied tumor cell lines that respond to the cytotoxic action of TNF and resistant variants that bind TNF, normal cell lines that are stimulated to proliferate by TNF and those that are not affected by TNF, and peripheral blood granulocytes whose activation is also augmented by TNF. Using 125I-labeled HurTNF, we found that it bound mainly to four cellular polypeptides (138, 90, 75, and 54 kDa), three of which were found in every cell type examined and one (138 kDa) that was observed only in a human breast carcinoma cell line (MCF-7) that is highly responsive to the cytotoxic action of TNF. The 138-kDa polypeptide was not found in resistant variants of MCF-7 that bind TNF. In contrast to the other polypeptides, the 138-kDa protein was detected 30 min after incubation at 4 degrees C, as compared to 5 min. Scatchard analysis and cross-linking data suggest a model for the TNF receptor structure whereby the receptor is composed of noncovalently linked membrane-bound polypeptides that bind TNF with high affinity (Kd, 0.05-0.8 X 10(-9) M) with the 138-kDa protein being the least abundant and/or even absent in most cells. We compared the molecular structure of the receptor to human recombinant tumor necrosis factor (HurTNF) on cells of different tissue origin that differ in their response to one of the known activities of TNF. We studied (i) tumor cell lines that respond to the cytotoxic action of TNF and resistant variants that bind TNF, (ii) normal cell lines that are stimulated to proliferate by TNF and those that are not affected by TNF, and (iii) peripheral blood granulocytes whose activation is also augmented by TNF. Using125I-labeled HurTNF, we found that it bound mainly to four cellular polypeptides (138, 90, 75, and 54 kDa), three of which were found in every cell type examined and one (138 kDa) that was observed only in a human breast carcinoma cell line (MCF-7) that is highly responsive to the cytotoxic action of TNF. The 138-kDa polypeptide was not found in resistant variants of MCF-7 that bind TNF. In contrast to the other polypeptides, the 138-kDa protein was detected 30 min after incubation at 4 degrees C, as compared to 5 min. Scatchard analysis and cross-linking data suggest a model for the TNF receptor structure whereby the receptor is composed of noncovalently linked membrane-bound polypeptides that bind TNF with high affinity (Kd, 0.05-0.8 × 10-9M) with the 138-kDa protein being the least abundant and/or even absent in most cells. |
Author | Vitt, Charles R. Creasey, Abla A. Yamamoto, Ralph |
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Keywords | Human Cytotoxicity Tumor Property structure relationship Tumor necrosis factor Established cell line |
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SubjectTerms | Biological and medical sciences Carcinoma Cell growth Cell Line Cell lines Cell physiology Cell Survival Cells Cellular receptors Fibroblasts Fundamental and applied biological sciences. Psychology Glycoproteins - genetics Glycoproteins - metabolism Granulocytes Growth Inhibitors - metabolism Humans Kinetics Molecular and cellular biology Molecular Weight Receptors Receptors, Cell Surface - metabolism Receptors, Cell Surface - physiology Receptors, Tumor Necrosis Factor Recombinant Proteins - metabolism Responses to growth factors, tumor promotors, other factors Tumor cell line Tumor necrosis factor receptors Tumor Necrosis Factor-alpha |
Title | A High Molecular Weight Component of the Human Tumor Necrosis Factor Receptor is Associated with Cytotoxicity |
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