Cell surface interaction is sufficient for the biological activity of a bovine sialoglycopeptide inhibitor |
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| Authors: | B G Sharifi C C Bascom T C Johnson |
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| Institution: | 1. Faculty of Pharmaceutical Sciences, University of British Columbia, Vancouver, British Columbia, Canada;2. Department of Chemistry & Sarafan ChEM-H, Stanford University, Stanford, California, USA;3. Department of Biological Engineering, Massachusetts Institute of Technology, Boston, Massachusetts, USA;4. Department of Chemical Engineering, Massachusetts Institute of Technology, Boston, Massachusetts, USA;5. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Boston, Massachusetts, USA;6. Department of Chemistry, University of Washington, Seattle, Washington, USA;7. Howard Hughes Medical Institute, Stanford, California, USA;1. College of Food Science and Engineering, Henan University of Technology, Zhengzhou, 450001, PR China;2. Henan Key Laboratory of Cereal and Oil Food Safety Inspection and Control, Zhengzhou, Henan, 450001, PR China;1. Obstetrics and Gynaecology, Department of Obstetrics and Gynaecology, University of Thessaly, School of Health Sciences, Faculty of Medicine, 41110 Larissa, Greece;2. Embryology, Department of Obstetrics and Gynaecology, University of Thessaly, School of Health Sciences, Faculty of Medicine, 41110 Larissa, Greece;1. Department of Obstetrics and Gynecology, McGill University, 1001 Decarie Boulevard, Montreal, Quebec, Canada H4A 3J1;2. Department of Obstetrics and Gynecology, Division of Reproductive Endocrinology and Infertility, Western University, London, Ontario, Canada;3. Department of Obstetrics and Gynecology, University of Tabuk, Tabuk, Saudi Arabia;4. Department of Obstetrics and Gynecology, Division of Reproductive Endocrinology and Infertility, McGill University, Montreal, Quebec, Canada |
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| Abstract: | A sialoglycopeptide inhibitor, isolated from bovine cerebral cortex cells, that reversibly inhibits protein and DNA synthesis, was coupled to either Sepharose or polyacrylamide beads. Whereas over 1 ng of the inhibitor was released from Sepharose beads after 30 min at 37 degrees C, less than 0.2 ng of the sialoglycopeptide was released from the polyacrylamide beads. When added to 3T3 cells, the immobilized sialoglycopeptide efficiently inhibited protein synthesis. No detectable sialoglycopeptide inhibitor was released into the assay medium in the presence or absence of 3T3 cells. Addition of 125I]sialoglycopeptide, coupled to acrylamide P100 beads, to 3T3 cells also demonstrated that the sialoglycopeptide was not internalized by the cells. Thus we conclude that an interaction of the sialoglycopeptide at the cell surface is sufficient for biological inhibitory activity. |
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