Effects of sodium on cell surface and intracellular 3H-naloxone binding sites |
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| Authors: | A E Pollack G F Wooten |
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| Affiliation: | 1. Sarah Cannon Research Institute/Tennessee Oncology, Nashville, TN, USA;2. The Ohio State University Wexner Medical Center, James CCC, Columbus, OH, USA;3. Memorial Sloan Kettering Cancer Center and Weill Cornell Medical College, New York, NY, USA;4. City of Hope Comprehensive Cancer Center, Duarte, CA, USA;5. University of Chicago, Chicago, IL, USA;6. AbbVie Inc., South San Francisco, CA, USA;7. Oklahoma Cancer Center/Sarah Cannon Research Institute, University of Oklahoma, Oklahoma City, OK, USA;1. Hypertrophic Cardiomyopathy Center of Excellence, Johns Hopkins University, Baltimore, MD, USA;2. Division of General Medicine, Department of Medicine, Taipei Veterans General Hospital, Taipei, Taiwan;3. Institute of Public Health, National Yang-Ming University, Taipei, Taiwan;4. Hypertrophic Cardiomyopathy Center of Excellence, Division of Cardiology, University of California San Francisco, San Francisco, California;5. Department of Radiology, Johns Hopkins University, Baltimore, MD |
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| Abstract: | The binding of the opiate antagonist 3H-naloxone was examined in rat whole brain homogenates and in crude subcellular fractions of these homogenates (nuclear, synaptosomal, and mitochondrial fractions) using buffers that approximated intra- (low sodium concentration) and extracellular (high sodium concentration) fluids. Saturation studies showed a two-fold decrease in the dissociation constant (Kd) in all subcellular fractions examined in extracellular buffer compared to intracellular buffer. In contrast, there was no significant effect of the buffers on the Bmax. Thus, 3H-naloxone did not distinguish between binding sites present on cell surface and intracellular tissues in these two buffers. These results show that the "sodium effect" of opiate antagonist binding is probably not a function of altered selection of intra- and extracellular binding sites. |
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