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J Yu, ER Butelman, JH Woods, BT Chait and MJ Kreek
Laboratory of Biology of Addictive Disease, Rockefeller University, New York, New York, USA.
Dynorphin A (1-17) [Dyn A (1-17)] is an endogenous opioid peptide. In vitro biotransformation of Dyn A (1-17) in human and rhesus monkey blood was studied by matrix-assisted laser desorption/ionization mass spectrometry. Biotransformation was observed to produce various opioid and nonopioid dynorphin A peptides. In this study, in vitro Dyn A (1- 17) biotransformation at physiological temperature (37 degrees C) was found to be very similar in human and rhesus monkey blood, although Dyn A (1-17) processing occurred at a faster rate in vitro in monkey blood than in human blood. One dominant pathway in this biotransformation was the slow removal of tyrosine at position one from Dyn A (1-17) to yield the dominant product, Dyn A (2-17). Further slow biotransformation of Dyn A (2-17) also occurred. Another major pathway of Dyn A (1-17) biotransformation is cleavage of the peptide linkage between Arg(6) and Arg(7) to produce the opioid peptide, Dyn A (1-6), and the nonopioid peptide, Dyn A (7-17). These two peptides had a short lifetime in blood, undergoing rapid biotransformation. Our results indicate that the rhesus monkey may be a good model for further in vivo pharmacological and neurobiological studies.
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M. J. Kreek, J. Schluger, L. Borg, M. Gunduz, and A. Ho Dynorphin A1-13 Causes Elevation of Serum Levels of Prolactin Through an Opioid Receptor Mechanism in Humans: Gender Differences and Implications for Modulation of Dopaminergic Tone in the Treatment of Addictions J. Pharmacol. Exp. Ther., January 1, 1999; 288(1): 260 - 269. [Abstract] [Full Text]
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J. Yu, E. R. Butelman, J. H. Woods, B. T. Chait, and M. J. Kreek Dynorphin A (1-8) Analog, E-2078, Is Stable in Human and Rhesus Monkey Blood J. Pharmacol. Exp. Ther., March 1, 1997; 280(3): 1147 - 1151. [Abstract] [Full Text]
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