By Charles R. Craig, Robert E. Stitzel
Development at the strengths of prior variations, the 6th variation of Modern Pharmacology with scientific Applications maintains to supply an up to date and finished textbook for college kids of pharmacology. targeting the medical program of substances inside of a context of the foremost ideas of pharmacology, this article provides either scholars and college with an creation to trendy pharmacotherapeutics.
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Extra info for Modern Pharmacology With Clinical Applications (6th Edition)
A second type of CYP enzyme inhibition is mechanism-based inactivation (or suicide inactivation). , Ritonavir), amiodarone, cimetidine, diltiazem, erythromycina, grapefruit juice, ketoconazole Thought to be same as CYP3A4 Unclear at this time but may be similar to CYP3A4 CYP2A6 CYP2B6 CYP2C8 CYP2C9 CYP2C19 CYP2D6 CYP2E1 CYP3A4 Regulation of the CYP Enzymes CYP450 enzymes can be regulated by the presence of other drugs or by disease states. This regulation can either decrease or increase enzyme function, depending on the modulating agent.
With respect to the drug inducer, drugs with a shorter halflife will reach equilibrium concentrations sooner (less time to steady state) and thus result in a more rapid maximal induction, with the opposite being true for drugs with a longer half-life. Flavin Monooxygenases The flavin monooxygenases (FMOs) are a family of five enzymes (FMO 1–5) that operate in a manner analogous to the cytochrome P450 enzymes in that they oxidize the drug compound in an effort to increase its elimination. Though they possess broad substrate specificity, in general they do not play a major role in the metabolism of drugs but appear to be more involved in the metabolism of environmental chemicals and toxins.
Thus, patients expressing both CYP3A4 and CYP3A5 have the potential to exhibit increased metabolism of CYP3A substrates as compared to individuals expressing only the CYP3A4 isoform. Levels of CYP enzyme expression of any isoform can vary substantially among individuals. The other identified human CYP3A isoform is CYP3A7, which appears to be expressed only in the fetus and rapidly disappears following birth, to be replaced by CYP3A4 and CYP3A5. It is becoming increasingly clear that different enzyme expression patterns, and thus different drug metabolism capabilities, are observed throughout the various stages of life.