Phospholipidosis in the alveolar macrophage induced by cationic amphiphilic drugs. Kinetic isotope effects in cytochrome P-450-catalyzed oxidation reactions. Intermolecular and intramolecular deuterium isotope effects during the N-demethylation of N,N-dimethylphentermine. N-oxidation of phentermine to N-hydroxyphentermine by a reconstituted cytochrome P-450 oxidase system from rabbit liver. Ionamin online references

Ionamin online research references

Fed Proc. 1984 Aug;43(11):2578-81.
Phospholipidosis in the alveolar macrophage induced by cationic amphiphilic drugs.

Reasor MJ.

The administration of a number of cationic amphiphilic drugs to certain species of laboratory animals results in a phospholipid storage disorder in the lungs. The alveolar macrophage (AM) shows a pronounced response to drug treatment. The most thorough quantification of this response has occurred after chlorphentermine treatment of rats. There is a striking increase in the accumulation of AMs in the alveolar spaces. The accumulated cells are very heterogeneous in size with many being larger than AMs from untreated rats. Cells are present that have a volume 10 times larger than normal AMs. The hypertrophic AMs show striking ultrastructural changes. The cells become engorged with lamellar inclusions, which may give rise to larger quantities of granular or membranous material. The affected AMs show an increase in total phospholipid content, and there is a good correlation between the size of the AM and its level of phospholipid. The phospholipidosis is reversible after termination of drug treatment; however, the above-mentioned changes do not return to control levels at the same time.

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6745447&dopt=Abstract

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J Biol Chem. 1980 Jul 10;255(13):6049-54.
Kinetic isotope effects in cytochrome P-450-catalyzed oxidation reactions. Intermolecular and intramolecular deuterium isotope effects during the N-demethylation of N,N-dimethylphentermine.

Miwa GT, Garland WA, Hodshon BJ, Lu AY, Northrop DB.

Two N,N-dimethylphentermine (N,N-dimethyl-2-amino-2-methyl-3-phenylpropane) substrates differing in deuterium substitution have been used to determine the intermolecular and intramolecular isotope effects associated with the cytochrome P-450-dependent N-demethylation of this substrate. No intermolecular isotope effect was observed in Vmax or Vmax/Km when the reaction rates for this substrate were compared to those for the substrate in which both N-methyl groups contained deuterium. In contrast, identical isotope effects of 1.6 to 2.0 were observed in both Vmax and Vmax/Km when this reaction was studied with a substrate in which only one of the two N-methyl groups was substituted with deuterium. Furthermore, both the intermolecular and intramolecular isotope effects were independent of the cytochrome P-450/NADPH-cytochrome P-450 reductase mole ratio. From these data, it is concluded that: 1) the carbon-hydrogen bond cleavage step does not contribute significantly to Vmax; 2) the contribution of the carbon-hydrogen bond cleavage step to Vmax is not detectably increased through changes in the cytochrome P-450/NADPH-cytochrome P-450 reductase mole ratio; 3) the N-methyl groups are free to exchange at the enzyme active site. The basis for these conclusions is the proposal of a new kinetic model for interpretation of intramolecular isotope effects which shows that intramolecular isotope effects are not necessarily equal to intrinsic isotope effects and, in fact, may be much smaller.

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6771263&dopt=Abstract

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Mol Pharmacol. 1982 Sep;22(2):235-8.
N-oxidation of phentermine to N-hydroxyphentermine by a reconstituted cytochrome P-450 oxidase system from rabbit liver.

Duncan JD, Cho AK.

Previous studies in our laboratory have indicated that the cytochrome P-450 system is involved in the oxidation of phentermine (2-methyl-1-phenyl-2-aminopropane) to N-hydroxyphentermine by liver microsomal preparations. In the present study, a reconstituted system which consisted of cytochrome P-450 and NADPH cytochrome P-450 reductase purified from liver microsomes of phenobarbital-induced rabbits was found to oxidize phentermine to N-hydroxyphentermine. The reaction was NADPH-dependent and required the presence of both the cytochrome P-450 and reductase preparations. N-Hydroxyphentermine was formed 3 times more rapidly in incubation mixtures which contained dilauroyl phosphatidylcholine than in those without added phospholipid. The reaction was inhibited several-fold by octylamine. It is concluded that the cytochrome P-450 system is able to catalyze the oxidation of phentermine to N-hydroxyphentermine.

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6815477&dopt=Abstract

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