The disposition of phentermine and its N-oxidized metabolic products in the rabbit. Precursor utilization of 5-hydroxytryptophan for 5-hydroxytryptamine biosynthesis in isolated and perfused rabbit and rat lungs. Lung surfactant-associated proteins and type IV collagen share common epitopes. An immunocytochemical demonstration. Ionamin online references

Ionamin online research references

Xenobiotica. 1978 Jan;8(1):55-60.
The disposition of phentermine and its N-oxidized metabolic products in the rabbit.

Beckett AH, Belanger PM.

1. When phentermine was injected intraperitoneally to rabbits, 77% of the dose was excreted in the urine within 2 days; N-oxidized metabolic products accounted for 62% dose. Major excretion products were N-hydroxyphentermine (28% dose), conjugated N-hydroxyphentermine (32% dose) and unchanged phentermine (16% dose). 2. Similarly injected N-hydroxyphentermine was excreted (62% dose) in the urine in 2 days; only 4% dose was recovered unchanged. Major routes of metabolism of N-hydroxyphentermine was conjugation (36% dose) and reduction to the parent amine (15% dose). Conditions for hydrolysis of urine to liberate N-hydroxyphentermine from its conjugates were studied; N-hydroxyphentermide decomposes in strong acid. 3. Only 10% of injected alpha, alpha-dimethyl-alpha-nitroso-beta-phenylethane was excreted in the urine in 2 days. 4. N-Oxidations is the major pathway of metabolism of phentermine in rabbits; the present results suggest that some biological activity may be mediated by the pharmacologically active N-hydroxyphentermine.

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=24306&dopt=Abstract

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Can J Physiol Pharmacol. 1987 Oct;65(10):2117-23.
Precursor utilization of 5-hydroxytryptophan for 5-hydroxytryptamine biosynthesis in isolated and perfused rabbit and rat lungs.

Prasada Rao KS, Mehendale HM.

Department of Pharmacology and Toxicology, University of Mississippi Medical Center, Jackson 39216-4505.

The present study was designed to investigate whether lungs can utilize 5-hydroxytryptophan (5-HTP), formed elsewhere and transported, for the synthesis of 5-hydroxytryptamine (5-HT). [14C]5-HTP uptake was 7.7 +/- 1.1 and 3.9 +/- 0.2% by rabbit and rat lungs, respectively, after 1 h of perfusion with 10 microM [14C]5-HTP. There was an increase in the lung uptake of [14C]5-HTP when the lungs were preperfused with 0.5 mM chlorphentermine (CP) and the uptake was low when the lungs were preperfused with 0.1 mM hydroxybenzylhydrazine dihydrochloride (HBH). The perfusate concentration of 5-hydroxyindole acetic acid (5-HIAA) increased significantly (3-4 micrograms/100 mL) during rabbit lung perfusion with 10 microM [14C]5-HTP and this did not change significantly when the lungs were preperfused with 0.5 mM CP. However, 5-HT increased with time in the perfusate. 5-HT, but not 5-HIAA, was detected in the perfusate and increased with time of perfusion when the rat lungs were perfused either with 10 microM 5-HTP or with 0.5 mM CP and 10 microM 5-HTP. However, no metabolites were detected in either the rabbit lung or rat lung perfusates when they were preperfused with 0.1 mM HBH. Lung contents of 5-HT and 5-HIAA were significantly higher in the rat lungs and only 5-HIAA increased in rabbit lungs after 1 h of perfusion with 10 microM 5-HTP. Preperfusion with 0.5 mM CP resulted in a greater increase in the 5-HT content of both rabbit and rat lungs.(ABSTRACT TRUNCATED AT 250 WORDS)

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2448021&dopt=Abstract

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Am Rev Respir Dis. 1989 Oct;140(4):1040-4.
Lung surfactant-associated proteins and type IV collagen share common epitopes. An immunocytochemical demonstration.

Coulombe PA, Bendayan M.

Department of Anatomy, Faculty of Medicine, Universite de Montreal, Quebec, Canada.

Among the surfactant-associated proteins (SP-A) characterized so far, there is a group of glycoproteins 26 to 34 kDa that features collagenlike sequences near their N-terminal end. We herein report the cross-reactivity of a rabbit polyclonal antibody to EHS tumor-derived type IV collagen towards rat SP-A. Rat lung tissues were processed for the localization of both type IV collagen and SP-A by high-resolution immunocytochemistry, applying the protein A-gold technique with specific antibodies. In addition to the various basal laminae of the pulmonary tissue, the antitype IV collagen antibody labeled the surfactant material found in alveolar spaces and macrophages, as well as in type II pneumocytes. The surfactant nature of the alveolar material labeled by the antiserum to type IV collagen was confirmed by the positive labeling obtained using an antibody to SP-A. This antibody labeled specifically the alveolar surfactant material, without binding any basal laminae. Several control experiments demonstrated the specificity of each labeling. These results were further supported by immunoblot experiments on nitrocellulose membrane. These findings thus provide further support to the existence of collagenlike sequences on SP-A, and further demonstrate that this structural similarity with collagens can lead to some cross-antigenicity.

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2478054&dopt=Abstract

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