Drugs online research references
Tumour Biol. 1991;12(2):99-110.
Prostaglandin E2 from macrophages of murine splenocyte cultures inhibits the generation of lymphokine-activated killer cell activity.
Ohnishi H, Lin TH, Nakajima I, Chu TM.
Department of Diagnostic Immunology Research and Biochemistry, Roswell Park Memorial Institute, Buffalo, N.Y.
The present work investigated the association between prostaglandin E2 (PGE2) from macrophages and its inhibition of murine lymphokine-activated killer (LAK) cell generation. The coculture of indomethacin with interleukin-2 (IL-2) augmented LAK cell activity in an indomethacin dose-response manner, and diminished PGE2 content in the corresponding culture supernatant in a reverse dose-response manner. The correlation between the increase in LAK cell activity and the decrease in PGE2 content was highly significant. Identical results were obtained with diclofenac. A profound inhibition of LAK cell activity by exogenous PGE2 in a dose-response manner was detected. Polyclonal anti-PGE2 antiserum augmented in a dose-dependent manner the LAK cell activity, by neutralizing PGE2 in the medium. A reduction of PGE2 content in the culture supernatant was also detected when the macrophage subpopulations were cultured and was indomethacin dose-dependent. In comparison with that of normal mouse splenocytes, the incubation of whole splenocytes of tumor-bearing mice, which contained a greater subpopulation of macrophages (24% vs. 12%), produced a greater PGE2 content and a correspondingly depressed LAK cell activity. Additionally, PGE2 reduced protein kinase C (PKC) activity along with LAK cell activity generated from macrophage-depleted T cells and natural-killer-like cells. These results overall indicate that PGE2 from macrophages in murine splenocyte cultures inhibits the LAK cell generation, and PKC may be involved in the inhibition mechanism.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2028183&dopt=Abstract
Br J Clin Pharmacol. 1988 Jul;26(1):107-9.
The binding of drugs to major human milk whey proteins.
Atkinson HC, Begg EJ.
Department of Clinical Pharmacology, Christchurch School of Medicine, Christchurch Hospital, New Zealand.
The binding of nine drugs of diverse physicochemical characteristics to major human milk whey proteins is reported. This group included acids, bases and neutral drugs. No drug bound to alpha-lactalbumin, which is the protein present in greatest concentrations in mature milk. Four drugs, diclofenac, phenytoin, prednisolone and warfarin, bound to albumin but to a much lesser extent than in plasma, consistent with quantitatively less albumin in milk. None of the basic drugs studied bound to albumin. Five drugs, atenolol, diclofenac, prednisolone, propranolol and warfarin, bound to lactoferrin though the extent was minimal except for diclofenac. This group included acids, bases and neutral drugs.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3203054&dopt=Abstract
Life Sci. 1994;54(14):951-6.
Selective inhibition of major drug metabolizing cytochrome P450 isozymes in human liver microsomes by carbon monoxide.
Leemann T, Bonnabry P, Dayer P.
Department of Medicine, University Hospital, Geneva, Switzerland.
The selectivity of carbon monoxide binding to specific human cytochrome P450 isozymes was investigated by studying its inhibition of prototype reactions for 3 major drug metabolizing P450s in liver microsomes: dextromethorphan O-demethylation and (+)-bufuralol 1'-hydroxylation (P450DB1, CYP2D6), diclofenac 4'-hydroxylation (P450TB, CYP2C subfamily), and midazolam 1'-hydroxylation (P450NF, CYP3A subfamily). The affinity of carbon monoxide is different for each P450 isozyme. Warburg partition coefficients were 0.35, 1.1 and 3.9 microM for P450DB1, P450TB and P450NF, respectively. Differential inhibition by carbon monoxide may be a useful tool to identify specific human cytochrome P450 isozymes in the early screening of drug biotransformation catalysts. Further studies involving other P450 isozymes and substrates should extend our understanding of the phenomena and their implications.
online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8139385&dopt=Abstract
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