Biomedical subjects

V Moravec

Publications and source records attributed to V Moravec.

10 recordsLinked to original sources

PubMed2002

Effects of alprazolam and fluoxetine on morphine sensitization in mice.

Benzodiazepines seem to be frequently abused in conjunction with opioids. Fluoxetine was reported to block morphine locomotor sensitization in rats. Sensitization has been implicated in some aspects of drug abuse. We have investigated the effect of alprazolam (0.25 mg/kg) and fluoxetine (5 mg/kg) on the development and expression of sensitization to the locomotor stimulant effect of morphine (10 mg/kg) in mice. Sensitization was produced by daily injections of morphine (10 mg/kg) for 10 days. There was a clear sensitization of locomotor activity produced by morphine in photocell activity cages but co-administration of alprazolam with morphine had no effect on the degree of sensitization. Alprazolam was also without effect on the expression of the sensitized response to morphine in mice sensitized with morphine alone. Fluoxetine partly reduced both the development and expression of morphine sensitization. In conclusion, the present experiments have not yielded evidence that alprazolam may influence the development or the expression of sensitization to morphine. However, they have corroborated and extended results indicating that fluoxetine can attenuate, to a certain level, the development and expression of morphine sensitization.

Alprazolam↗

PubMed1996

Improved method for rapid purification of protein kinase from streptomycetes.

Protein kinase from Streptomyces lincolnensis was purified nearly to homogeneity using a high performance liquid chromatography (HPLC) and a Pharmacia FPLC system. The procedure used employed column chromatography on DE-53, followed by FPLC affinity chromatography with serine- or threonine-Sepharose (prepared as described in this paper) and gel filtration using a Superose 12 or TSK G3000SW column. Starting with 3.5 g of mycelial proteins, approximately 1 mg of pure enzyme was obtained. The procedure is simple and highly reproducible. The protein kinase thus obtained was nearly pure by silver staining after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified protein kinase phosphorylated substrate proteins at the seryl residues.

Bacterial Proteins↗

PubMed1993

Peripheral membrane molecules of leukocytes and NK cytotoxicity.

Some leukocyte effector cell-surface molecules movement toward the adjoining target cells takes place during the reaction of NK cytotoxicity (NK R). The majority of the moving molecules are usually anchored via a divalent-ion-dependent interaction (PMM-M2+). The released PMM-M2+ can interact also with the secreted tumor necrosis factor alfa (TNF-alpha). In agreement with PMM-M2+ movement, the number of TNF-alpha binding sites on the target cell surface increases during NK R. In addition, antibodies against PMM-M2+, as well as D-mannose- or N-acetyl-D-glucosamine-terminated oligosaccharides of PMM-M2+ inhibit NK R. A more detailed analysis of PMM-M2+ with monoclonal antibodies used flow cytometry and cell-surface biotinylation. Only 3 of 31 tested CD antigens (CD2, LAK-1 and CD45) were passed through this first strongly restricted experimental screening. The EDTA-released LAK-1 antigen, but not CD2 and CD45, interact with TNF-alpha and cell surface via a mannose-inhibitable interaction dependent on the presence of Ca2+ ions. The mechanism of possible participation of PMM-M2+ in cytotoxic events is discussed in relation to Ca2+ influx and subsequent cytolysin secretion.

Antibody-Dependent Cell Cytotoxicity↗

PubMed1977