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V K Jansons

Publications and source records attributed to V K Jansons.

11 recordsLinked to original sources
PubMed1983

Liposomes as a means to introduce fragment A of diphtheria toxin into cells.

The incorporation of fragment A of diphtheria toxin into liposomes is described. The intracellular delivery of the entrapped toxin, as evidenced by the inhibition of protein synthesis by a human lymphoblastoid cell line could be demonstrated with liposomes that contained phosphatidylethanolamine or phosphatidylserine in addition to phosphatidylcholine and cholesterol. Free fragment A, either alone or added to empty liposomes of any composition, did not affect protein synthesis, even when present in considerably higher concentrations than the liposome-entrapped form.

Cell Line↗
PubMed1979

Control of in vitro cytotoxicity of positively charged liposomes.

The parameters which influence the in vitro cytotoxicity of positively charged liposomes for L 1210 cells were analyzed. The cytotoxicity was liposome/cell ratio-dependent. It also depended upon the mole fractions of stearylamine (SA) to phosphatidylcholine (PC). There was no difference between the cytotoxicity of unilamellar and multilamellar vesicles but the cytotoxic effect of free SA was about 4 times greater than that of liposome incorporated SA at a molar ratio of 1:4, SA:PC, respectively. The process which resulted in cell death was irreversible after 60 min of cell-liposome contact. The simultaneous presence of neutral liposomes or of positively charged liposomes with a lesser charge density decreased the cytotoxic effect of liposomes with a higher SA content. The cytotoxicity could be decreased by trypsinization of cells following exposure to liposomes while treatment of cells with trypsin prior to the exposure to positively charged liposomes had no effect on the subsequent cytotoxicity. The cytotoxicity was also decreased if cells were incubated in the presence of sodium azide. The usual concentration of serum (10%) present in the growth medium had no effect on the cytotoxicity while preincubation of cells with liposomes in 80% serum resulted in full protection. The protective effect of serum could be replaced by the albumin fraction.

Amines↗
PubMed1978

In vitro interaction of L1210 cells with phospholipid vesicles.

The in vitro uptake of phospholipid vesicles by mouse leukemia L1210 cells was examined. Liposomes were generated by prolonged ultrasonic dispersion of aqueous dispersions of mixed lipids in the presence of radiolabeled inulin. Multilamellar vesicles were separated from unilamellar vesicles by column chromatography. Vesicle populations were examined by electron microscopy. Neutral vesicles were generated from egg yolk phosphatidylcholine and cholesterol, and surface charge was introduced via either phosphatidylserine or octadecylamine. Uptake, measured as cell-associated radioactivity, was temperature dependent and was strongly decreased by metabolic inhibitors. These results suggested that liposomes are taken up to a major extent by an energy-dependent mechanism. The uptake of liposomes by cells of a young culture was about 2-fold higher than was the uptake of liposomes by cells of a stationary culture. The uptake of positively charged liposomes by cells was about 20-fold higher than that of either neutral or negatively charged vesicles. About one-half of the cell-associated radioactivity transferred by positively charged liposomes could be removed by cell surface treatment with trypsin or neuraminidase or by a short exposure to 0.6 N NaCl.

Animals↗
PubMed1977

The effect of temperature on concanavalin A-mediated agglutination of cells with rigid receptors.

The agglutination of a yeast, Candida albicans, by concanavalin A has been described. The agglutination was cell-number dependent. Prolonged incubation (60 min) was needed to reach maximum agglutination at 37 degrees C. The rate but not the extent of agglutination was temperature dependent. The dimeric forms of concanavalin A, obtained either at low pH or after succinylation, agglutinated the yeast cells as well as the tetramer. Temperature changes affected the agglutination of yeast cells by dimers and by tetramers to the same extent.

Agglutination Tests↗
PubMed1975

Lectin-receptor interactions in liposomes.

The major sialoglycoprotein of mammalian erythrocytes has been incorporated into phosphatidylcholine membranes to generate a model system, glycoprotein-liposomes. Electron microscopic examination revealed these structures to be vesicles, approximately 300 A in diameter. An aqueous compartment inside the glycoprotein-liposomes has been identified by trapped volume studies with [14C]sucrose. These glycoprotein-liposomes were found to interact with the lectins, wheat germ agglutinin, and phytohemagglutinin, to form aggregates of mainly unfused vesicles. The aggregation process has been studied by electron microscopy, 90 degrees light scattering, and differential ultracentrifugation analysis. Hapten inhibitors of the lectins were found to inhibit the lectin-induced aggregation of the glycoprotein-liposomes. Binding of 125I-labeled wheat germ agglutinin to glycoprotein-liposomes was studied by differential ultracentrifugation. Hapten inhibitors of wheat germ agglutinin were also found to inhbit the binding of 125I-labled wheat germ agglutinin to the glycoprotein-liposomes. The characteristics of the lectin interactions with glycoprotein-liposomes appeared to be phenomenologically similar to lectin-cell interactions.

Acetylglucosamine↗
PubMed1970

Induction, morphogenesis, and germination of the chlamydospore of Candida albicans.

Early log phase yeast cells of Candida albicans transformed into suspensor cells and chlamydospores when streaked on washed agar without added nutrients. The transformation was apparently a result of endogenous metabolism since starved yeast cells did not form chlamydospores. Addition of glucose (5 mg/ml) to washed agar completely suppressed chlamydospore formation. Size of inoculum and age of inoculum markedly affected chlamydospore yield. Electron microscopy of thin sections revealed the chlamydospore wall to be double layered, the outer thin layer being continuous with the wall of the suspensor cell. A technique was devised to study germination of chlamydospores. Chlamydospores germinated by budding, and the fluorescent antibody technique was used to study the budding process.

Amino Acids↗
PubMed1970

Chemical composition of chlamydospores of Candida albicans.

A variety of analytical techniques was employed to study the composition of the chlamydospore of Candida albicans. The outer, thin, electron-transparent layer was found to be composed of glucan, together with a small amount of chitin. The inner, thick, electron-dense layer is proteinaceous. The central structure is composed largely of ribonucleic acid and lipid globules. In addition to being acid-fast, the chlamydospore was found to contain glycolipids and to lose the property of acid-fastness on extraction with ethanol-ether.

Amino Acids↗
PubMedDate not supplied

Diphtheria toxin sensitivity in a monochromosomal hybrid containing human chromosome 5.

Among the mouse-human hybrids prepared in our laboratory one clone was found to contain only human chromosome 5 with an integrated selectable marker. This monochromosomal hybrid was used to investigate different aspects related to the toxicity of diphtheria toxin (DT). The hybrid was as sensitive to diphtheria toxin as the human donor cells. The protective effect of NH4Cl against diphtheria toxin could be demonstrated in the hybrid and also in the mouse and human cell lines. The reversal of the protective NH4Cl effect at acid pH also could be demonstrated in all three cell types. Incubation of cells with 125I-diphtheria toxin at 37 degrees C in the presence of methylamine showed a time-dependent increase in specific association in the human and the hybrid but not in the mouse cell line. The results obtained for the first time on a stable monochromosomal hybrid suggest that chromosome 5 is both necessary and sufficient for the expression of DT sensitivity.

Ammonium Chloride↗