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Biophysical and structural characterization of 1H-NMR-detectable mobile lipid domains in NIH-3T3 fibroblasts.
Biochim Biophys Acta
June 1999
Laboratory of Cell Biology, Istituto Superiore di Sanità, Viale Regina Elena, 299, 00161, Rome, Italy.
Nature and subcellular localization of 1H-NMR-detectable mobile lipid domains (ML) were investigated by NMR, Nile red fluorescence and electron microscopy, in NIH-3T3 fibroblasts and their H-ras transformants (3T3ras) transfected with a high number of oncogene copies. Substantial ML levels (ratio of (CH2)n/CH3 peak areas R=1. 56+/-0.
View Article and Find Full Text PDFLower levels of 1H MRS-visible mobile lipids in H-ras transformed tumorigenic fibroblasts with respect to their untransformed parental cells.
Cell Mol Biol (Noisy-le-grand)
July 1997
Laboratory of Cell Biology, Istituto Superiore di Sanità, Roma, Italy.
High resolution 1H MRS studies report increased mobile neutral lipid (MNL) signals in transformed and malignant as well as in some in vitro cultured embryonic cells. Nature, subcellular localization and biological function of MNL are still under debate. This work was aimed at assessing alterations induced in MNL signals of NIH-3T3 mouse embryo fibroblasts by transformation with human HJ-ras oncogene.
View Article and Find Full Text PDFStable transfection of provirus of human immunodeficiency virus into a murine packaging cell line.
Acta Virol
April 1997
Istituto Superiore di Sanità, Laboratorio di Virologia, Roma, Italy.
In order to generate HIV (murine leukemia virus (MuLV)) pseudotypes, HIV genome was transfected into the ecotropic murine packaging cell line (GP+E86) and four of the nine transfected clones were extensively characterized. One clone (801), harbouring a full copy of integrated HIV sequences, exhibited a detectable level of intracellular HIV p24 antigen expression. Northern blot analysis revealed that clone 801 expressed all three classes of HIV mRNAs.
View Article and Find Full Text PDFDetection of phosphatidylcholine-specific phospholipase C in NIH-3T3 fibroblasts and their H-ras transformants: NMR and immunochemical studies.
Anticancer Res
August 1996
Department of Cell Biology, Istituto Superiore di Sanità, Roma, Italy.
Although evidence supports constitutive activation of phosphatidylcholine specific phospholipase C (PC-plc) in rastransformed fibroblasts, no studies have been devoted to measure the basal activity levels of this enzyme, its molecular characteristics and subcellular localization. This paper reports for the first time measurements of the activity of different enzymes responsible for PC hydrolysis (PC-plc; phospholipases A2 (pla2) and A1 (pla1)) in homogenates of murine NIH-3T3 fibroblasts (3T3) and their transformants obtained by human H-ras transfection (3T3ras). To this end, 31P NMR analyses were carried out on total cell homogenates, incubated in the presence of mixed diheptanoylphosphatidylcholine: sphingomyelin (DHPC:SM) unilamellar vesicles (SLUV), in which DHPC acts as a suitable substrate for water-soluble lipolytic enzymes.
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