Membrane-bound neomycin phosphotransferase confers drug-resistance in mammalian cells: A marker for high-efficiency targeting of genes encoding secreted and cell-surface proteins

1994 ◽  
Vol 20 (3) ◽  
pp. 153-162 ◽  
Author(s):  
William A. Mohler ◽  
Helen M. Blau
Keyword(s):  
Drug Resistance ◽  
Cell Surface ◽  
Mammalian Cells ◽  
High Efficiency ◽  
Surface Proteins ◽  
Neomycin Phosphotransferase ◽  
Cell Surface Proteins ◽  
Genes Encoding ◽  
Membrane Bound

Detection and Quantification of β2AR Internalization in Living Cells Using FAP-Based Biosensor Technology

2010 ◽  
Vol 15 (6) ◽  
pp. 703-709 ◽  
Author(s):  
Gregory W. Fisher ◽  
Sally A. Adler ◽  
Margaret H. Fuhrman ◽  
Alan S. Waggoner ◽  
Marcel P. Bruchez ◽  
...  
Keyword(s):  
Cell Surface ◽  
Adrenergic Receptor ◽  
High Throughput Screening ◽  
Mammalian Cells ◽  
Living Cells ◽  
Surface Proteins ◽  
Receptor Internalization ◽  
Cell Interior ◽  
Cell Surface Proteins ◽  
Signaling Systems

Ligand-dependent receptor internalization is a feature of numerous signaling systems. In this article, the authors describe a new kind of live-cell biosensor of receptor internalization that takes advantage of fluorogen-activating protein (FAP) technology. Recombinant genes that express the human beta2 adrenergic receptor (β2AR) with FAP domains at their extracellular N-termini were transduced into mammalian cells. Exposure of the cells to membrane-impermeant fluorogens led to a strong fluorescent signal from the cell surface. Agonist-dependent translocation of the receptor from the surface to the cell interior was readily observed and quantified by fluorescence microscopy or flow cytometry in a homogeneous format without wash or separation steps. The approach described here is generalizable to other receptors and cell surface proteins and is adaptable to a variety of fluorescence-based high-throughput screening platforms.

scholarly journals CELL SURFACE PROTEINS OF CRYPTOCOCCUS NEOFORMANS MEDIATE ADHERENCE AND INTERNALISATION INTO MAMMALIAN CELLS

2019 ◽  
Vol 22 (2) ◽  
pp. 24-30
Author(s):  
Khi Khi Choo ◽  
Voon Kin Chin ◽  
Pei Pei Chong ◽  
Siong Hock Ho ◽  
Voon Chen Yong
Keyword(s):  
Cell Surface ◽  
Cryptococcus Neoformans ◽  
Mammalian Cells ◽  
Surface Proteins ◽  
Cell Surface Proteins

The role of cell surface proteins gene expression in diagnosis, prognosis, and drug resistance of colorectal cancer: In silico analysis and validation

2021 ◽  
Vol 123 ◽  
pp. 104688
Author(s):  
Nasrin Nazempour ◽  
Mohammad Hossein Taleqani ◽  
Navid Taheri ◽  
Amir Hossein Haji Ali Asgary Najafabadi ◽  
Alireza Shokrollahi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Colorectal Cancer ◽  
Drug Resistance ◽  
Cell Surface ◽  
In Silico ◽  
In Silico Analysis ◽  
Surface Proteins ◽  
Cell Surface Proteins ◽  
Silico Analysis

scholarly journals Regulation of agr-Dependent Virulence Genes in Staphylococcus aureus by RNAIII from Coagulase-Negative Staphylococci

1998 ◽  
Vol 180 (12) ◽  
pp. 3181-3186 ◽  
Author(s):  
Karin Tegmark ◽  
Eva Morfeldt ◽  
Staffan Arvidson
Keyword(s):  
Staphylococcus Aureus ◽  
Cell Surface ◽  
Serine Protease ◽  
Protein A ◽  
Surface Proteins ◽  
Open Reading Frames ◽  
Alpha Toxin ◽  
Coagulase Negative Staphylococci ◽  
Cell Surface Proteins ◽  
Genes Encoding

ABSTRACT Many of the genes coding for extracellular toxins, enzymes, and cell surface proteins in Staphylococcus aureus are regulated by a 510-nucleotide (nt) RNA molecule, RNAIII. Transcription of genes encoding secreted toxins and enzymes, includinghla (alpha-toxin), saeB (enterotoxin B),tst (toxic shock syndrome toxin 1), and ssp(serine protease), is stimulated, while transcription of genes encoding cell surface proteins, like spa (protein A) andfnb (fibronectin binding proteins), is repressed. Besides being a regulator, RNAIII is also an mRNA coding for staphylococcal delta-lysin. We have identified RNAIII homologs in three different coagulase-negative staphylococci (CoNS), i.e., Staphylococcus epidermidis, Staphylococcus simulans, andStaphylococcus warneri. RNAIII from these CoNS turned out to be very similar to that of S. aureus and contained open reading frames encoding delta-lysin homologs. Though a number of big insertions and/or deletions have occurred, mainly in the 5′ half of the molecules, the sequences show a high degree of identity, especially in the first 50 and last 150 nt. The CoNS RNAIII had the ability to completely repress transcription of protein A in an RNAIII-deficientS. aureus mutant and the ability to stimulate transcription of the alpha-toxin and serine protease genes. However, the stimulatory effect was impaired compared to that of S. aureus RNAIII, suggesting that these regulatory functions are independent. By creating S. epidermidis-S. aureus RNAIII hybrids, we could also show that both the 5′ and 3′ halves of the RNAIII molecule are involved in the transcriptional regulation of alpha-toxin and serine protease mRNAs in S. aureus.

What do nanometer molecular trajectories tell us about heterogeneous cell surface domaines?

1995 ◽  
Vol 53 ◽  
pp. 786-787
Author(s):  
Watt W. Webb
Keyword(s):  
Cell Surface ◽  
Lipid Membranes ◽  
Surface Proteins ◽  
Protein Diffusion ◽  
Coated Pits ◽  
Cell Surface Proteins ◽  
Membrane Heterogeneity ◽  
Fluorescence Photobleaching Recovery ◽  
Photobleaching Recovery ◽  
Plasma Membrane Heterogeneity

Plasma membrane heterogeneity is implicit in the existence of specialized cell surface organelles which are necessary for cellular function; coated pits, post and pre-synaptic terminals, microvillae, caveolae, tight junctions, focal contacts and endothelial polarization are examples. The persistence of these discrete molecular aggregates depends on localized restraint of the constituent molecules within specific domaines in the cell surface by strong intermolecular bonds and/or anchorage to extended cytoskeleton. The observed plasticity of many of organelles and the dynamical modulation of domaines induced by cellular signaling evidence evanescent intermolecular interactions even in conspicuous aggregates. There is also strong evidence that universal restraints on the mobility of cell surface proteins persist virtually everywhere in cell surfaces, not only in the discrete organelles. Diffusion of cell surface proteins is slowed by several orders of magnitude relative to corresponding protein diffusion coefficients in isolated lipid membranes as has been determined by various ensemble average methods of measurement such as fluorescence photobleaching recovery(FPR).

Sign in / Sign up

Export Citation Format

Share Document