Identification of tumour-induced changes in endothelial cell surface protein expression: an in vitro model

Hewett, Peter W.

doi:10.1016/s1357-2725(01)00020-6

Cited by 21 publications

(16 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To optimize the biotinylation conditions, we compared two reagents, sulfo-NHS-LC-biotin (LC-biotin), recently used in several similar studies (11)(12)(13), and a more water-soluble analogue, sulfo-NHS-SS-biotin (SS-biotin). A SA-conjugated fluorescent dye, Alexa 488 was used to visualize the subcellular distribution of labeled proteins (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Several groups have attempted this using the established technique of cell surface biotinylation (10) and affinity capture with avidin (11)(12)(13). However, because the approach does little to address the intrinsic limitations of 2DE, it is unsurprising that the number of membrane proteins characterized remains disappointing; 18 in a recent study of the gastric pathogen Helicobacter pylori (11) and 14 in an investigation of human tumor cell lines (13), which, in the latter study, were accompanied by a large number of heat shock proteins, not normally thought of as PM proteins.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Expression Profiling of Lymphocyte Plasma Membrane Proteins

Peirce

Wait

Begum

et al. 2004

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

The physicochemical properties of plasma membrane proteins of mammalian cells render them refractory to systematic analysis by two-dimensional electrophoresis. We have therefore used in vivo cell surface labeling with a water-soluble biotinylation reagent, followed by cell lysis and membrane purification, prior to affinity capture of biotinylated proteins. Purified membrane proteins were then separated by solution-phase isoelectric focusing and SDS-PAGE and identified by high-pressure liquid chromatography electrospray/tandem mass spectrometry. Using this approach, we identified 42 plasma membrane proteins from a murine T cell hybridoma and 46 from unfractionated primary murine splenocytes. These included three unexpected proteins; nicastrin, osteoclast inhibitory lectin, and a transmembrane domain-containing hypothetical protein of 11.4 kDa. Following stimulation of murine splenocytes with phorbol ester and calcium ionophore, we observed differences in expression of CD69, major histocompatibility complex class II molecules, the glucocorticoid-induced TNF receptor family-related gene product, and surface immunoglobulin M and D that were subsequently confirmed by Western blot or flow cytometric analysis. This approach offers a generic and powerful strategy for investigating differential expression of surface proteins in many cell types under varying environmental and pathophysiological conditions. Molecular & Cellular Proteomics 3:56 -65, 2004.

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Expression Profiling of Lymphocyte Plasma Membrane Proteins

Peirce

Wait

Begum

et al. 2004

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

show abstract

“…The microvasculature was previously shown to be involved in tumor angiogenesis and microvasculature-derived ECs exhibited functional differences compared to large vessel-derived ECs, 48,49 including differences in the response to growth stimulators 50,51 and extracellular protein expression patterns. [52][53][54] To generate natural EC phenotypes and appropriate responses of ECs to growth stimuli, it is essential that primary HMECs be used rather than cell lines.…”

mentioning

confidence: 99%

Design of universal cancer vaccines using natural tumor vessel-specific antigens (SANTAVAC)

Lokhov¹,

Balashova²

2015

Human Vaccines & Immunotherapeutics

View full text Add to dashboard Cite

“…We have implemented a biotinylation-based strategy for targeting surface membrane-derived proteins, to allow capture of these proteins, thereby providing substantial enrichment, and increased sensitivity through the use of avidin labels for detection. There have been prior studies that have combined protein biotinylation with two-dimensional gels (9). In these studies, protein identification was largely based on the use of antibodies to specific proteins.…”

mentioning

confidence: 99%

Global Profiling of the Cell Surface Proteome of Cancer Cells Uncovers an Abundance of Proteins with Chaperone Function

Shin¹,

Wang²,

Yim³

et al. 2003

Journal of Biological Chemistry

498

377

View full text Add to dashboard Cite

There is currently limited data available pertaining to the global characterization of the cell surface proteome. We have implemented a strategy for the comprehensive profiling and identification of surface membrane proteins. This strategy has been applied to cancer cells, including the SH-SY5Y neuroblastoma, the A549 lung adenocarcinoma, the LoVo colon adenocarcinoma, and the Sup-B15 acute lymphoblastic leukemia (B cell) cell lines and ovarian tumor cells. Surface membrane proteins of viable, intact cells were subjected to biotinylation then affinity-captured and purified on monomeric avidin columns. The biotinylated proteins were eluted from the monomeric avidin columns as intact proteins and were subsequently separated by two-dimensional PAGE, transferred to polyvinylidene difluoride membranes, and visualized by hybridization with streptavidin-horseradish peroxidase. Highly reproducible, but distinct, two-dimensional patterns consisting of several hundred biotinylated proteins were obtained for the different cell populations analyzed. Identification of a subset of biotinylated proteins among the different cell populations analyzed using matrix-assisted laser desorption ionization and tandem mass spectrometry uncovered proteins with a restricted expression pattern in some cell line(s), such as CD87 and the activin receptor type IIB. We also identified more widely expressed proteins, such as CD98, and a sushi repeat-containing protein, a member of the selectin family. Remarkably, a set of proteins identified as chaperone proteins were found to be highly abundant on the cell surface, including GRP78, GRP75, HSP70, HSP60, HSP54, HSP27, and protein disulfide isomerase. Comprehensive profiling of the cell surface proteome provides an effective approach for the identification of commonly occurring proteins as well as proteins with restricted expression patterns in this compartment.

show abstract

Identification of tumour-induced changes in endothelial cell surface protein expression: an in vitro model

Cited by 21 publications

References 29 publications

Expression Profiling of Lymphocyte Plasma Membrane Proteins

Expression Profiling of Lymphocyte Plasma Membrane Proteins

Design of universal cancer vaccines using natural tumor vessel-specific antigens (SANTAVAC)

Global Profiling of the Cell Surface Proteome of Cancer Cells Uncovers an Abundance of Proteins with Chaperone Function

Contact Info

Product

Resources

About