Publications by authors named "Jacquelyn R Cole"

2 Publications

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Expression of the aryl hydrocarbon receptor is not required for the proliferation, migration, invasion, or estrogen-dependent tumorigenesis of MCF-7 breast cancer cells.

Mol Carcinog 2013 Jul 2;52(7):544-54. Epub 2012 Mar 2.

Laboratory of Molecular Toxicology, Wadsworth Center, New York State Department of Health, Albany, New York 12201-0509, USA.

The AhR was initially identified as a ligand-activated transcription factor mediating effects of chlorinated dioxins and polycyclic aromatic hydrocarbons on cytochrome P450 1 (CYP1) expression. Recently, evidence supporting involvement of the AhR in cell-cycle regulation and tumorigenesis has been presented. To further define the roles of the AhR in cancer, we investigated the effects of AhR expression on cell proliferation, migration, invasion, and tumorigenesis of MCF-7 human breast cancer cells. In these studies, the properties of MCF-7 cells were compared with those of two MCF-7-derived sublines: AH(R100) , which express minimal AhR, and AhR(exp) , which overexpress AhR. Quantitative PCR, Western immunoblots, 17β-estradiol (E2 ) metabolism assays, and ethoxyresorufin O-deethylase assays showed the lack of AhR expression and AhR-regulated CYP1 expression in AH(R100) cells, and enhanced AhR and CYP1 expression in AhR(exp) cells. In the presence of 1 nM E2 , rates of cell proliferation of the three cell lines showed an inverse correlation with the levels of AhR mRNA. In comparison with MCF-7 and AhR(exp) cells, AH(R100) cells produced more colonies in soft agar and showed enhanced migration and invasion in chamber assays with E2 as the chemoattractant. Despite the lack of significant AhR expression, AH(R100) cells retained the ability to form tumors in severe combined immunodeficient mice when supplemented with E2 , producing mean tumor volumes comparable to those observed with MCF-7 cells. These studies indicate that, while CYP1 expression and inducibility are highly dependent on AhR expression, the proliferation, invasion, migration, anchorage-independent growth, and estrogen-stimulated tumor formation of MCF-7 cells do not require the AhR.
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http://dx.doi.org/10.1002/mc.21889DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3433635PMC
July 2013

Affinity capture and detection of immunoglobulin E in human serum using an aptamer-modified surface in matrix-assisted laser desorption/ionization mass spectrometry.

Anal Chem 2007 Jan;79(1):273-9

Department of Chemistry and Chemical Biology, Cogswell Building, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.

Capture and detection of immunoglobulin E (IgE) in simple solution and in human serum using an aptamer-modified probe surface for affinity matrix-assisted laser desorption/ionization mass spectroscopy detection is reported. Detectable signals were obtained for 1 amol of IgE applied either in a single, 1microL application of 1 pM IgE or after 10 successive, 1-microL applications of 100 fM IgE. In both cases, the surface was rinsed after each application of IgE to remove sample concomitants including salts and free or nonspecifically associated proteins. Detection of native IgE, which is the least abundant of the serum immunoglobulins and occurs at subnanomolar levels, in human serum was demonstrated and interference from the high-abundance immunoglobulins and albumin was investigated. The aptamer-modified surface showed high selectivity toward immunoglobulins in serum, with no significant interference from serum albumin. Addition of IgE to the serum suppressed the signals from the other immunoglobulins, confirming the expected selectivity of the aptamer surface toward IgE. Dilution of the serum increased the selectivity toward IgE; the protein was detected without interference in a 10,000-fold dilution of the serum, which is consistent with detection of IgE at amol (pM) levels in standard solutions.
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http://dx.doi.org/10.1021/ac061256bDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2569142PMC
January 2007