Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 131 to 133 of 133

Publication Record


Epidermal growth factor receptor activation induces nuclear targeting of cyclooxygenase-2, basolateral release of prostaglandins, and mitogenesis in polarizing colon cancer cells.
Coffey RJ, Hawkey CJ, Damstrup L, Graves-Deal R, Daniel VC, Dempsey PJ, Chinery R, Kirkland SC, DuBois RN, Jetton TL, Morrow JD
(1997) Proc Natl Acad Sci U S A 94: 657-62
MeSH Terms: Amphiregulin, Cell Compartmentation, Cell Nucleus, Cell Polarity, Cyclooxygenase 2, Cyclooxygenase 2 Inhibitors, Cyclooxygenase Inhibitors, EGF Family of Proteins, ErbB Receptors, Glycoproteins, Growth Substances, Humans, Intercellular Signaling Peptides and Proteins, Isoenzymes, Membrane Proteins, Mitosis, Nitrobenzenes, Prostaglandin-Endoperoxide Synthases, Prostaglandins, Pyrazoles, RNA, Neoplasm, Sulfonamides, Sulindac, Transforming Growth Factor alpha, Tumor Cells, Cultured
Show Abstract · Added March 27, 2014
Nonsteroidal antiinflammatory drugs reduce the risk of colon cancer, possibly via cyclooxygenase (COX) inhibition. The growth factor-inducible COX-2, which is overexpressed in neoplastic colonic tissue, is an attractive target to mediate this effect. Herein we have exploited the ability of a human colon cancer cell line, HCA-7 Colony 29, to polarize when cultured on Transwell (Costar) filters to study COX-2 production and the vectorial release of prostaglandins (PGs). Administration of type alpha transforming growth factor to the basolateral compartment, in which the epidermal growth factor receptor (EGFR) resides, results in a marked induction of COX-2 immunoreactivity at the base of the cells and the unexpected appearance of COX-2 in the nucleus. The increase in COX-2 protein is associated with a dose- and time-dependent increase in PG levels in the basolateral, but not apical, medium. Amphiregulin is the most abundantly expressed EGFR ligand in these cells, and the protein is present at the basolateral surface. EGFR blockade reduces baseline COX-2 immunoreactivity, PG levels, and mitogenesis in a concentration-dependent manner. Two specific COX-2 inhibitors, SC-58125 and NS 398, also, in a dose-dependent manner, attenuate baseline and type alpha transforming growth factor-stimulated mitogenesis, although PG levels are decreased > 90% at all concentrations of inhibitor tested. These findings show that activation of the EGFR stimulates COX-2 production and its translocation to the nucleus, vectorial release of PGs, and mitogenesis in polarized HCA-7 Colony 29 cells.
1 Communities
1 Members
0 Resources
25 MeSH Terms
Cell-specific sorting of biogenic amine transporters expressed in epithelial cells.
Gu HH, Ahn J, Caplan MJ, Blakely RD, Levey AI, Rudnick G
(1996) J Biol Chem 271: 18100-6
MeSH Terms: Animals, Biogenic Amines, Biological Transport, Carrier Proteins, Cell Compartmentation, Cell Membrane, Cell Polarity, Cells, Cultured, Dogs, Dopamine, Dopamine Plasma Membrane Transport Proteins, Epithelial Cells, Humans, Immunohistochemistry, Membrane Glycoproteins, Membrane Transport Proteins, Nerve Tissue Proteins, Norepinephrine, Norepinephrine Plasma Membrane Transport Proteins, Rats, Recombinant Proteins, Serotonin, Serotonin Plasma Membrane Transport Proteins, Symporters
Show Abstract · Added July 10, 2013
We have utilized polarized epithelial cells stably expressing neurotransmitter transporters to analyze the sorting behavior of these membrane proteins. The transporters for serotonin (5-HT), dopamine (DA), and norepinephrine (NE) are expected to be present in situ in the most distal extremities of axonal membranes, where they terminate the action of their biogenic amine substrates. Both Madin-Darby canine kidney (MDCK) and LLC-PK1 cells were stably transfected with cDNAs encoding either the rat 5-HT transporter (SERT), the human NE transporter (NET), or the rat or human DA transporter (DAT). These cells were grown on permeable filter supports, and the transporters were localized by three independent techniques. Confocal immunofluorescence microscopy indicated that each of the transporters expressed in LLC-PK1 cells was sorted to the basolateral membrane, co-localizing with the Na+/K+-ATPase. In MDCK cells, however, DAT was located primarily on the apical surface, while SERT and NET were found on the basolateral membranes. Cell surface biotinylation using an impermeant biotinylating reagent confirmed the immunocytochemistry results. Thus, SERT and NET in MDCK cells were labeled more efficiently from the basolateral medium than the apical medium, and DAT in MDCK cells was labeled more efficiently from the apical side than the basolateral side. Transport measurements in transfected MDCK cells agreed with the immunocytochemistry and biotinylation results. These results suggest the existence of cell-specific mechanisms that discriminate between neurotransmitter transporters for surface expression and render unlikely any simple hypothesis that sorting mechanisms in neurons and epithelia are identical.
1 Communities
1 Members
0 Resources
24 MeSH Terms
An unusual mosaic protein with a protease domain, encoded by the nudel gene, is involved in defining embryonic dorsoventral polarity in Drosophila.
Hong CC, Hashimoto C
(1995) Cell 82: 785-94
MeSH Terms: Amino Acid Sequence, Animals, Cell Polarity, Cloning, Molecular, Drosophila, Embryo, Nonmammalian, Extracellular Matrix Proteins, Gene Expression Regulation, Developmental, Genes, Insect, In Situ Hybridization, Molecular Sequence Data, Oocytes, Serine Endopeptidases, Temperature
Show Abstract · Added August 19, 2012
Dorsoventral polarity of the Drosophila embryo is induced by a ventral extracellular signal, which is produced by a locally activated protease cascade within the extraembryonic perivitelline compartment. Local activation of the protease cascade depends on a positional cue that is laid down during oogenesis outside the oocyte. Here we present evidence that the nudel gene encodes an essential component of this cue. The nudel gene, which is expressed in follicle cells covering the oocyte, encodes an unusual mosaic protein resembling an extracellular matrix protein with a central serine protease domain. Our findings suggest that embryonic dorsoventral polarity is defined by a positional cue that requires the nudel protein to anchor and to trigger the protease cascade producing the polarity-inducing signal.
1 Communities
1 Members
0 Resources
14 MeSH Terms