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Your search keyword '"Steplewski, Klaudia M."' showing total 7 results
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7 results on '"Steplewski, Klaudia M."'

1. Quantitative Analysis of Orphan G Protein-Coupled Receptor mRNAs by TaqMan® Real-Time PCR: G2A and GPR4 Lysophospholipid Receptor Expression in Leukocytes and in a Rat Myocardial Infarction-Heart Failure Model

Author

Douglas, Stephen A., primary, Ao, Zhaohui, additional, Johns, Douglas G., additional, Maniscalco, Kristeen, additional, Willette, Robert N., additional, Sarov-Blat, Lea, additional, Cogswell, John P., additional, Seepersaud, Sheila, additional, Murdock, Paul, additional, Steplewski, Klaudia M., additional, and Patel, Lisa, additional

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2. Discovery of Substituted Maleimides as Liver X Receptor Agonists and Determination of a Ligand-Bound Crystal Structure

Author

Jaye, Michael C., primary, Krawiec, John A., additional, Campobasso, Nino, additional, Smallwood, Angela, additional, Qiu, Chunyan, additional, Lu, Quinn, additional, Kerrigan, John J., additional, De Los Frailes Alvaro, Maite, additional, Laffitte, Bryan, additional, Liu, Wu-Schyong, additional, Marino,, Joseph P., additional, Meyer, Craig R., additional, Nichols, Jason A., additional, Parks, Derek J., additional, Perez, Paloma, additional, Sarov-Blat, Lea, additional, Seepersaud, Sheila D., additional, Steplewski, Klaudia M., additional, Thompson, Scott K., additional, Wang, Ping, additional, Watson, Mike A., additional, Webb, Christine L., additional, Haigh, David, additional, Caravella, Justin A., additional, Macphee, Colin H., additional, Willson, Timothy M., additional, and Collins, Jon L., additional

Published
2005
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3. Neuromedin Elicits Cytokine Release in Murine Th2-Type T Cell Clone D10.G4.1

Author

Johnson, Eric N., primary, Appelbaum, Edward R., additional, Carptenter, Donald C., additional, Cox, Richard F., additional, Disa, Jyoti, additional, Foley, James J., additional, Ghosh, Sujoy K., additional, Naselsky, Diane P., additional, Pullen, Mark A., additional, Sarau, Henry M., additional, Scheff, Samuel R., additional, Steplewski, Klaudia M., additional, Zaks-Zilberman, Meirav, additional, and Aiyar, Nambi, additional

Published
2004
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4. The Orphan G Protein-coupled Receptors GPR41 and GPR43 Are Activated by Propionate and Other Short Chain Carboxylic Acids

Author

Brown, Andrew J., primary, Goldsworthy, Susan M., additional, Barnes, Ashley A., additional, Eilert, Michelle M., additional, Tcheang, Lili, additional, Daniels, Dion, additional, Muir, Alison I., additional, Wigglesworth, Mark J., additional, Kinghorn, Ian, additional, Fraser, Neil J., additional, Pike, Nicholas B., additional, Strum, Jay C., additional, Steplewski, Klaudia M., additional, Murdock, Paul R., additional, Holder, Julie C., additional, Marshall, Fiona H., additional, Szekeres, Philip G., additional, Wilson, Shelagh, additional, Ignar, Diane M., additional, Foord, Steve M., additional, Wise, Alan, additional, and Dowell, Simon J., additional

Published
2003
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5. Quantitative Analysis of Orphan G Protein-Coupled Receptor mRNAs by TaqMan® Real-Time PCR.

Author

Walker, John M., Davenport, Anthony P., Douglas, Stephen A., Ao, Zhaohui, Johns, Douglas G., Maniscalco, Kristeen, Willette, Robert N., Sarov-Blat, Lea, Cogswell, John P., Seepersaud, Sheila, Murdock, Paul, Steplewski, Klaudia M., and Patel, Lisa

Abstract

Historically, the G protein-coupled receptor (GPCR) protein family has proven to be an extremely tractable target class (1). It is estimated that approximately one-half of all drugs currently marketed exert their actions, either directly or indirectly, via GPCRs (2). Given the potential commercial opportunities emanating from the identification of small molecule modulators of "novel" GPCRs (currently, GPCRs generate in excess of $25 billion per year in worldwide sales revenue [xc33}]), it is not surprising that it is with great enthusiasm that both the pharmaceutical industry and academia move toward identifying novel members of this protein class. [ABSTRACT FROM AUTHOR]

Published
2005
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6. Quantitative analysis of orphan G protein-coupled receptor mRNAs by TaqMan Real-Time PCR: G2A and GPR4 lysophospholipid receptor expression in leukocytes and in a rat myocardial infarction-heart failure model.

Author

Douglas SA, Ao Z, Johns DG, Maniscalco K, Willette RN, Sarov-Blat L, Cogswell JP, Seepersaud S, Murdock P, Steplewski KM, and Patel L

Subjects
Animals, Blood Cells chemistry, Cell Cycle Proteins genetics, Humans, RNA, Messenger analysis, RNA, Messenger metabolism, Rats, Receptors, G-Protein-Coupled genetics, Cell Cycle Proteins metabolism, Polymerase Chain Reaction methods, Receptors, G-Protein-Coupled metabolism
Published
2005
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7. Neuromedin U elicits cytokine release in murine Th2-type T cell clone D10.G4.1.

Author

Johnson EN, Appelbaum ER, Carpenter DC, Cox RF, Disa J, Foley JJ, Ghosh SK, Naselsky DP, Pullen MA, Sarau HM, Scheff SR, Steplewski KM, Zaks-Zilberman M, and Aiyar N

Subjects
Animals, Calcineurin physiology, Calcium metabolism, Cell Line, Clone Cells, Cytokines antagonists & inhibitors, Dogs, Estrenes pharmacology, Humans, Interleukins antagonists & inhibitors, Interleukins metabolism, MAP Kinase Signaling System immunology, Membrane Proteins biosynthesis, Membrane Proteins genetics, Mice, Mitogen-Activated Protein Kinases metabolism, Neuropeptides metabolism, Phosphatidylinositol 3-Kinases physiology, Pyrrolidinones pharmacology, Rats, Receptors, Interleukin-4 physiology, Receptors, Neurotransmitter biosynthesis, Receptors, Neurotransmitter genetics, Signal Transduction immunology, Swine, Type C Phospholipases antagonists & inhibitors, Type C Phospholipases physiology, Cytokines metabolism, Membrane Proteins physiology, Neuropeptides physiology, Receptors, Neurotransmitter physiology, Th2 Cells immunology, Th2 Cells metabolism
Abstract

Neuromedin U (NmU), originally isolated from porcine spinal cord and later from other species, is a novel peptide that potently contracts smooth muscle. NmU interacts with two G protein-coupled receptors designated as NmU-1R and NmU-2R. This study demonstrates a potential proinflammatory role for NmU. In a mouse Th2 cell line (D10.G4.1), a single class of high affinity saturable binding sites for (125)I-labeled NmU (K(D) 364 pM and B(max) 1114 fmol/mg protein) was identified, and mRNA encoding NmU-1R, but not NmU-2R, was present. Competition binding analysis revealed equipotent, high affinity binding of NmU isopeptides to membranes prepared from D10.G4.1 cells. Exposure of these cells to NmU isopeptides resulted in an increase in intracellular Ca(2+) concentration (EC(50) 4.8 nM for human NmU). In addition, NmU also significantly increased the synthesis and release of cytokines including IL-4, IL-5, IL-6, IL-10, and IL-13. Studies using pharmacological inhibitors indicated that maximal NmU-evoked cytokine release required functional phospholipase C, calcineurin, MEK, and PI3K pathways. These data suggest a role for NmU in inflammation by stimulating cytokine production by T cells.

Published
2004
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