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Your search keyword '"Deck, Kathryn M."' showing total 15 results
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15 results on '"Deck, Kathryn M."'

3. Triisopropyltriazacyclononane copper(II): an efficient phosphodiester hydrolysis catalyst and DNA cleavage agent

Author

Deck, Kathryn M., Tseng, T. Andrew, and Burstyn, Judith N.

Subjects
Chemistry, Inorganic -- Research, DNA -- Physiological aspects, Hydrolysis -- Physiological aspects, Catalysts -- Physiological aspects, Esters -- Physiological aspects, Phosphorus -- Physiological aspects, Copper -- Physiological aspects, Chemistry
Abstract

Research has been conducted on the bis(p-nitrophenyl)phosphate (BNPP) hydrolysis. The kinetics of BNPP hydrolysis and DNA cleavage by this hydrolysis have been investigated and the results are presented.

Published
2002

4. Dysregulation of the sensory and regulatory pathways controlling cellular iron metabolism in unilateral obstructive nephropathy.

Author

Votava, James A., Reese, Shannon R., Deck, Kathryn M., Nizzi, Christopher P., Anderson, Sheila A., Djamali, Arjang, and Eisenstein, Richard S.

Subjects
IRON metabolism, ERYTHROPOIETIN receptors, RNA-binding proteins, IRON proteins, CHRONIC kidney failure, TRANSFERRIN receptors
Abstract

Chronic kidney disease involves disturbances in iron metabolism including anemia caused by insufficient erythropoietin (EPO) production. However, underlying mechanisms responsible for the dysregulation of cellular iron metabolism are incompletely defined. Using the unilateral ureteral obstruction (UUO) model in Irp1+/+ and Irp1-/- mice, we asked if iron regulatory proteins (IRPs), the central regulators of cellular iron metabolism and suppressors of EPO production, contribute to the etiology of anemia in kidney failure. We identified a significant reduction in IRP protein level and RNA binding activity that associates with a loss of the iron uptake protein transferrin receptor 1 (TfR1), increased expression of the iron storage protein subunits H- and L-ferritin, and a low but overall variable level of stainable iron in the obstructed kidney. This reduction in IRP RNA binding activity and ferritin RNA levels suggests the concomitant rise in ferritin expression and iron content in kidney failure is IRP dependent. In contrast, the reduction in the Epo mRNA level in the obstructed kidney was not rescued by genetic ablation of IRP1, suggesting disruption of normal hypoxia-inducible factor (HIF)-2α regulation. Furthermore, reduced expression of some HIF-α target genes in UUO occurred in the face of increased expression of HIF-a proteins and prolyl hydroxylases 2 and 1, the latter of which is not known to be HIF-a mediated. Our results suggest that the IRP system drives changes in cellular iron metabolism that are associated with kidney failure in UUO but that the impact of IRPs on EPO production is overridden by disrupted hypoxia signaling. [ABSTRACT FROM AUTHOR]

Published
2022
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9. The mTORC1/4E-BP pathway coordinates hemoglobin production with L -leucine availability

Author

Chung, Jacky, primary, Bauer, Daniel E., additional, Ghamari, Alireza, additional, Nizzi, Christopher P., additional, Deck, Kathryn M., additional, Kingsley, Paul D., additional, Yien, Yvette Y., additional, Huston, Nicholas C., additional, Chen, Caiyong, additional, Schultz, Iman J., additional, Dalton, Arthur J., additional, Wittig, Johannes G., additional, Palis, James, additional, Orkin, Stuart H., additional, Lodish, Harvey F., additional, Eisenstein, Richard S., additional, Cantor, Alan B., additional, and Paw, Barry H., additional

Published
2015
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10. Erythroid Cells Adapt to L-Leucine Scarcity By Reducing Hemoglobin Production Via the mTORC1/4E-BP Pathway

Author

Chung, Jacky, primary, Bauer, Daniel E., additional, Ghamari, Alireza, additional, Nizzi, Christopher P., additional, Deck, Kathryn M., additional, Kingsley, Paul D., additional, Yien, Yvette Y., additional, Huston, Nicholas C., additional, Chen, Caiyong, additional, Wittig, Johannes G., additional, Palis, James, additional, Orkin, Stuart H., additional, Lodish, Harvey F., additional, Eisenstein, Richard S., additional, Cantor, Alan B., additional, and Paw, Barry H., additional

Published
2014
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11. Iron regulatory protein-1 protects against mitoferrin-1-deficient porphyria.

Author

Chung, Jacky, primary, Anderson, Sheila A., additional, Gwynn, Babette, additional, Deck, Kathryn M., additional, Chen, Michael J., additional, Langer, Nathaniel B., additional, Shaw, George C., additional, Huston, Nicholas C., additional, Boyer, Leah F., additional, Datta, Sumon, additional, Paradkar, Prasad N., additional, Li, Liangtao, additional, Wei, Zong, additional, Lambert, Amy J., additional, Sahr, Kenneth, additional, Wittig, Johannes G., additional, Chen, Wen, additional, Lu, Wange, additional, Galy, Bruno, additional, Schlaeger, Thorsten M., additional, Hentze, Matthias W., additional, Ward, Diane M., additional, Kaplan, Jerry, additional, Eisenstein, Richard S., additional, Peters, Luanne L., additional, and Paw, Barry H., additional

Published
2014
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15. Selective Inhibition of Collagen Prolyl 4-Hydroxylase in Human Cells

Author

Vasta, James D., Andersen, Kristen A., Deck, Kathryn M., Nizzi, Christopher P., Eisenstein, Richard S., and Raines, Ronald T.

Abstract

Collagen is the most abundant protein in animals. Its overproduction is associated with fibrosis and cancer metastasis. The stability of collagen relies on post-translational modifications, the most prevalent being the hydroxylation of collagen strands by collagen prolyl 4-hydroxylases (CP4Hs). Catalysis by CP4Hs enlists an iron cofactor to convert proline residues to 4-hydroxyproline residues, which are essential for the conformational stability of mature collagen. Ethyl 3,4-dihydroxybenzoate (EDHB) is commonly used as a “P4H” inhibitor in cells, but suffers from low potency, poor selectivity, and off-target effects that cause iron deficiency. Dicarboxylates of 2,2′-bipyridine are among the most potent known CP4H inhibitors but suffer from a high affinity for free iron. A screen of biheteroaryl compounds revealed that replacing one pyridyl group with a thiazole moiety retains potency and enhances selectivity. A diester of 2-(5-carboxythiazol-2-yl)pyridine-5-carboxylic acid is bioavailable to human cells and inhibits collagen biosynthesis at concentrations that neither cause general toxicity nor disrupt iron homeostasis. These data anoint a potent and selective probe for CP4H and a potential lead for the development of a new class of antifibrotic and antimetastatic agents.

Published
2016
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