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Your search keyword '"Ostanin, Kirill"' showing total 17 results
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17 results on '"Ostanin, Kirill"'

1. Data from Characterization of the Cellular and Antitumor Effects of MPI-0479605, a Small-Molecule Inhibitor of the Mitotic Kinase Mps1

Author

Tardif, Keith D., primary, Rogers, Aaron, primary, Cassiano, Jared, primary, Roth, Bruce L., primary, Cimbora, Daniel M., primary, McKinnon, Rena, primary, Peterson, Ashley, primary, Douce, Thomas B., primary, Robinson, Rosann, primary, Dorweiler, Irene, primary, Davis, Thaylon, primary, Hess, Mark A., primary, Ostanin, Kirill, primary, Papac, Damon I., primary, Baichwal, Vijay, primary, McAlexander, Ian, primary, Willardsen, J. Adam, primary, Saunders, Michael, primary, Christophe, Hoarau, primary, Kumar, D. Vijay, primary, Wettstein, Daniel A., primary, Carlson, Robert O., primary, and Williams, Brandi L., primary

Published
2023
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2. Supplementary Tables 1-2, Figures 1-7 from Characterization of the Cellular and Antitumor Effects of MPI-0479605, a Small-Molecule Inhibitor of the Mitotic Kinase Mps1

Author

Tardif, Keith D., primary, Rogers, Aaron, primary, Cassiano, Jared, primary, Roth, Bruce L., primary, Cimbora, Daniel M., primary, McKinnon, Rena, primary, Peterson, Ashley, primary, Douce, Thomas B., primary, Robinson, Rosann, primary, Dorweiler, Irene, primary, Davis, Thaylon, primary, Hess, Mark A., primary, Ostanin, Kirill, primary, Papac, Damon I., primary, Baichwal, Vijay, primary, McAlexander, Ian, primary, Willardsen, J. Adam, primary, Saunders, Michael, primary, Christophe, Hoarau, primary, Kumar, D. Vijay, primary, Wettstein, Daniel A., primary, Carlson, Robert O., primary, and Williams, Brandi L., primary

Published
2023
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3. Small GTPase ARF6 controls VEGFR2 trafficking and signaling in diabetic retinopathy

Author

Zhu, Weiquan, Shi, Dallas S., Winter, Jacob M., Rich, Bianca E., Tong, Zongzhong, Sorensen, Lise K., Zhao, Helong, Huang, Yi, Tai, Zhengfu, Mleynek, Tara M., Yoo, Jae Hyuk, Dunn, Christine, Ling, Jing, Richards, Jackson R. Bergquist, Jake A., Jiang, Amanda, Lesniewski, Lisa A., Ward, M. Elizabeth Hartnet Diane M., Mueller, Alan L., Ostanin, Kirill, Thomas, Kirk R., Odelberg, Shannon J., and Li, Dean Y.

Subjects
Diabetic retinopathy -- Genetic aspects -- Research, Vascular endothelial growth factor -- Research, Binding proteins -- Research, Cellular signal transduction -- Research, Health care industry
Abstract

The devastating sequelae of diabetes mellitus include microvascular permeability, which results in retinopathy. Despite clinical and scientific advances, there remains a need for new approaches to treat retinopathy. Here, we have presented a possible treatment strategy, whereby targeting the small GTPase ARF6 alters VEGFR2 trafficking and reverses signs of pathology in 4 animal models that represent features of diabetic retinopathy and in a fifth model of ocular pathological angiogenesis. Specifically, we determined that the same signaling pathway utilizes distinct GEFs to sequentially activate ARF6, and these GEFs exert distinct but complementary effects on VEGFR2 trafficking and signal transduction. ARF6 activation was independently regulated by 2 different ARF GEFs - ARNO and GEP100. Interaction between VEGFR2 and ARNO activated ARF6 and stimulated VEGFR2 internalization, whereas a VEGFR2 interaction with GEP100 activated ARF6 to promote VEGFR2 recycling via coreceptor binding. Intervening in either pathway inhibited VEGFR2 signal output. Finally, using a combination of in vitro, cellular, genetic, and pharmacologic techniques, we demonstrated that ARF6 is pivotal in VEGFR2 trafficking and that targeting ARF6-mediated VEGFR2 trafficking has potential as a therapeutic approach for retinal vascular diseases such as diabetic retinopathy., Introduction Over 25 million people in the United States have diabetes mellitus (1) and are prone to suffer from its devastating sequelae. The metabolic derangements seen in diabetes lead to [...]

Published
2017
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4. ARF6 Is an Actionable Node that Orchestrates Oncogenic GNAQ Signaling in Uveal Melanoma

Author

Yoo, Jae Hyuk, primary, Shi, Dallas S., additional, Grossmann, Allie H., additional, Sorensen, Lise K., additional, Tong, ZongZhong, additional, Mleynek, Tara M., additional, Rogers, Aaron, additional, Zhu, Weiquan, additional, Richards, Jackson R., additional, Winter, Jacob M., additional, Zhu, Jie, additional, Dunn, Christine, additional, Bajji, Ashok, additional, Shenderovich, Mark, additional, Mueller, Alan L., additional, Woodman, Scott E., additional, Harbour, J. William, additional, Thomas, Kirk R., additional, Odelberg, Shannon J., additional, Ostanin, Kirill, additional, and Li, Dean Y., additional

Published
2016
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7. The Small GTPase ARF6 Stimulates β-Catenin Transcriptional Activity During WNT5A-Mediated Melanoma Invasion and Metastasis

Author

Grossmann, Allie H., primary, Yoo, Jae Hyuk, additional, Clancy, James, additional, Sorensen, Lise K., additional, Sedgwick, Alanna, additional, Tong, Zongzhong, additional, Ostanin, Kirill, additional, Rogers, Aaron, additional, Grossmann, Kenneth F., additional, Tripp, Sheryl R., additional, Thomas, Kirk R., additional, D’Souza-Schorey, Crislyn, additional, Odelberg, Shannon J., additional, and Li, Dean Y., additional

Published
2013
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8. Characterization of the Cellular and Antitumor Effects of MPI-0479605, a Small-Molecule Inhibitor of the Mitotic Kinase Mps1

Author

Tardif, Keith D., primary, Rogers, Aaron, additional, Cassiano, Jared, additional, Roth, Bruce L., additional, Cimbora, Daniel M., additional, McKinnon, Rena, additional, Peterson, Ashley, additional, Douce, Thomas B., additional, Robinson, Rosann, additional, Dorweiler, Irene, additional, Davis, Thaylon, additional, Hess, Mark A., additional, Ostanin, Kirill, additional, Papac, Damon I., additional, Baichwal, Vijay, additional, McAlexander, Ian, additional, Willardsen, J. Adam, additional, Saunders, Michael, additional, Christophe, Hoarau, additional, Kumar, D. Vijay, additional, Wettstein, Daniel A., additional, Carlson, Robert O., additional, and Williams, Brandi L., additional

Published
2011
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9. Discovery and SAR of Methylated Tetrahydropyranyl Derivatives as Inhibitors of Isoprenylcysteine Carboxyl Methyltransferase (ICMT)

Author

Judd, Weston R., primary, Slattum, Paul M., additional, Hoang, Khanh C., additional, Bhoite, Leena, additional, Valppu, Liisa, additional, Alberts, Glen, additional, Brown, Brita, additional, Roth, Bruce, additional, Ostanin, Kirill, additional, Huang, Liwen, additional, Wettstein, Daniel, additional, Richards, Burt, additional, and Willardsen, J. Adam, additional

Published
2011
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10. Analogues of 4-[(7-Bromo-2-methyl-4-oxo-3H-quinazolin-6-yl)methylprop-2-ynylamino]-N-(3-pyridylmethyl)benzamide (CB-30865) as Potent Inhibitors of Nicotinamide Phosphoribosyltransferase (Nampt)

Author

Lockman, Jeffrey W., primary, Murphy, Brett R., additional, Zigar, Daniel F., additional, Judd, Weston R., additional, Slattum, Paul M., additional, Gao, Zhong-Hua, additional, Ostanin, Kirill, additional, Green, Jeremy, additional, McKinnon, Rena, additional, Terry-Lorenzo, Ryan T., additional, Fleischer, Tracey C., additional, Boniface, J. Jay, additional, Shenderovich, Mark, additional, and Willardsen, J. Adam, additional

Published
2010
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12. Abstract LB-288: MPI-0486348: A novel inhibitor of nicotinamide phosphoribosyltransferase (Nampt) induces tumor regression in a preclinical model

Author

Fleischer, Tracey C., primary, Baichwal, Vijay R., additional, Bradford, Chad L., additional, Demie, Lynn, additional, Green, Jeremy P., additional, Hess, Mark A., additional, Lockman, Jeffrey W., additional, McKinnon, Rena, additional, Ostanin, Kirill, additional, Papac, Damon I., additional, Reeves, Leslie F., additional, Terry-Lorenzo, Ryan T., additional, and Willardsen, J Adam, additional

Published
2010
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15. Human XPAand XRCC1DNA Repair Proteins Expressed in Yeast, Saccharomyces cerevisiae

Author

Pushnova, Elena A., Ostanin, Kirill, and Thelen, Michael P.

Abstract

Human XPA and XRCC1 DNA repair proteins have been expressed in a series of novel yeast episomal vectors. Expression of XPAcDNA resulted in synthesis of anti-XPA crossreacting polypeptides of 40 and 42 kDa, the status of the native protein found in human cells. Likewise, the majority of the recombinant XRCC1 found in the yeast intracellular fraction corresponded to the molecular mass of the full-length human protein. Recombinant XPA protein expressed as an NH2-terminal polyhistidine fusion could be affinity purified using Ni2+agarose.

Published
2001
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16. Cloning and Characterization of a Saccharomyces cerevisiaeGene Encoding the Low Molecular Weight Protein-tyrosine Phosphatase (∗)

Author

Ostanin, Kirill, Pokalsky, Christine, Wang, Shuishu, and Van Etten, Robert L.

Abstract

The low molecular weight protein-tyrosine phosphatase (low MrPTPase) is an 18-kDa cytoplasmic enzyme of unknown function that has been previously found in several vertebrates. Using an oligonucleotide probe derived from the active site sequence of the mammalian low MrPTPases, a Saccharomyces cerevisiaegene that encodes a homolog of this enzyme was cloned by low stringency hybridization. This gene, LTP1, together with a neighboring gene, TKL1, is shown to be located on the right arm of chromosome XVI. The deduced amino acid sequence of its 161-amino acid residue product shows a 39% average identity with that of the mammalian enzymes. The yeast Ltp1 protein was expressed in Escherichia coli,purified to homogeneity, and shown to possess PTPase activity. The recombinant Ltp1 efficiently hydrolyzes phosphotyrosine and a phosphotyrosine-containing peptide, Tyr531-fyn, but it shows low activity toward phosphoserine and phosphothreonine. The catalytic activity of Ltp1 toward a number of substrates was approximately 30-fold lower than the corresponding values measured for the bovine low MrPTPase. However, the yeast enzyme was markedly activated by adenine and some purine nucleosides and nucleotides, including cAMP and cGMP. In the case of adenine, the activity of Ltp1 was increased by approximately 30-fold. The high degree of evolutionary conservation of the low MrPTPases implies a significant role for this enzyme. However, neither the disruption of the LTP1gene nor an approximately 10-fold overexpression of its product in S. cerevisiaecaused any apparent phenotypic changes under the conditions tested. No proteins related to Ltp1 could be detected in extracts of the ltp1null mutant, either by immunoblotting or by gel-filtration analysis accompanied by extended kinetic assays, consistent with the conclusion that LTP1is the only low MrPTPase-encoding gene in S. cerevisiae.

Published
1995
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17. Small GTPase ARF6 controls VEGFR2 trafficking and signaling in diabetic retinopathy.

Author

Winter, Jacob M., Rich, Bianca E., Sorensen, Lise K., Helong Zhao, Mleynek, Tara M., Jae Hyuk Yoo, Jing Ling, Bergquist, Jake A., Jiang, Amanda, Thomas, Kirk R., Odelberg, Shannon J., Weiquan Zhu, Li, Dean Y., Shi, Dallas S., Richards, Jackson R., Hartnett, M. Elizabeth, Ward, Diane M., Dunn, Christine, Mueller, Alan L., and Ostanin, Kirill

Subjects
*ADP-ribosylation factors, *VASCULAR endothelial growth factor genetics, *DIABETIC retinopathy, *GUANOSINE triphosphatase genetics, *NEOVASCULARIZATION, *GENETICS of diabetes, *CELLULAR signal transduction, *GENETICS
Abstract

The devastating sequelae of diabetes mellitus include microvascular permeability, which results in retinopathy. Despite clinical and scientific advances, there remains a need for new approaches to treat retinopathy. Here, we have presented a possible treatment strategy, whereby targeting the small GTPase ARF6 alters VEGFR2 trafficking and reverses signs of pathology in 4 animal models that represent features of diabetic retinopathy and in a fifth model of ocular pathological angiogenesis. Specifically, we determined that the same signaling pathway utilizes distinct GEFs to sequentially activate ARF6, and these GEFs exert distinct but complementary effects on VEGFR2 trafficking and signal transduction. ARF6 activation was independently regulated by 2 different ARF GEFs - ARNO and GEP100. Interaction between VEGFR2 and ARNO activated ARF6 and stimulated VEGFR2 internalization, whereas a VEGFR2 interaction with GEP100 activated ARF6 to promote VEGFR2 recycling via coreceptor binding. Intervening in either pathway inhibited VEGFR2 signal output. Finally, using a combination of in vitro, cellular, genetic, and pharmacologic techniques, we demonstrated that ARF6 is pivotal in VEGFR2 trafficking and that targeting ARF6-mediated VEGFR2 trafficking has potential as a therapeutic approach for retinal vascular diseases such as diabetic retinopathy. [ABSTRACT FROM AUTHOR]

Published
2017
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