Joseph A. Dunn
University at Buffalo
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Annals of the New York Academy of Sciences | 1983
Peter M. Blumberg; K. Barry Delclos; Joseph A. Dunn; Susan Jaken; Karen L. Leach; Emily Yeh
The evidence for the multistage nature of tumor promotion in vivo and for multiple subclasses of phorbol ester receptors in vitro argues that multiple mechanisms of tumor promotion exist. The existence of multiple mechanisms suggests that brute force assay for tumor promoters in vivo may be inadequate and that understanding of mechanisms may be essential. The interest in the phorbol esters is not primarily that they are environmental hazards for man, but rather that they provide a probe for phorbol ester receptors. These receptors are found in people, and modulation of their activity may play a role in tumor promotion in man.
Biochemical Pharmacology | 1996
David G. Sawutz; Donald C. Bode; G.Maurice Briggs; John Reid; Paul C. Canniff; Lisa Caldwell; Connie R. Faltynek; Deborah Miller; Joseph A. Dunn; Lawrence de Garavilla; Joseph Guiles; Carolyn Weigelt; William F. Michne; Adi Treasurywala; Paul J. Silver
In this report, we describe the discovery and characterization of a novel biarylhydrazone series of platelet-derived growth factor (PDGF) receptor tyrosine kinase inhibitors typified by the prototype WIN 41662 (3-phenyl-N1-[1-(4-pytidyl)pyrimidine]hydrazone). WIN 41662 inhibited PDGF-stimulated autophosphorylation of PDGF receptors from human vascular smooth muscle cells (hVSMC) with an IC50 value of 60 nM. The inhibitor appeared to be competitive with respect to substrate (Mn(2+)-ATP), having a calculated Ki of 15 +/- 5 nM. WIN 41662 was approximately 500-fold more potent in inhibiting the PDGF receptor tyrosine kinase than the p56lck tyrosine kinase. It was inactive against other serine/threonine and tyrosine kinases tested. WIN 41662 produced concentration-dependent inhibition of PDGF-stimulated receptor autophosphorylation in intact hVSMC with an IC50 < 100 nM. Intracellular Ca2+ mobilization and cell proliferation were events that occurred in hVSMC subsequent to PDGF receptor activation. WIN 41662 inhibited PDGF-stimulated Ca2+ mobilization and cell proliferation ([3H]TdR incorporation) with IC50 values of 430 nM and 2.3 microM, respectively. These effects appeared to be specifically related to PDGF receptor tyrosine kinase inhibition since WIN 41662 was not cytotoxic (in vitro) and since WIN 72039, a close structural analog that does not inhibit PDGF receptor tyrosine kinase, also did not inhibit PDGF-stimulated receptor autophosphorylation, Ca2+ mobilization, or hVSMC proliferation. Thus, WIN 41662 is representative of a novel class of selective PDGF receptor tyrosine kinase inhibitors that inhibit PDGF-regulated secondary events in intact cells.
International Journal of Radiation Oncology Biology Physics | 1979
Thomas J. Bardos; Joseph A. Dunn; Michael E. Perlman
Abstract Three 2,2-dimethyl phosphoraziridines, bis(2,2-dimethylaziridinyl)phosphinyl urethane (AB-132, NSC 51325), ethyl bis(2,2-dimethylaziridinyi)phosphinate (AB-163 NSC 108878) and bis(2,2-dimethylaziridinyl)-N-hydroxyurethane (AB-182, NSC 200724) which have shown synergistic antitumor effects in conjunction with X-irradiation, are characterized by their rapid hydrolysis via S N 1-mechanism and via the formation of transient 5-membered cyclic intermediates exhibiting phosphorylating activities. It was shown that the formation of the latter correlates with the observed maxima in the cholinesterase inhibitory effects of these compounds. It is proposed that the same intermediate hydrolysis products may block the repair of X-irradiation induced breaks in the DNA strands by phosphorylating their free YOH end groups. Additional mechanisms of the radiation potentiating effects of these compounds (not shown by their C-unsubstituted analogs), involving free radical-ion formation, are currently under investigation.
Journal of Medicinal Chemistry | 1994
Roland E. Dolle; Joseph A. Dunn; Mark A. Bobko; Baldev Singh; Joan E. Kuster; Eugene R. Baizman; Alex L. Harris; David G. Sawutz; Deborah Miller; Su Wang; Connie R. Faltynek; Wen Xie; Jay Sarup; D. Christopher Bode; Edward D. Pagani; Paul J. Silver
Cancer Research | 1983
Joseph A. Dunn; Peter M. Blumberg
Cancer Research | 1985
Joseph A. Dunn; Arco Y. Jeng; Stuart H. Yuspa; Peter M. Blumberg
Virology | 2005
András Horváth; Szilvia Tokés; Tracy L. Hartman; Karen Watson; Jim A. Turpin; Robert W. Buckheit; Zsolt Sebestyén; János Szöllosi; Ilona Benko; Thomas J. Bardos; Joseph A. Dunn; László Fésüs; Ferenc Tóth; János Aradi
Cancer Research | 1992
Joseph A. Dunn; Michael B. Faletto; Steven J. Kasper; Hira L. Gurtoo
Journal of Medicinal Chemistry | 1991
Michael E. Perlman; Joseph A. Dunn; Thomas A. Piscitelli; Julie Earle; William C. Rose; Galen L. Wampler; Joan E. MacDiarmid; Thomas J. Bardos
Journal of Medicinal Chemistry | 1990
Robert G. Breiner; William C. Rose; Joseph A. Dunn; Joan E. MacDiarmid; Thomas J. Bardos