Edward P. Feener
Brigham and Women's Hospital
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Featured researches published by Edward P. Feener.
Science | 1996
Hidehiro Ishii; Michael R. Jirousek; Daisuke Koya; Chikako Takagi; Pu Xia; Allen C. Clermont; Sven Erik Bursell; Timothy S. Kern; Lawrence M. Ballas; William F. Heath; Lawrence E. Stramm; Edward P. Feener; George L. King
The vascular complications of diabetes mellitus have been correlated with enhanced activation of protein kinase C (PKC). LY333531, a specific inhibitor of the β isoform of PKC, was synthesized and was shown to be a competitive reversible inhibitor of PKC β1 and β2, with a half-maximal inhibitory constant of ∼5 nM; this value was one-fiftieth of that for other PKC isoenzymes and one-thousandth of that for non-PKC kinases. When administered orally, LY333531 ameliorated the glomerular filtration rate, albumin excretion rate, and retinal circulation in diabetic rats in a dose-responsive manner, in parallel with its inhibition of PKC activities.
Journal of Clinical Investigation | 1995
Edward P. Feener; J M Northrup; Lloyd Paul Aiello; George L. King
Angiotensin II (AII)- and Arg8-vasopressin (AVP)-regulated gene expression in vascular cells has been reported to contribute to vascular homeostasis and hypertrophy. In this report, AVP-induced expression of plasminogen activator inhibitor (PAI)-2 mRNA in rat microvessel endothelial (RME) cells was identified using differential mRNA display. Further characterization of vasoactive peptide effects on PAI expression revealed that AII stimulated a 44.8 +/- 25.2-fold and a 12.4 +/- 3.2-fold increase in PAI-2 mRNA in RME cells and rat aortic smooth muscle cells (RASMC), respectively. AII also stimulated a 10- and 48-fold increase in PAI-1 mRNA in RME cells and RASMC, respectively. These AII effects were inhibited by either Sar1, Ile8-angiotensin or the AT1 antagonist DuP 735, but were not significantly altered in the presence of the AT2 antagonist PD123319. AII stimulation of RASMC and RME cells also significantly increased both PAI-1 protein and PAI activity released to the culture medium. Inhibition of protein kinase C completely blocked PMA-stimulated induction of PAI-2 mRNA in both cell types and inhibited the AII-stimulated increase in RASMC by 98.6 +/- 2.8%. In contrast, protein kinase C inhibition only partially decreased the AII-stimulated PAI-2 expression in RME cells by 68.8 +/- 11.1%, suggesting that a protein kinase C-independent mechanism contributes to a 6.9 +/- 1.5-fold AII induction of PAI-2 expression in endothelial cells. AII and PMA also stimulated protein tyrosine phosphorylation in RME cells, and the tyrosine kinase inhibitor genistein partially blocked their induction of PAI-2 mRNA. These findings suggest that AII may regulate plasminogen activation in the vasculature by inducing both PAI-1 and PAI-2 expression.
Journal of Biological Chemistry | 2005
Zhiheng He; Kerrie J. Way; Emi Arikawa; Eva Chou; Darren M. Opland; Allen C. Clermont; Keiji Isshiki; Ronald Cw Ma; Joshua A. Scott; Frederick J. Schoen; Edward P. Feener; George L. King
Protein kinase C (PKC) and angiotensin II (AngII) can regulate cardiac function in pathological conditions such as in diabetes or ischemic heart disease. We have reported that expression of connective tissue growth factor (CTGF) is increased in the myocardium of diabetic mice. Now we showed that the increase in CTGF expression in cardiac tissues of streptozotocin-induced diabetic rats was reversed by captopril and islet cell transplantation. Infusion of AngII in rats increased CTGF mRNA expression by 15-fold, which was completely inhibited by co-infusion with AT1 receptor antagonist, candesartan. Similarly, incubation of cultured cardiomyocytes with AngII increased CTGF mRNA expression by 2-fold, which was blocked by candesartan and a general PKC inhibitor, GF109203X. The role of PKC isoform-dependent action was further studied using adenoviral vector-mediated gene transfer of dominant negative (dn) PKC or wild type PKC isoforms. Expression of dnPKCα, -ϵ, and -ζ isoforms suppressed AngII-induced CTGF expression in cardiomyocytes. In contrast, expression of dominant negative PKCδ significantly increased AngII-induced CTGF expression, whereas expression of wild type PKCδ inhibited this induction. This inhibitory effect was further confirmed in the myocardium of transgenic mice with cardiomyocyte-specific overexpression of PKCδ (δTg mice). Thus, AngII can regulate CTGF expression in cardiomyocytes through a PKC activation-mediated pathway in an isoform-selective manner both in physiological and diabetic states and may contribute to the development of cardiac fibrosis in diabetic cardiomyopathy.
Archive | 1992
George L. King; Teruo Shiba; Edward P. Feener; Ramesh C. Nayak
Vascular complications affect all diabetic patients to some extent and involve both microvessels and macrovessels. In this chapter we discuss studies that show the effects of elevated glucose levels on the metabolism of retinal and aortic vascular cells in culture.
Diabetes Care | 1999
Sven-Erik Bursell; Allen C. Clermont; Lloyd Paul Aiello; Lloyd M. Aiello; Deborah K. Schlossman; Edward P. Feener; Lori Laffel; George L. King
Journal of Biological Chemistry | 1991
F J Oliver; G de la Rubia; Edward P. Feener; Mu-En Lee; Mary R. Loeken; Teruo Shiba; Thomas Quertermous; George L. King
Journal of Biological Chemistry | 1993
Edward P. Feener; Jonathan M. Backer; George L. King; Peter A. Wilden; Xiao Jian Sun; C R Kahn; Morris F. White
Journal of Biological Chemistry | 2002
Izumi Suzuma; Kiyoshi Suzuma; Kohjiro Ueki; Yasuaki Hata; Edward P. Feener; George L. King; Lloyd Paul Aiello
Heart failure monitor | 2001
Edward P. Feener; George L. King
Biochemical Journal | 1994
Edward P. Feener; Teruo Shiba; Kang-Quan Hu; P. A. Wilden; M. F. White; George L. King