Article citationsMore>>
Silva Lde, P., Patah, P.A., Saliba, R.M., Szewczyk, N.A., Gilman, L., Neumann, J., Han, X.Y., Tarrand, J., Ribeiro, R., Gulbis, A., Shpall, E.J., Jones, R., Popat, U., Walker, J.A., Petropoulos, D., Chiattone, A., Stewart, J., El-Zimaity, M. anderlini, P., Giralt, S., Champlin, R.E. and de Lima, M. (2010) Hemorrhagic cystitis after allogeneic hematopoietic stem cell transplants is the complex result of BK virus infection, preparative regimen intensity and donor type. Haematologica, 95, 1183-1190.
doi:10.3324/haematol.2009.016758
has been cited by the following article:
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TITLE:
Cyclophosphamide induces an early wave of acrolein-independent apoptosis in the urothelium
AUTHORS:
Francis M. Hughes, Alexa G. Corn, Andrew R. Nimmich, Jeffery D. Pratt-Thomas, J. Todd Purves
KEYWORDS:
Cystitis; Cyclophosphamide; Apoptosis; Bladder; Urothelium
JOURNAL NAME:
Advances in Bioscience and Biotechnology,
Vol.4 No.8B,
August
8,
2013
ABSTRACT:
Hemorrhagic cystitis (HC) affects a significant number of patients undergoing cyclophosphamide (CP) chemotherapy despite treatment
with 2-mercaptoethane sulfonate
(Mesna) to inactivate the metabolite acrolein. While the mechanism is unknown,
there is clearly acrolein-independent damage to the urothelium. In this study
we have explored the induction of apoptosis in the urothelium as a marker of
damage and the mechanism underlying the acrolein-independent apoptosis. Two
waves of apoptosis (measured as caspase-3/7 activity and Poly (ADP-ribosyl) polymerase (PARP) cleavage) were detected following CP administration, one peaking
at 2 h and a second at 48 h. The first wave was not blocked by Mesna, indicating
it was independent of acrolein. Caspase-1 was also active at 2 h and activation
of caspase-3/7 was blocked by a caspase-1 inhibitor, but not an IL-1 receptor
antagonist, suggesting the direct activation of caspase-3/7 by caspase-1
without the need for IL-1 as an intermediate. Our results indicate that CP
initiates an early, acrolein-independent wave of apoptosis that results from
direct cleavage of caspase-3/7 by caspase-1.
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