Note
Charles E. Schmidt College of Science
Member of
Contributors
Publisher
Florida Atlantic University
Date Issued
2006
EDTF Date Created
2006
Description
The excess generation of Reactive oxygen species (ROS) can damage
cell components and disrupt cellular functions. Methionine in proteins is easily
oxidized by ROS and converted to methionine sulfoxide. The enzyme peptide
Methionine Sulfoxide Reductase reduces methionine sulfoxide back to methionine.
We report here that MsrA over expression in rat cardiac myocytes prevents damage
from ROS and increases cell viability after hypoxic/reoxygenation events. The nonsteroidal
anti-inflamatory drug (NSAID) sulindac contains a methyl sulfoxide moiety
that can scavenge ROS. Sulindac can be reduced by MsrA and contribute as an
antioxidant in the cell. Our results demonstrate that 1 OOuM sulindac can reduce cell
death in rat cardiac myocytes during hypoxia/reoxygenation, and
ischemia/reperfusion in Langendorf[ perfusions. The BNIP proteins are pro-apoptotic
members of the Bcl-2 family of apoptosis regulating proteins. Hypoxia/acidosis
stabilizes BNIP-3 and increases its association with the mitochondria, causing the
release of cytochrome C and cell death. We report the retrograde perfusion
Langendorffmodel is inconclusive in mouse hearts.
cell components and disrupt cellular functions. Methionine in proteins is easily
oxidized by ROS and converted to methionine sulfoxide. The enzyme peptide
Methionine Sulfoxide Reductase reduces methionine sulfoxide back to methionine.
We report here that MsrA over expression in rat cardiac myocytes prevents damage
from ROS and increases cell viability after hypoxic/reoxygenation events. The nonsteroidal
anti-inflamatory drug (NSAID) sulindac contains a methyl sulfoxide moiety
that can scavenge ROS. Sulindac can be reduced by MsrA and contribute as an
antioxidant in the cell. Our results demonstrate that 1 OOuM sulindac can reduce cell
death in rat cardiac myocytes during hypoxia/reoxygenation, and
ischemia/reperfusion in Langendorf[ perfusions. The BNIP proteins are pro-apoptotic
members of the Bcl-2 family of apoptosis regulating proteins. Hypoxia/acidosis
stabilizes BNIP-3 and increases its association with the mitochondria, causing the
release of cytochrome C and cell death. We report the retrograde perfusion
Langendorffmodel is inconclusive in mouse hearts.
Language
Type
Form
Extent
41 p.
Subject (Topical)
Identifier
FA00000820
Additional Information
Charles E. Schmidt College of Science
Thesis (M.S.)--Florida Atlantic University, 2006.
Date Backup
2006
Date Created Backup
2006
Date Text
2006
Date Created (EDTF)
2006
Date Issued (EDTF)
2006
Extension
FAU
IID
FA00000820
Organizations
Attributed name: Florida Atlantic University
Person Preferred Name
Rickaway, Zach T.
Graduate College
Physical Description
application/pdf
41 p.
Title Plain
Tissue Protection and Cell Death Pathways in Myocardial Ischemia
Use and Reproduction
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Origin Information
2006
2006
Florida Atlantic University
Boca Raton, Fla.
Physical Location
Florida Atlantic University Libraries
Place
Boca Raton, Fla.
Sub Location
Digital Library
Title
Tissue Protection and Cell Death Pathways in Myocardial Ischemia
Other Title Info
Tissue Protection and Cell Death Pathways in Myocardial Ischemia