OXYGEN RADICAL TOXICITY AND RED CELL PROTEIN DEGRADATION
Project Number2R01ES003598-04
Contact PI/Project LeaderDAVIES, KELVIN J. A.
Awardee OrganizationUNIVERSITY OF SOUTHERN CALIFORNIA
Description
Abstract Text
In recent years it has become increasingly apparent that free
radicals, and related oxidants, play important roles numerous
toxicological processes.
The long-term goal of this research is to understand the mechanisms
of cellular antioxidant protection against environmental and
metabolic toxins.
The objective of this application is to test the following
hypothesis; "Oxygen radicals and other activated oxygen species,
oxidatively denature or fragment hemoglobin, superoxide dismutase,
and other red blood cell proteins. Such modified proteins are
recognized and rapidly degraded by a red cell proteolytic system
which includes a high molecular weight (approximately 700-kDa) ATP-
independent, neutral, endo-protease, and several peptidases. By
preventing the aggregation of denatured proteins, as well as the
potential toxicity of protein fragments, this proteolytic system
acts as a line of "Secondary Antioxidant Defense" for the red cell.
Secondary Antioxidant functions for proteolytic systems in other
cells may be a general biological phenomenon.
The specific aims of this proposal are to quantify and describe
protein damage and degradation in intact erythrocytes and
reticulocytes, the modification of proteins (particularly
hemoglobin and superoxide dismutase) by active oxygen species, the
degradation of modified proteins in cell-free extracts of red blood
cells, and comparative measurements in E. coli. Major specific
aims also include, the purification and characterization of the
red cell 700-kDa protease, production of polyclonal antibodies
against the protease and its subunits, and cloning the protease
subunits in E. coli (using a phage expression vector).
The approaches and methodology include: proteolysis measures with
cell, and purified (labeled) protein modification by
spectrophotometry, fluorometry, scintillation counting, HPLC, LC,
electrophoresis, and IEF; chromatographic isolation of the 700-kDa
protease, generation of antibodies against the protease, and
construction of an affinity column; cloning the protease subunits
in bacteria and construction of a cDNA library (using a lambda gt11
expression vector).
The relationship to health concerns involves: 1) The toxicity of
many "rodox active" xenobiotics (environmental agents and drugs);
2) The defenses of cells against oxidative stresses, in health and
disease; 3) Adaptive responses to toxins and stress.
National Institute of Environmental Health Sciences
CFDA Code
DUNS Number
072933393
UEI
G88KLJR3KYT5
Project Start Date
15-June-1985
Project End Date
31-January-1993
Budget Start Date
15-February-1988
Budget End Date
31-January-1989
Project Funding Information for 1988
Total Funding
$195,880
Direct Costs
$132,390
Indirect Costs
$63,490
Year
Funding IC
FY Total Cost by IC
1988
National Institute of Environmental Health Sciences
$195,880
Year
Funding IC
FY Total Cost by IC
Sub Projects
No Sub Projects information available for 2R01ES003598-04
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