Ceruloplasmin inhibits carbonyl formation in endogenous proteins in phorbol myristate acetate (PMA)-stimulated neutrophils
- St. Louis Univ., MO (United States)
The respiratory burst of stimulated neutrophils can cause oxidative modifications of endogenous neutrophil proteins as measured by increased carbonyl formation. Ceruloplasmin is an acute phase protein and may act as an antioxidant during inflammation. Therefore, the role of ceruloplasmin in preventing oxidative damage of endogenous neutrophil proteins was investigated. Protein carbonyl content was determined spectrophotometrically using 2,4-dinitrophenylhydrazine. Ceruloplasmin, at a concentration present during inflammation significantly inhibited carbonyl formation in endogenous proteins of PMA-stimulated neutrophils. In order to determine if oxidative damage was occurring to the ceruloplasmin upon incubation with stimulated neutrophils, carbonyl formation in the ceruloplasmin in the presence and absence of stimulated neutrophils. This data suggests that ceruloplasmin may play a role in regulating oxidative damage to proteins and that ceruloplasmin itself may act as a target for these modifications.
- OSTI ID:
- 5751707
- Report Number(s):
- CONF-9104107-; CODEN: FAJOE
- Journal Information:
- FASEB Journal (Federation of American Societies for Experimental Biology); (United States), Vol. 5:4; Conference: 75. annual meeting of the Federation of American Societies for Experimental Biology (FASEB), Atlanta, GA (United States), 21-25 Apr 1991; ISSN 0892-6638
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
CARBONYLS
BIOSYNTHESIS
CERULOPLASMIN
BIOLOGICAL FUNCTIONS
PHORBOL ESTERS
BIOLOGICAL EFFECTS
NEUTROPHILS
PROTEINS
SPECTROPHOTOMETRY
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARCINOGENS
COMPLEXES
COPPER COMPLEXES
ESTERS
GLOBULINS
GLOBULINS-ALPHA
LEUKOCYTES
MATERIALS
METALLOPROTEINS
ORGANIC COMPOUNDS
SYNTHESIS
TRANSITION ELEMENT COMPLEXES
560300* - Chemicals Metabolism & Toxicology