Abstract
The two cytochromes (cyt) b558 of acidic nature, one-95-100 kDa and another one, 60-70 kDa were isolated for the first time from the human's lymphosarcoma tissue cells using gel filtration and ion exchange chromatography. These hemoproteins possess NADPH dependent O2 --producing and ferrihemoglobin-reducing activities. The incubation of neuropeptide PRP-1 (5 μg) with cytochrome b558, caused elevation of these activities. The gel filtration results indicated possible binding of PRP-1 to these cytochromes b558. PRP-1 activated both NADPH dependent O2 --producing and ferriHb-reducing activities of the cyt b1 558 and cyt b2 558, obtained from human lymphosarcoma tissue cells. One can assume that PRP-1 associated with cyt b 558 on the surface of the tumor cells by increasing both NADPH dependent O2 --producing and ferriHb-reducing activities of cyt b558, increases the oxidation- reduction status. Changing the oxidation-reduction status and oxygen homeostasis of the tumor cells by PRP-1 can serve as one of the possible explanation of antitumorigenic effect of this cytokine.
Original language | English (US) |
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Pages (from-to) | 739-745 |
Number of pages | 7 |
Journal | Neurochemical Research |
Volume | 36 |
Issue number | 5 |
DOIs | |
State | Published - May 2011 |
Keywords
- Cytochrome b
- Human lymphosarcoma
- Metalloproteins
- NADPH oxidase
- Prolin rich polypeptide
- Reactive oxygen species
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience
- Biochemistry