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Proline rich polypeptide (PRP-1) increases the superoxide-producing and ferrihemoglobin reducing activities of cytochrome B(558) isoforms from human lymphosarcoma tissue cells.

Abstract
The two cytochromes (cyt) b(558) 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 O(2)(-)-producing and ferrihemoglobin-reducing activities. The incubation of neuropeptide PRP-1 (5 μg) with cytochrome b(558), caused elevation of these activities. The gel filtration results indicated possible binding of PRP-1 to these cytochromes b(558). PRP-1 activated both NADPH dependent O(2)(-)-producing and ferriHb-reducing activities of the cyt b(1)(558) and cyt b(2)(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 O(2)(-)-producing and ferriHb-reducing activities of cyt b(558), 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.
AuthorsG M Simonyan, K A Galoian, R M Simonyan, M A Simonyan, A A Galoyan
JournalNeurochemical research (Neurochem Res) Vol. 36 Issue 5 Pg. 739-45 (May 2011) ISSN: 1573-6903 [Electronic] United States
PMID21213045 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Cytochrome b Group
  • Isoenzymes
  • PRP-1 peptide
  • Peptides
  • Superoxides
  • Methemoglobin
  • cytochrome b558
  • NADPH Oxidase
Topics
  • Cytochrome b Group (metabolism)
  • Humans
  • Isoenzymes (metabolism)
  • Methemoglobin (metabolism)
  • NADPH Oxidase (metabolism)
  • Peptides (pharmacology)
  • Spectrum Analysis (methods)
  • Superoxides (metabolism)
  • Tumor Cells, Cultured

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