Proline rich polypeptide (prp-1) increases the superoxide-producing and ferrihemoglobin reducing activities of cytochrome b558 isoforms from human lymphosarcoma tissue cells

G. M. Simonyan, K. A. Galoian, R. M. Simonyan, M. A. Simonyan, A. A. Galoyan

Research output: Contribution to journalArticle

2 Scopus citations

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 languageEnglish (US)
Pages (from-to)739-745
Number of pages7
JournalNeurochemical Research
Volume36
Issue number5
DOIs
StatePublished - May 1 2011

Keywords

  • Cytochrome b
  • Human lymphosarcoma
  • Metalloproteins
  • NADPH oxidase
  • Prolin rich polypeptide
  • Reactive oxygen species

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Biochemistry

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