Proline Rich Polypeptide (PRP-1) Increases the Superoxide-Producing and Ferrihemoglobin Reducing Activities of Cytochrome B558 Isoforms from Human Lymphosarcoma Tissue Cells

• Published in: Neurochemical research Vol. 36; no. 5; pp. 739 - 745
• Main Authors: Simonyan, G. M., Galoian, K. A., Simonyan, R. M., Simonyan, M. A., Galoyan, A. A.
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01-05-2011
• Subjects: Biochemistry; Biomedical and Life Sciences; Biomedicine; Cell Biology; Neurochemistry; Neurology; Neurosciences; Original Paper; Human lymphosarcoma; Reactive oxygen species; Cytochrome b; Prolin rich polypeptide; Metalloproteins; NADPH oxidase
• ISSN: 0364-3190; 1573-6903
• DOI: 10.1007/s11064-010-0389-7

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.