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Russ J Immunol. 1999 Jul;4(2):123-130.

Purification and Partial Characterization of a 14 kDa Protein Enhancing Mitogen-Stimulated Proliferation of Human Peripheral Blood Mononuclear Cells.

Russian journal of immunology : RJI : official journal of Russian Society of Immunology

Victor M. Paromov, Samira Bughlava, Natalia V. Malakhova, Mikhail V. Kiselevsky, Dmitry A. Dolgikh, Mikhail P. Kirpichnikov

Affiliations

  1. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.

PMID: 12687119

Abstract

Cytotoxicity of plasma free platelets or peripheral blood mononuclear cells (PBMCs) upon stimulation with Ca-ionophore A23187 at various (10(-9) - 10(-6) M) concentrations has been studied on human erythroid leukaemia cell line (K562). A 14 kDa protein, which did not display any cytotoxic activity to K562 cells, but stimulate PBMC proliferation has been isolated from the supernatant of plasma free platelets stimulated by 10(-7) M Ca-ionophore. The protein displayed a very slight mitogenic effect on PBMCs, but it enhanced proliferative response of PBMC stimulated by concanavalin A at suboptimal concentrations. The p14 N-terminal sequence ((1)VLERTXA(7)-) is identical to the region 99-103 residues of the human MHC class II antigen DQ-beta chain. Also, we identified this 14 kDa protein in the supernatant of PBMCs stimulated by 10(-7) M Ca-ionophore. Its N-terminal sequence (VLERTXA-) is identical to the one of p14 from the stimulated plasma-free platelet supernatant.

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