Mouse splenocyte blast transformation in the presence of plasma γ-globulin fraction proteins and their complexes with copper and zinc

Bull Exp Biol Med. 2011 Mar;150(5):624-6. doi: 10.1007/s10517-011-1206-2.

Abstract

Plasma γ-globulin fraction proteins, copper and zinc cations, and metal complexes formed by these cations and human serum γ-globulin induce blast transformation of splenocytes from BALB/c mice at a level comparable to that induced by concanavalin A. Zinc bound to γ-globulin reduces by 25% and copper in complex with this protein stimulates by 1.6 times its capacity to induce blast transformation. Combinations with concanavalin A reproduce the effects of γ-globulin-metal complex under conditions of mitogen induction. Incorporation of(3)H-thymidine in splenocytes incubated with combinations of γ-globulin-copper metalcomplex, copper cations, and control protein with concanavalin A was by 1.4, 1.3 (p<0.1), and 1.25 times higher (p<0.05), respectively, than after incubation with concanavalin A alone.

MeSH terms

  • Animals
  • Concanavalin A / pharmacology
  • Coordination Complexes / blood
  • Copper / blood*
  • Lymphocyte Activation / drug effects*
  • Mice
  • Mice, Inbred BALB C
  • Mitogens
  • Spleen / cytology*
  • Thymidine / metabolism
  • Zinc / blood*
  • gamma-Globulins / metabolism*

Substances

  • Coordination Complexes
  • Mitogens
  • gamma-Globulins
  • Concanavalin A
  • Copper
  • Zinc
  • Thymidine