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The inhibition of the mitogenic stimulation of lymphocytes-b by a serine protease inhibitor - commitment to proliferation correlates with an enhanced expression of a cell-associated arginine-specific serine enzyme

Academic Article
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Overview

authors

  • Ku, G. S. B.
  • Quigley, James
  • Sultzer, B. M.

publication date

  • 1983

journal

  • Journal of Immunology  Journal

abstract

  • By the use of diisopropylfluorophosphate (DFP) we have been able to show that the mitogenic stimulation of murine B lymphocytes can be maximally inhibited a few hours before commitment of the cells to DNA synthesis. This inhibition was shown to be specific for a serine enzyme(s). The results of experiments designed to determine the location of this enzyme indicated that the mitogens-linked serine enzyme is not a secreted extracellular factor but is cell-associated. Fluorographic analysis of electrophoretic gels of cell homogenates labeled with [3H]DFP revealed the presence of one major and three minor bands which were arginine-specific serine enzymes. In stimulated cells, there was a clear quantitative difference in the amount of [3H]DFP bound to the major band (approx. 23,000 m.w.) suggesting that this protein may be critical to the progression of the cells through the cell cycle into the S phase of DNA synthesis.

subject areas

  • Animals
  • Arginine
  • B-Lymphocytes
  • DNA
  • Endopeptidases
  • Female
  • Isoflurophate
  • Lymphocyte Activation
  • Mice
  • Mice, Inbred CBA
  • Plasminogen Activators
  • Protease Inhibitors
  • Serine Endopeptidases
  • Substrate Specificity
  • Tosylarginine Methyl Ester
  • Tuberculin
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Identity

International Standard Serial Number (ISSN)

  • 0022-1767

PubMed ID

  • 6355295
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Additional Document Info

start page

  • 2494

end page

  • 2499

volume

  • 131

issue

  • 5

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