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Human IL-1-beta processing and secretion in recombinant baculovirus-infected Sf9 cells is blocked by the cowpox virus serpin crmA

Academic Article
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Overview

authors

  • Howard, A. D.
  • Palyha, O. C.
  • Griffin, Patrick
  • Peterson, E. P.
  • Lenny, A. B.
  • Ding, G. J. F.
  • Pickup, D. J.
  • Thornberry, N. A.
  • Schmidt, J. A.
  • Tocci, M. J.

publication date

  • March 1995

journal

  • Journal of Immunology  Journal

abstract

  • Biologically active, mature IL-1 beta (mIL-1 beta) is released from activated monocytes after proteolytic processing from an inactive precursor (pIL-1 beta). IL-1 beta converting enzyme (ICE), the first member of a newly discovered family of cysteine proteinases, is required for this processing event. The cleaved cytokine is released from monocytes by an unknown mechanism which does not employ a standard hydrophobic signal sequence. As in mammalian fibroblasts, insect Sf9 cells do not normally process or secrete human IL-1 beta. The expression of active ICE enables Sf9 cells to process 31-kDa pIL-1 beta correctly at Asp27 and Asp116, and to export 17.5-kDa mIL-1 beta. The recombinant heterodimeric human enzyme purified from Sf9 cells possesses a sp. act. of 2.9 +/- 0.5 x 10(6) U/mg and is indistinguishable from native ICE with regard to its subunit composition and catalytic properties. In this system, co-expression of the cowpox virus crmA gene, an extremely potent serpin inhibitor of ICE (Ki < 7 pM), inhibits ICE activation completely and blocks pIL-1 beta processing and mIL-1 beta secretion by approximately 95%. The results indicate that ICE, in addition to its processing function, facilitates the transport of IL-1 beta across the plasma membrane.

subject areas

  • Amino Acid Sequence
  • Animals
  • Baculoviridae
  • Binding Sites
  • Caspase 1
  • Cell Line
  • Cowpox virus
  • Cysteine Endopeptidases
  • Humans
  • In Vitro Techniques
  • Interleukin-1
  • Kinetics
  • Molecular Sequence Data
  • Oligopeptides
  • Protein Processing, Post-Translational
  • Recombinant Proteins
  • Serpins
  • Spodoptera
  • Substrate Specificity
  • Viral Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0022-1767

PubMed ID

  • 7868902
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Additional Document Info

start page

  • 2321

end page

  • 2332

volume

  • 154

issue

  • 5

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