Calpain-calpastatin and fusion. Fusibility of erythrocytes is determined by a protease-protease inhibitor [calpain-calpastatin] balance

Tova Glaser*, Nechama S. Kosower

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Rat erythrocytes fuse when treated with the membrane mobility agent, 2-(2-methoxyethoxy)ethyl-cis-8-(2-octylcyclopropyl) octanoate (A2C) and Ca2+, whereas human cells do not. Membrane proteolysis promoted by calpain is required for rat cell fusion [(1986) Eur. J. Biochem., in press]. Human calpain induced a selective proteolysis in both the human and rat erythrocyte ghosts (mainly band 4.1 in the human, band 4.1 and band 3 in the rat cell) and rendered them fusible. Calpastatin (calpain inhibitor) prevented A2C-induced fusion in both ghosts, via inhibition of proteolysis. The human erythrocyte has excess calpastatin and resists A2C-promoted fusion. A regulatory role of calpastatin in membrane fusion is thus indicated.

Original languageEnglish
Pages (from-to)115-120
Number of pages6
JournalFEBS Letters
Volume206
Issue number1
DOIs
StatePublished - 29 Sep 1986

Keywords

  • Calpain/calpastatin
  • Erythrocyte membrane Membrane mobility agent
  • Fusogenic agent
  • Membrane fusion
  • Membrane proteolysis

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