Catabolism of the human erythrocyte C3b/C4b receptor (CR1, CD35): Vesiculation and/or proteolysis?

Xavier Dervillez, Stéphane Oudin, Marcelle Tonye Libyh, Thierry Tabary, Brigitte Reveil, Frédérique Philbert, Francine Bougy, Michel Pluot, Jacques H.M. Cohen*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

20 Citations (Scopus)


Human erythrocytes (E) react by exocytosis of membrane vesicles to various stresses including the fixation of the membrane attack complex of Complement. E from normal individuals loose a notable proportion of their initial number of surface CR1 molecules during the ageing process. An acquired decrease of CR1 on E also occurs in pathological conditions such as Systemic Lupus Erythematosus or AIDS. The present study investigated whether calcium ionophore A23187 (Ca-ion) induced vesicle formation of human E in vitro is responsible for a preferential loss of CR1 as well as whether CR1 molecules at the surface of Ca-ion treated E or vesicles are: (i) functional, (ii) native or protease degraded, or (iii) more clustered than CR1 on native E. A study of E from 137 normal individuals showed that a one-hour Ca-ion induced vesicle formation preferentially removed one third of E surface CR1. Kinetic experiments suggested that all surface CR1 could be removed from E upon longer incubation times. CR1 molecules on vesicles were still able to inhibit Complement activation, and were found in larger clusters than on native E. These data suggest that a significant part of surface CR1 molecules may be removed from E by vesicle formation during the life of E in normal individuals. This phenomenon could be exacerbated in pathological conditions.

Original languageEnglish
Pages (from-to)129-140
Number of pages12
Issue number1-2
Publication statusPublished - Dec 1997
Externally publishedYes


  • Calcium ionophore A23187
  • Complement receptor type 1 (CR1)
  • Electron microscopy
  • Erythrocyte
  • Exocytosis
  • Flow cytometry


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