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

Immunopharmacology. 1997 Dec;38(1-2):129-40. doi: 10.1016/s0162-3109(97)00066-0.

Abstract

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.

MeSH terms

  • Aging / immunology
  • Alleles
  • Calcimycin / pharmacology
  • Complement C1r / genetics*
  • Complement C4b / immunology
  • Complement Inactivator Proteins*
  • Complement Membrane Attack Complex / metabolism
  • Erythrocytes / drug effects
  • Erythrocytes / immunology*
  • Exocytosis / drug effects*
  • Exocytosis / immunology
  • Flow Cytometry
  • Glycoproteins*
  • Humans
  • Immunohistochemistry
  • Ionophores / pharmacology
  • Microscopy, Electron
  • Papain / pharmacology
  • Polymorphism, Restriction Fragment Length
  • Receptors, Complement / drug effects*
  • Receptors, Complement 3b / drug effects*
  • Synaptic Vesicles / drug effects
  • Synaptic Vesicles / metabolism

Substances

  • Complement Inactivator Proteins
  • Complement Membrane Attack Complex
  • Glycoproteins
  • Ionophores
  • Receptors, Complement
  • Receptors, Complement 3b
  • Calcimycin
  • Complement C4b
  • Complement C1r
  • Papain