title: Cell-associated adhesion molecules as early markers of bioincompatibility.
abstract: BACKGROUND
  Transient nature of adhesive interactions occurring during cell margination is mainly dependent on expression of selectins which are shed by activated cells. This shedding in the circulation may play an important role as anti-inflammatory mediator. Haemodialysis is also associated with P-selectin (CD62P)/sialyl-Lewis(x) (CD15s) interactions which mediate platelet-leukocyte coaggregation. We further investigated the mechanisms underlying leukocyte margination during haemodialysis.
  
  
  METHODS
  CD15s, CD11b and CD61 expression on circulating leukocytes from patients dialysed on synthetic membranes (modified polyacrylonitrile (SPAN), polysulphone (PS), and polyacrylonitrile (AN69) was assessed by cytofluorometry in a prospective crossover trial. We measured plasma levels C3a/C3a desArg, soluble CD62P, and CD62E molecules obtained from patients and healthy individuals.
  
  
  RESULTS
  Expression of CD11b and CD15s was upregulated on neutrophils from patients dialysed with SPAN and PS membranes during the dialysis session. A significant negative correlation was found between the expression of CD11b or CD15s molecules and neutrophil counts as well as between CD15s expression and monocyte counts during haemodialysis. As assessed by CD61 expression on leukocytes, we observed that platelets bound significantly onto both neutrophils and monocytes during dialysis with both membranes. A significant positive correlation was found between the expression of CD11b molecules and the percentage of CD61+ monocytes counts during SPAN and PS dialysis. We found a significant increase of soluble CD62P in plasma samples obtained from haemodialysed patients before the dialysis session as compared to the levels detected in plasma from healthy individuals.
  
  
  CONCLUSIONS
  This study documents a major role of CD15s, CD11b, CD61, CD62P molecules in the transient leukocytes activation and margination during haemodialysis on synthetic membranes despite their low complement-activating properties.
authors.affiliation: Institut National de la Santé et de la Recherche Médicale (INSERM U430), Hôpital Broussais, Paris, France.
authors.forename: M P
authors.initials: MP
authors.lastname: Carreno
authors.forename: S
authors.initials: S
authors.lastname: Stuard
authors.forename: M
authors.initials: M
authors.lastname: Bonomini
authors.forename: N
authors.initials: N
authors.lastname: Settefrati
authors.forename: C
authors.initials: C
authors.lastname: Tetta
authors.forename: A
authors.initials: A
authors.lastname: Albertazzi
authors.forename: N
authors.initials: N
authors.lastname: Haeffner-Cavaillon
mesh_terms: D000328:Adult; D000368:Aged; D015703:Antigens, CD / Q000032:analysis*; D001672:Biocompatible Materials; D015415:Biomarkers; D018845:CD11 Antigens / Q000032:analysis*; D002448:Cell Adhesion; D005260:Female; D006801:Humans; D039661:Integrin beta3; D007674:Kidney Diseases / Q000097:blood* / Q000628:therapy; D016256:Lewis X Antigen / Q000032:analysis*; D008297:Male; D008875:Middle Aged; D009504:Neutrophils / Q000378:metabolism* / Q000473:pathology; D010980:Platelet Membrane Glycoproteins / Q000032:analysis*; D006435:Renal Dialysis / Q000295:instrumentation
chemical_list: D015703:Antigens, CD; D001672:Biocompatible Materials; D015415:Biomarkers; D018845:CD11 Antigens; D039661:Integrin beta3; D016256:Lewis X Antigen; D010980:Platelet Membrane Glycoproteins