Modulation of CD11b/CD18 on monocytes and granulocytes following hemodialysis membrane interaction in vitro.
We studied the generation of CD11b/CD18 mobilizing factors in serum after incubation with dialysis membrane fragments of different chemical composition. We also evaluated the relative importance of the alternative and classical pathways of the complement system in the generation of such factors. Monocytes and granulocytes from healthy blood donors were incubated in normal human serum (NHS) and in NHS that had been preincubated with Cuprophan (CU) membrane (NHS-CU), Hemophan (HE) (NHS-HE) or polysulfone (PS) (NHS-PS). NHS-CU caused the highest up-regulation of the CD11b/CD18 receptor on monocytes and granulocytes. The rank in capacity to mobilize CD11b/CD18 on granulocytes was CU > HE > PS (p < 0.001), CU > HE (p < 0.05) and HE > PS (p < 0.001). The rank in capacity to mobilize CD11b/CD18 on monocytes was CU > HE > PS (p < 0.001), CU > HE (p < 0.05) and HE > PS (p < 0.01). NHS-PS induced a lower up-regulation of CD11b/CD18 compared to NHS which indicates that serum factors with the ability to mobilize the CD11b/CD18 receptor on monocytes and granulocytes are deposited on or absorbed by PS. In order to study the relative contribution of the alternative and classical pathways of the complement system in the generation of CD11b/CD18 mobilizing factors in serum, three different serum preparations (1. both pathways intact. 2. only the alternative intact and 3. only the classical pathway intact) were used. The CU membrane activated the classical pathway to a larger extent than the PS membrane (p < 0.01). When only the alternative pathway was intact no difference in the generation of CD11b/CD18 mobilizing factors between the CU and PS membranes was observed. These studies show that CD11b/CD18 mobilizing serum factors are generated after incubation with CU membranes and that such factors are probably adsorbed by PS. The classical pathway of complement activation seems to contribute to the generation of CD11b/CD18 mobilizing factors in serum.
Thylén
P
P
Department of Internal Medicine, Karolinska Hospital, Stockholm, Sweden.
Fernvik
E
E
Lundahl
J
J
Hed
J
J
Jacobson
S H
SH
D001672:Biocompatible Materials / Q000009:adverse effects* / Q000378:metabolism; D018845:CD11 Antigens / Q000097:blood*; D018821:CD18 Antigens / Q000097:blood*; D015815:Cell Adhesion Molecules / Q000378:metabolism; D002482:Cellulose / Q000009:adverse effects / Q000031:analogs & derivatives / Q000097:blood; D003167:Complement Activation / Q000187:drug effects; D005434:Flow Cytometry; D006098:Granulocytes / Q000166:cytology / Q000187:drug effects / Q000276:immunology*; D006801:Humans; D008567:Membranes, Artificial; D009000:Monocytes / Q000166:cytology / Q000187:drug effects / Q000276:immunology*; D011108:Polymers / Q000009:adverse effects / Q000378:metabolism; D006435:Renal Dialysis; D013194:Staining and Labeling; D013329:Structure-Activity Relationship; D013450:Sulfones / Q000009:adverse effects / Q000378:metabolism
D001672:Biocompatible Materials; D018845:CD11 Antigens; D018821:CD18 Antigens; D015815:Cell Adhesion Molecules; D008567:Membranes, Artificial; D011108:Polymers; D013450:Sulfones; C054645:Hemophan; C017662:polysulfone P 1700; D002482:Cellulose; C009865:cuprammonium cellulose