Prevention of hyperacute rejection by phosphatidylinositol-anchored mini-complement receptor type 1
Autor: | Masato Ikawa, Ryota Shirakura, Hikaru Matsuda, Shoki Mikata, Masao Yoshitatsu, Masaru Okabe, Shuji Miyagawa |
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Rok vydání: | 1998 |
Předmět: |
Graft Rejection
DNA Complementary Glycosylphosphatidylinositols Swine Transplantation Heterologous Immunology Complement factor I Biology Transfection Mice chemistry.chemical_compound Complement Receptor Type 1 Animals Humans Immunology and Allergy Endothelium Phosphatidylinositol Receptor Decay-accelerating factor Transplantation CD55 Antigens CD46 Molecular biology Complement system chemistry Factor H Receptors Complement 3b |
Zdroj: | Transplant Immunology. 6:107-110 |
ISSN: | 0966-3274 |
Popis: | Complement receptor type 1 (CR1, CD35) contains both factor I cofactor activity and convertase decay accelerating activity, but is, in general, thought to be an extrinsic regulator of complement activation. In this study, we prepared a phosphatidylinositol (PI)-anchored mini-CR1, which is composed of the short consensus repeat (SCR) 8-11 of CR1 and the PI anchor of DAF, and expressed it stably on a swine endothelial cell (SEC) line. We then examined the intrinsic regulatory activity of the mini-CR1, with respect to complement-mediated cell lysis as an in vitro hyperacute rejection model of a swine to human discordant xenograft. Flowcytometric profiles of the stable SEC lines with mini-CR1 showed a moderate level of expression for this molecule. Mini-CR1 blocked human complement-mediated cell lysis by approximately 50-70% on SEC. From the data of this study and our previous studies, mini-CR1 was more effective than membrane cofactor protein (MCP, CD46), and as effective as decay accelerating factor (DAF, CD55) in this system. The results suggest that PI-anchored mini-CR1 represents a useful molecule for clinical xenotransplantation. |
Databáze: | OpenAIRE |
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