Function of human factor H and I on xenosurface

Biochem Biophys Res Commun. 1999 Nov 19;265(2):556-62. doi: 10.1006/bbrc.1999.1713.

Abstract

The cell membrane-bound forms of mini-factor H with 1-4 short consensus repeats (fH-PI) and factor I (fI-PI) were constructed. Swine endothelial cell (SEC) lines and Chinese hamster ovary (CHO) cell expressing fH-PI or fI-PI were established and confirmed by flow cytometry. The cell lysate of the SEC line expressing fH-PI showed strong cofactor activity for the cleavage of C3b, and fI-PI demonstrated the protease activity for C4b and C3b not only in the fluid phase but also on the cell membrane. In addition, fH-PI blocked human complement-mediated cell lysis by approximately 30-40%. An SEC line with a low expression of fI-PI showed a weak inhibition of cell lysis in human serum, whereas a CHO cell transfectant with a high expression of fI-PI showed over a 60% inhibition of cell lysis. The results suggest that fH-PI and fI-PI have potential for use in clinical xenotransplantation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • CD55 Antigens / genetics
  • CD55 Antigens / metabolism
  • CHO Cells
  • Cell Line
  • Cell Membrane / metabolism
  • Complement Activation
  • Complement C3 / metabolism
  • Complement C4 / metabolism
  • Complement Factor H / chemistry
  • Complement Factor H / genetics
  • Complement Factor H / metabolism*
  • Cricetinae
  • DNA Primers / genetics
  • Fibrinogen / chemistry
  • Fibrinogen / genetics
  • Fibrinogen / metabolism*
  • Graft Rejection / prevention & control
  • Humans
  • Models, Biological
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Swine
  • Transfection
  • Transplantation, Heterologous

Substances

  • CD55 Antigens
  • CFH protein, human
  • Complement C3
  • Complement C4
  • DNA Primers
  • Recombinant Proteins
  • Complement Factor H
  • Fibrinogen