Get access

Time-dependent loss of surface complement regulatory activity during storage of donor blood

Authors

  • K.E. Long,

    Search for more papers by this author
    • 1

      Kristin E. Long, BA. Graduate Student. Medical Scientist Training Program, Case Western Reserve University.

  • R. Yomtovian,

    Corresponding author
      2Director. Blood Bank-Transfusion Med-icine Service, and Assistant Professor. Department of Pathology. Case Western Reserve University, 2085 Adelbrt Road, Cleveland, OH 44106.
    Search for more papers by this author
  • M. Kida,

    Search for more papers by this author
    • *

      Assistant Professor, De-partment of Pathology, University of Oklahoma.

    • 3

      Masatoshi Kida, MD. Resident, Department of Pathology. Case Western Reserve University;

  • J.J. Knez,

    Search for more papers by this author
    • 4

      Jansen J. Knez, BS, Graduate Student, Department of Pathology, Case Western Reserve University.

  • M.E. Medof

    Search for more papers by this author
    • 5

      M. Edward Medof, MD. PhD, Professor, Departments of Pathology and Medicine, Institute of Pathology, Case Western Resew University.


2Director. Blood Bank-Transfusion Med-icine Service, and Assistant Professor. Department of Pathology. Case Western Reserve University, 2085 Adelbrt Road, Cleveland, OH 44106.

Abstract

The survival of transfused red cells (RBCs) diminishes with time of in vitro storage in blood banks, but the molecular mechanisms underlying the slow but incessant deterioration are incompletely understood. To investigate the possibility that impaired resistance to autologous complement attack could play a role in this phenomenon, packed RBCs stored for variable periods were assayed for decay-accelerating factor (DAF) and CD59, two glycoinositol-phospholipid (GPI)-anchored, membrane- associated complement regulatory proteins that function physiologically to protect blood cells from autologous complement activation on their surfaces. Immunoradiometric and flow cytometric assays employing DAF and CD59 monoclonal antibodies showed that levels of both surface proteins gradually declined over 6 weeks. Digestion analyses with phosphatidylinositol-specific phospholipase C, an enzyme that releases GPI-anchored proteins from cell surfaces, showed that DAF and CD59 molecules with GPI anchors containing unacylated inositol were preferentially lost. These findings suggest: 1) that DAF and CD59 molecules with acylated GPI anchors are more stable in RBC membranes than are molecules with unacylated GPI anchors, and 2) that DAF and CD59 loss may participate with other membrane alterations that occur during in vitro storage in compromising the survival of transfused cells.

Get access to the full text of this article

Ancillary