Antigenic Alteration of Red Cell Surfaces Exposed to Enzymatic Actions of Autologous Polymorphonuclear Leukocytes

Abstract

Isolated polymorphonuclear leukocytes induce alterations of the antigen receptor mosaic of autologous red cell surfaces in vitro. Such alterations are represented by decreased expression or loss of MN receptors and the ‘appearance’ of HLe^b- and Le^a-like receptor activities, which can be demonstrated by means of reactions of leukocyteexposed erythrocytes with anti-H lectins and heterologous anti-Le sera and by specific inhibition of these reactions. Since the receptor changes observed were most pronounced on the surfaces of secretar erythrocytes and since demonstrable Lewis-type modifications could not be created on erythrocytes of nonsecretors in these investigations, the antigenic polymorphism unmasked by contact of red cells with polymorphonuclear leukocytes was genetically limited to some extent. These limitations are perhaps due to restricted antigenic variability of the nonsecretor erythrocyte membrane components. The receptormodifying activity is confined to particle fractions of polymorphonuclear leukocytes; it is thermostable up to 70 °C, destroyed at 80 °C, blocked by α(1)-antitrypsin and other natural protease inhibitors, and reaches its peak at physiological pH values between 7.2 and 7.4. These properties correspond with those of the particulate neutral protease of human polymorphonuclear leukocytes. However, glycosidases probably also play a role.

Effects on Blood Group Antigens from Storage at Low Ionic Strength in the Presence of Neomycin

“…Under these conditions there is loss of the N antigen without detectable change in the M antigen as defined by human antisera as well as loss of Leb and H activity [16]. These observations support the proposed interpre tation that WBC derived components can produce antigen changes in stored RBC.…”

Degradation of glycophorin A of human erythrocytes in patients with myelo‐ or lymphoproliferative disorders: possible role of neutrophil proteases

“…Oxygen metabolites and proteolytic enzymes liberated from stimulated PMN are considered to be responsible for these phenomena. Oxidative and proteolytic injury of erythrocytes in vivo was found to be associated with K þ ions leakage (Claster et al, 1987), increased binding of immunoglobulins (Weiss et al, 1992) and haemoglobin (Claster et al, 1991) to the membrane components and with changes in expression of the surface antigenic determinants (Arend & Malchow, 1974). Degradation of the membrane proteins and antigenic alterations also seem to be involved in the processes of erythrocyte aging (for review see Bartosz, 1991).…”

Erythrocyte Endogenous Proteinase Activity during Blood Bank Storage

“…These events can be ascribed to endogenous red cell proteinases since the hypothetical effect of leukocyte lyso somal enzymes for ghost proteolysis [1,2,18,19,21] could be excluded by experiments in which leukocytes were re moved or where the addition of preservative solution did not result in WBC degranulation. Therefore, we hypothe size that damage to membrane structure during storage [22] may induce a subsequent susceptibility of ghost proteins to the action of endogenous proteinases.…”

“…Studies on red blood cell abnormalities during storage revealed changes in membrane antigen expression resem bling those accompanying proteolytic modification of the red cell [1][2][3] ; these alterations appear to be more relevant when red cells are stored in protein-free media [3]. How ever, the previously published data primarily explored sur face-exposed red blood cell antigens with the aid of serolog ical techniques and not the structural changes of membrane proteins.…”

“…How ever, the previously published data primarily explored sur face-exposed red blood cell antigens with the aid of serolog ical techniques and not the structural changes of membrane proteins. It has been suggested that proteinases released by granulocytes during storage may promote red blood cell membrane alterations leading to a loss of antigen sites as well as increased hemolysis [1][2][3], Several authors have reported on the presence and the activity of cytosolic and membrane-bound erythrocyte proteinases [4][5][6][7][8][9][10], which may also account for postsynthetic abnormalities of red cell membrane proteins [11][12][13].…”