Splenectomy prolongs in vivo survival of erythrocytes differently in spectrin/ankyrin- and band 3–deficient hereditary spherocytosis

The red pulp of the cat spleen, including terminal segments of arterial capillaries, pulp venules, and the reticular meshwork, was studied by transmission electron microscopy. Splenic congestion and contraction were produced by barbiturate anesthetic and norepinephrine.



Terminal segments of arterial capillaries were ampullary and flared. Blood escaped into surrounding pulp spaces through interendothelial gaps. Pulp venules originated as open-ended vessels in the reticular meshwork near trabeculae and drained into trabecular veins. Venule walls were thin and composed of squamous endothelial cells, a continuous basement membrane, and reticular cells. Venules in congested spleens had many mural apertures, but venules in contracted spleens had few. The interstices of the reticular meshwork in congested spleens contained large amounts of blood, which often was concentrated, many macrophages, lymphocytes, and plasma cells. Fewer blood cells and scant plasma were present in contracted spleens.



The vascular arrangements are anatomically open. Blood takes pathways through the reticular meshwork from arterial terminations to pulp venules. Some pathways through the reticular meshwork probably function as closed vascular channels conveying rapidly flowing blood. Other pathways are functionally open and probably contain slowly moving blood that constitutes a reservoir of red cells.



Macrophages formed associations with mature red cells and with reticulocytes. Mature red cells were attached to macrophages in a manner indicating erythrophagocytosis. Reticulocyte attachment had a different appearance and likely resulted in reticulocyte sequestration. Platelets bore pseudopodia which would impede their passage through irregular and cell-filled pulp spaces. The change in platelet shape probably is responsible for the formation of the splenic pool of platelets.

Vascular pathways in nonsinusal red pulp--an electron microscope study of the cat spleen.

Hypergammaglobulinemia can be associated with a positive direct antiglobulin test, a nonreactive eluate, and no evidence of hemolysis.

Binding of autologous IgG to human red blood cells before and after ATP-depletion. Selective exposure of binding sites (autoantigens) on spectrin-free vesicles.

Summary
Naturally occurring anti-band 3 antibodies (anti-band 3 NAbs) are directed against the 55-kDa chymotryptic fragment of the anion transport protein (band 3) of red blood cells (RBCs). They bind to senescent and oxidatively stressed RBCs and induce their selective clearance. These IgG NAbs exist at low concentrations, and have a weak affinity that prevents them from actively recruiting second binding sites. Cellular senescence or oxidative damage induces a cascade of biochemical events that results in the detachment of band 3 from the cytoskeleton and in clustering of band 3 protein by bound hemichromes and Syk kinase. Clustered band 3 proteins allow bivalent binding of anti-band 3 NAbs. Bivalently bound anti-band 3 NAbs have the unique capacity to stimulate C3b deposition by preferentially generating C3b2-IgG complexes, which act as potent C3 convertase precursors of the alternative complement pathway. Antibody binding not only to clustered, but also to oligomerized band 3 protein further increases if the human plasma also contains induced anti-lactoferrin antibodies. These bind to the polylactosaminyl oligosaccharide, a carbohydrate that exists in lactoferrin and in the 38-kDa fragment of band 3 protein. Anti-lactoferrin antibodies are found primarily in plasma of patients with autoimmune diseases and who have anti-neutrophil cytoplasmic antibodies (ANCA).

/pdf/naturally-occurring-anti-band-3-antibodies-in-clearance-of-4ytbhy0kyb.pdf

Naturally Occurring Anti-Band 3 Antibodies in Clearance of Senescent and Oxidatively Stressed Human Red Blood Cells

Red blood cell associated IgG in normal and pathologic states

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Red blood cell associated IgG in normal and pathologic states