Studies with Monospecific Antisera against Complement Components in Cold Agglutinin Disease1

The Unitary Nature of "Complete" and "Incomplete" Pathologic Cold Hemagglutinins

Blood ◽

10.1182/blood.v19.3.379.379 ◽

1962 ◽

Vol 19 (3) ◽

pp. 379-398 ◽

Cited By ~ 13

Author(s):

JOHN P. LEDDY ◽

NORMA C. TRABOLD ◽

JOHN H. VAUGHAN ◽

SCOTT N. SWISHER

Keyword(s):

Anion Exchange Chromatography ◽

Exchange Chromatography ◽

Cold Agglutinin ◽

Complement Components ◽

Cold Agglutinins ◽

Zone Electrophoresis ◽

Human Sera ◽

Normal Human ◽

Physicochemical Methods ◽

Reduced Activity

Abstract Several human pathologic sera containing high titered cold agglutinins were studied to determine whether the serologic activity ascribed to an "incomplete cold antibody" could be separated from the "complete" cold agglutinin activity. Separation was not achieved by physicochemical methods, including zone electrophoresis, density gradient ultracentrifugation, and anion exchange chromatography. Both activities were susceptible to destruction by mercaptans. Neither activity could be differentially absorbed from the sera. Using "Bombay" and I-negative ("i") red cells, a difference in specificity of the two activities for the H or I antigen of human erythrocytes could not be demonstrated. The simplest interpretation of these findings is that there is only one antibody involved, the cold agglutinin, and that the serologic manifestation usually attributed to an additional "incomplete cold antibody", i.e. the production of a positive antiglobulin reaction of the "non-γ-globulin" type, results from an interaction of complement components with the cold agglutinin-erythrocyte complex. Three of these cold agglutinating sera were unreactive with I-negative erythrocytes, in keeping with the reported anti-I specificity of these antibodies. A fourth serum retained moderate, though greatly reduced, activity against these cells, and the interpretation of this finding is discussed. The anti-H specificity of the incomplete cold antibodies in normal human sera was confirmed by their failure to sensitize "Bombay" erythrocytes. This was in sharp contrast to the excellent reactivity of the pathologic sera with these cells, demonstrating that pathologic cold agglutinins are unrelated to the incomplete cold antibodies present in most normal sera.

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The variability of hemolysis in the cold agglutinin syndrome

Blood ◽

10.1182/blood.v56.3.409.409 ◽

1980 ◽

Vol 56 (3) ◽

pp. 409-416 ◽

Cited By ~ 44

Author(s):

WF Rosse ◽

JP Adams

Keyword(s):

Complement Activation ◽

Cold Agglutinin ◽

Complement Components ◽

Cold Agglutinins ◽

Thermal Amplitude

Abstract The amount of lysis effected by cold agglutinins is directly related to the ability of the antibody to initiate complement activation. This ability is modified by the concentration of antibody, its thermal amplitude (the highest temperature at which the antibody will react with the cell), the degree to which antibody fixation is modified by the presence of complement components (particularly C3) on the membrane, and the degree to which antibody, once fixed, is able to fix the components of complement. In vitro measurement of these factors correlates with the rate of hemolysis in vivo.

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The variability of hemolysis in the cold agglutinin syndrome

Blood ◽

10.1182/blood.v56.3.409.bloodjournal563409 ◽

1980 ◽

Vol 56 (3) ◽

pp. 409-416 ◽

Cited By ~ 4

Author(s):

WF Rosse ◽

JP Adams

Keyword(s):

Complement Activation ◽

Cold Agglutinin ◽

Complement Components ◽

Cold Agglutinins ◽

Thermal Amplitude

The amount of lysis effected by cold agglutinins is directly related to the ability of the antibody to initiate complement activation. This ability is modified by the concentration of antibody, its thermal amplitude (the highest temperature at which the antibody will react with the cell), the degree to which antibody fixation is modified by the presence of complement components (particularly C3) on the membrane, and the degree to which antibody, once fixed, is able to fix the components of complement. In vitro measurement of these factors correlates with the rate of hemolysis in vivo.

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Immunoenzymatic demonstration of the simultaneous presence of transferrin, hemopexin and albumin in a same hepatocyte and their ultrastructural localization

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100081309 ◽

1978 ◽

Vol 36 (2) ◽

pp. 88-89

Author(s):

M. Kraemer ◽

J. Foucrier ◽

J. Vassy ◽

M.T. Chalumeau

Keyword(s):

Plasma Proteins ◽

Rat Hepatocytes ◽

Ultrastructural Localization ◽

Carrier Proteins ◽

Normal Cells ◽

Adult Rat ◽

Adult Rat Hepatocytes ◽

Monospecific Antisera ◽

Different Levels

Some authors using immunofluorescent techniques had already suggested that some hepatocytes are able to synthetize several plasma proteins. In vitro studies on normal cells or on cells issued of murine hepatomas raise the same conclusion. These works could be indications of an hepatocyte functionnal non-specialization, meanwhile the authors never give direct topographic proofs suitable with this hypothesis.The use of immunoenzymatic techniques after obtention of monospecific antisera had seemed to us useful to bring forward a better knowledge of this problem. We have studied three carrier proteins (transferrin = Tf, hemopexin = Hx, albumin = Alb) operating at different levels in iron metabolism by demonstrating and localizing the adult rat hepatocytes involved in their synthesis.Immunological, histological and ultrastructural methods have been described in a previous work.

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Localization of cell-surface and basement-membrane heparan-sulfate proteoglycans using the malaria circumsporozoite protein

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100169201 ◽

1994 ◽

Vol 52 ◽

pp. 294-295

Author(s):

U. Frevert ◽

S. Sinnis ◽

C. Cerami ◽

V. Nussenzweig

Keyword(s):

Heparan Sulfate ◽

Protein A ◽

Kidney Tissue ◽

Plasmodium Species ◽

Its Region ◽

Basement Membranes ◽

Heparan Sulfate Proteoglycans ◽

Infected Mosquito ◽

Complement Components ◽

Region Ii

Malaria sporozoites, which invade hepatocytes within minutes after transmission by an infected mosquito, are covered with the circumsporozoite (CS) protein, which in all Plasmodium species contains the conserved region II-plus. This region is also found as a cell-adhesive motif in a variety of host proteins like thrombospondin, properdin and the terminal complement components.The CS protein with its region II-plus specifically binds to heparan sulfate proteoglycans (HSPG) on the basolateral surface of hepatocytes in the space of Disse (FIG. 1), to certain basolateral cell membranes and basement membranes of the kidney (FIG. 2) as well as to heparin in the granules of connective tissue mast cells. The distribution of the HSPG receptors for the CS protein was examined by incubation of Lowicryl K4M or LR White sections of liver and kidney tissue with the recombinant CS ligand, whose binding sites were detected with a monoclonal anti-CS antibody and protein A gold.

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Immunological Studies on the Blood Coagulation Factor X and Its Warfarin-induced Precursor

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649144 ◽

1974 ◽

Vol 31 (01) ◽

pp. 040-051 ◽

Cited By ~ 5

Author(s):

Gustav Gaudernack ◽

Åse Gladhaug Berre ◽

Bjarne Østerud ◽

Hans Prydz

Keyword(s):

Coagulation Factor ◽

Factor X ◽

Intrinsic Pathway ◽

Coagulation Activity ◽

Factor X Deficiency ◽

Warfarin Treatment ◽

The Cross ◽

Monospecific Antisera ◽

Purified Antigen ◽

Congenital Factor

SummaryMonospecific antisera against the human coagulation factor X have been raised in rabbits by injections of purified antigen. Such antiserum was used to study the cross-reacting material without factor X activity which is present in the blood of warfarin-treated patients and animals as well as to study the changes in factor X during coagulation. One patient with congenital factor X deficiency was also studied.A complete identity was found between factor X in Macaca mulatta and human blood. During warfarin treatment antigenically cross-reacting material appeared in plasma. This was not adsorbed on BaSO4, and inhibited the coagulation activity of normal factor X.Both this material, normal factor X and the cross-reacting material in plasma from a patient congenitally deficient in factor X gave rise to split products during coagulation by the intrinsic pathway, i. e. all of them served as substrates for the intrinsic activator of factor X.

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