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Biomedical subjects

D F Stroncek

Publications and source records attributed to D F Stroncek.

At least 73 records · Page 4Linked to original sources
PubMed1993

Psychosocial effects of unrelated bone marrow donation: experiences of the National Marrow Donor Program.

In this study, we investigated the psychosocial effects of unrelated marrow donation. Survey questionnaires were administered pre-donation, shortly post-donation, and 1 year post-donation to all donors through the National Marrow Donor Program over a 3-year period. Univariate, bivariate, and multivariate analyses were then performed. Donors were generally quite positive about the donation 1 year post-donation: 87% felt it was "very worthwhile" and 91% would be willing to donate again in the future. Marrow donors were more likely than kidney donors to feel better about themselves as a result of the donation (P < .001). Donors with longer collection times, in general, had less positive psychosocial outcomes from the donation. Donors who experienced lower back pain or difficulty walking as a result of the donation were more likely to experience the donation as more stressful and painful than expected, but no more likely to experience it as less positive emotionally than donors who did not experience these side effects.

Anesthesia↗
PubMed1993

Neutrophil alloantibodies react with cytoplasmic antigens: a possible cause of false-positive indirect immunofluorescence assays for antibodies to neutrophil cytoplasmic antigens.

Antibodies to neutrophil cytoplasmic antigens (ANCA) can be detected in patients with Wegener's granulomatosis and systemic vasculitis. During pregnancy or following transfusion, subjects sometimes produce alloantibodies to neutrophil antigens. If patient sera being tested for ANCA contain alloantibodies directed at neutrophil antigens that residue in the cytoplasm, the results may be difficult to interpret. At least one neutrophil antigen, NB1, is expressed on both neutrophil plasma membranes and secondary granules. We tested alloantibodies specific for neutrophil antigens NA1, NA2, NB1, NB2, 5b, 9a, and Mart in an ANCA-indirect immunofluorescence (ANCA-IF) assay to determine if these alloantibodies reacted with neutrophil cytoplasmic or granule antigens. Alloantibodies specific for neutrophil antigens NA1, NA2, NB2, 5b, and 9a did not react with neutrophil cytoplasmic components. However, all three NB1 alloantibodies studied demonstrated a cytoplasmic pattern of immunofluorescence (C-ANCA) when NB1-positive neutrophils were tested. While control ANCA resulted in cytoplasmic immunofluorescence of all neutrophils from each donor tested, NB1 antibodies reacted with a subpopulation of neutrophils from some donors. Cytoplasmic immunofluorescence was also observed with an antibody directed against the Mart neutrophil antigen. The Mart antigen is located on integrin CR3 (CD11b/CD18). To confirm that these reactions were due to anti-Mart, monoclonal antibodies to CD11b and CD18 were also tested and found to cause cytoplasmic immunofluorescence. When the ANCA-IF assay was performed using neutrophils that did not express Mart or NB1 antigen, cytoplasmic immunofluorescence was seen with the ANCA control antisera, but not with the NB1 or Mart alloantibodies.(ABSTRACT TRUNCATED AT 250 WORDS)

Antibodies, Antineutrophil Cytoplasmic↗
PubMed1993

Drug-induced immune neutropenia.

Drug-induced immune-mediated neutropenia is a serious complication of therapy with many different drugs. Its clinical presentation and outcome are highly variable. In addition to the drugs listed in this review it is likely that many other drugs also cause immune-mediated neutropenia but drug-dependent neutrophil antibodies were not reported because of the lack of widespread availability of testing. With the exception of quinine-dependent antibodies in three patients, the neutrophil antigens recognized by the drug-dependent antibodies are not known; however, the recent development of MAIGA assays will likely help identify the antigens other drug-dependent neutrophil antibodies recognize.

Autoantigens↗
PubMed1993

Prolonged neutropenia resulting from antibodies to neutrophil-specific antigen NB1 following marrow transplantation.

Marrow graft failure is a significant cause of morbidity following bone marrow transplantation. A case is reported of marrow graft failure due to neutrophil antibodies. A 13-year-old girl with a large granular lymphocytosis and chronic neutropenia was treated with granulocyte transfusions prior to undergoing a transplant with bone marrow from a partially matched, unrelated donor. Following the transplant, a bone marrow biopsy showed engraftment of donor myeloid cells, but the recipient remained neutropenic. Testing of the serum for neutrophil antibodies found that the recipient's serum had a high-titer neutrophil antibody. Immunoprecipitation studies using the marrow recipient's serum and 125I surface-labeled neutrophils showed that the antibody reacted to the neutrophil-specific antigen NB1. Phenotyping of neutrophils from the marrow donor found that they expressed NB1 antigen, and, in a crossmatch assay, the recipient's serum reacted with donor neutrophils. Despite treatment with granulocyte-macrophage--colony-stimulating factor, the marrow transplant recipient remained neutropenic and died of polymicrobial sepsis and aspergillosis 38 days after the transplant. The presence of high-titer antibodies to neutrophil-specific antigen NB1 in this patient following transplant likely prevented the recovery of her peripheral blood neutrophils and contributed to her death.

Adolescent↗
PubMed1993

Polyclonal antibodies against the NB1-bearing 58- to 64-kDa glycoprotein of human neutrophils do not identify an NB2-bearing molecule.

The neutrophil-specific NB antigen system has been serologically characterized with human alloantisera. Two alleles, NB1 and NB2, have been described; however, there may be important quantitative or qualitative variation in the expression of NB1 and NB2. Human alloantibodies have been used to identify the 58- to 64-kDa glycoprotein (GP) on which NB1 antigen is located, but an NB2 antigen-bearing molecule has not yet been identified. To identify the NB2 molecule, human alloantibody to NB1 was used to isolate the 58- to 64-kDa NB1 GP, and rabbits were immunized with this GP. Two rabbit antisera were produced. Both antisera immunoblotted and immunoprecipitated the 58- to 64-kDa GP on which NB1 is located, but neither identified the molecule on which NB2 is located. The inability of two rabbit polyclonal antibodies specific for the NB1 molecule to react with the NB2-bearing molecule suggests that considerable differences may exist between these two molecules or that NB2 as currently defined is not related to NB1.

Animals↗
PubMed1993

Analysis of the expression of neutrophil-specific antigen NB1: characterization of neutrophils that react with but are not agglutinated by anti-NB1.

The neutrophil-specific NB antigen system has been serologically characterized with human alloantisera. Two alleles, NB1 and NB2, have been described. NB1 is expressed on a subpopulation of peripheral blood neutrophils in 97 percent of healthy donors. Human alloantibodies have been used to identify the 58- to 64-kDa glycoprotein (GP) on which NB1 is located. NB1 can usually be detected by both a granulocyte immunofluorescence (GIF) assay and a granulocyte agglutination (GA) assay, but neutrophils from some donors have been found to react with anti-NB1 in GIF but not in GA assays. To determine if the latter neutrophils express NB1 and the corresponding 58- to 64-kDa GP, these neutrophils were probed with rabbit and human sera specific for NB1. First, the proportion of neutrophils that express NB1 was quantitated. Neutrophils from donors that typed as NB1-positive in both GA and GIF assays were analyzed by flow cytometry with antisera to NB1. Human and rabbit anti-NB1 reacted with 71 +/- 17 percent and 70 +/- 17 percent of neutrophils, respectively. There was no difference in the expression of NB1 in NB1-homozygous and NB1-heterozygous individuals. In contrast, significantly fewer neutrophils from four donors that typed as NB1-positive in GIF assay but not GA assay reacted with human (27 +/- 12%; p < 0.001) and rabbit (26 +/- 12%; p < 0.001) anti-NB1. When neutrophils from these same four donors were probed with rabbit and human anti-NB1 by immunoblotting and immunoprecipitation, the 58- to 64-kDa GP was identified.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1993

Neonatal immune neutropenia following the administration of intravenous immune globulin.

BACKGROUND: In adults--but not neonates--neutropenia has been reported to complicate treatment with intravenous immunoglobulin, but the mechanism is unknown. PURPOSE: To describe for the first time the case of a newborn infant who, after intravenous immunoglobulin, demonstrated serum antineutrophil antibodies and neutropenia. PATIENTS AND METHODS: The 1,425-g, 36-week-gestation boy was healthy except for intrauterine growth retardation. Intravenous immunoglobulin (1g/dose x 3) was administered to treat alloimmune thrombocytopenia. Neutrophil-specific antibodies were detected by a granulocyte immunofluorescence assay. RESULTS: After the intravenous immunoglobulin, the platelet count normalized but the neutrophil count declined to 450/mm3. Neutrophil-specific antibodies were detected in the serum of the infant but not in the maternal serum. Furthermore, cross-matching revealed that the maternal serum did not react with the infant's granulocytes. Two of three random lots of intravenous immunoglobulin contained detectible anti-neutrophil antibodies. CONCLUSIONS: After intravenous immunoglobulin, the infant's serum contained one or more anti-neutrophil antibodies that were not maternal in origin. We speculate that the neutropenia resulted from the administration of intravenous immunoglobulin containing antineutrophil antibodies.

Adult↗
PubMed1992

Characterization of multiple quinine-dependent antibodies in a patient with episodic hemolytic uremic syndrome and immune agranulocytosis.

A 23-year-old woman experienced six distinct episodes of severe combined neutropenia and thrombocytopenia. At least one of the episodes was accompanied by hemodialysis-requiring acute renal failure and fragmentation hemolysis (hemolytic uremic syndrome [HUS]). In retrospect, all episodes were probably associated with the ingestion of quinine. Quinine-dependent antibodies to platelets, neutrophils, T lymphocytes, and red blood cells (RBCs) were detected in the patient's serum. By a monoclonal antibody antigen capture assay, the patient's serum contained IgG antibodies, which in the presence, but not absence, of quinine reacted with platelet glycoprotein (GP) complexes Ib/IX and IIb/IIIa, but not Ia/IIa. By immunoprecipitation assay, the serum, after addition of quinine, reacted strongly with an 85-Kd neutrophil membrane protein and weakly with 130- and 60-Kd moieties. Serum adsorbed with RBCs in the presence of quinine continued to react with platelets and neutrophils, and serum that was absorbed with platelets continued to react with neutrophils and RBCs, indicating that the antigenic targets were different on platelets, neutrophils, and RBCs. Since platelets and endothelial cells share some antigens, we tested patient serum for antibodies to human umbilical vein endothelial cells (HUVEC); no quinine-dependent antibodies to HUVEC were detected. However, her quinine-dependent antibodies not only bound to platelets and neutrophils, but also activated neutrophils. Thus, the patient's serum with quinine aggregated neutrophils, but neither agent alone caused activation. Moreover, the patient's serum with quinine (but not without) augmented the adherence of neutrophils to HUVEC. Treatment of the patient's serum with staphylococcal protein A removed the quinine neutrophil aggregation cofactor, suggesting it was due to IgG. In both neutrophil aggregation and adherence assays, decomplementation of the patient's serum markedly blunted its effect. Furthermore, the patient's serum failed to aggregate formalin-inactivated neutrophils, suggesting neutrophil activation, probably by activated complement, was necessary for aggregation and adhesivity to endothelium. We conclude that our patient's neutropenia, thrombocytopenia, lymphopenia, and anemia were due to quinine-dependent antibodies, and that these antibodies recognized epitopes that were different in the three target cell populations. We further suggest that HUS was likely secondary to the activation and adhesion of neutrophils to endothelium.

Adult↗
PubMed1992

Autoimmune neutropenia in Sheboygan County, Wisconsin.

Autoimmune neutropenia is thought to be an uncommon disorder in adults. Over a 2-year period, however, autoimmune neutropenia was diagnosed in seven adults in a county with a population of approximately 105,000 people. The median age of the patients was 52 years old (range of 22 to 81 years), and five of the seven patients were women. All seven patients had at least one other symptom of autoimmune disease. Three patients had splenomegaly, three patients had positive direct antiglobulin tests, and two patients had immune thrombocytopenia. Antibodies reacting to neutrophils were detected by either granulocyte agglutination (GA) or granulocyte immunofluorescence (GIF) testing in five of the seven patients. Antibodies in four patients reacted with an 80 kd neutrophil membrane glycoprotein, and antibodies from two people reacted with a 60 kd membrane glycoprotein. Three patients were given treatment with splenectomy, which resulted in only transient improvement in the neutrophil counts. Serious infections occurred in only three patients over the 2 years of observation. In summary, autoimmune neutropenia in adults may occur more often than appreciated. Most cases of autoimmune neutropenia in adults appear to be associated with other autoimmune phenomena.

Adult↗
PubMed1992

Antibodies to granulocytes in patients infected with human immunodeficiency virus.

Individuals who are infected with human immunodeficiency virus (HIV) are known to have a high incidence of autoantibodies. In this study, serum samples from 100 individuals with HIV infection were tested for granulocyte antibodies (red cell antibodies, lymphocytotoxic antibodies, circulating immune complexes, and serum immunoglobulin G levels) by granulocyte agglutination (GA) and granulocyte immunofluorescence (GIF) assays. Granulocyte antibodies were detected in 66% of serum samples by GIF and in 21% of serum samples by GA. None of the positive sera reacted with granulocyte antigens of known specificity. Antibodies that reacted with red cell antigens other than ABO were detected in only three serum samples, but lymphocytotoxic antibodies were detected in 62% of patients. All serum samples were tested by immunoblotting with granulocyte plasma membranes. Only two samples were found to be positive; one sample reacted with a 58 kd protein and one reacted with a 55 kd protein, but neither serum sample immunoprecipitated any protein from granulocytes that were labeled at the cell surface with iodine 125. Since immune complexes that are bound to granulocyte membranes can be detected by GIF, circulating immune complex levels were measured in all 100 samples. Immune complexes were increased in GIF-reactive serum samples compared with GIF-nonreactive serum samples (23.3 +/- 19.5 micrograms Eq/ml [mean +/- SD] vs 9.6 +/- 8.1 micrograms Eq/ml, p less than 0.001) but not in GA-reactive serum samples compared with GA-nonreactive sera (24.4 +/- 21.3 micrograms Eq/ml versus 16.9 +/- 16.0 micrograms Eq/ml, p = 0.10).(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1991

Alloimmune neonatal neutropenia due to an antibody to the neutrophil Fc-gamma receptor III with maternal deficiency of CD16 antigen.

Antibodies to the neutrophil-specific antigens NA1 and NA2 are associated with alloimmune neonatal neutropenia (ANN), autoimmune neutropenia of childhood, and acute pulmonary transfusion reactions. These antigens have been found to be located on the neutrophil Fc-gamma receptor III (FcRIII). The mother of a child with ANN was found to lack both NA antigens and to produce an antibody that reacted with all normal neutrophils tested. We used maternal antibody and a CD16 monoclonal antibody (MoAb) that has specificity for FcRIII to immunoblot and immunoprecipitate neutrophil membranes of various NA phenotypes. Both antibodies immunoblotted an approximately 40- to 70-Kd glycoprotein (GP) on NA1, NA2-positive membrane, an approximately 40- to 55-Kd GP on NA1-homozygous membranes, and an approximately 55- to 70-Kd GP on NA2-homozygous membranes. Both antibodies also immunoprecipitated a 50- to 80-Kd GP from NA1, NA2-positive cells, a 50- to 60-Kd GP from NA1-homozygous cells, and a 55- to 80-Kd GP from NA2-homozygous cells. To further examine the specificity of the maternal antibody, sequential immunoprecipitation studies were performed using maternal antisera and a CD16 MoAb. After extracts of 125I surface-labeled neutrophils were precleared with maternal serum, CD16 MoAbs no longer immunoprecipitated any GP. Neither the CD16 MoAb nor a rabbit polyclonal antibody specific for FcRIII detected any GP in maternal neutrophil membranes by immunoblotting. Neutrophil FcRIII is a glycosyl-phosphatidylinositol anchored membrane GP as is decay accelerating factor and both are absent from neutrophils of patients with paroxysmal nocturnal hemoglobinuria (PNH). Maternal neutrophil membranes were probed with antibody specific for DAF and an 80-Kd GP was detected. This woman also has had no clinical evidence of PNH. These studies provide further evidence that the NA1 and NA2 antigens are on FcRIII and identify a healthy person whose neutrophils lack not only the neutrophil specific antigens NA1 and NA2 but multiple other epitopes of FcRIII and, therefore, likely lack FcRIII entirely.

Antibodies, Monoclonal↗
PubMed1991

Neutrophil-specific antigen NB1 is anchored via a glycosyl-phosphatidylinositol linkage.

Neutrophil-specific alloantibodies and the antigens they recognize are important in clinical medicine but little is known about the structure of these antigens. Alloimmunization to the antigen NB1 is a clinically important cause of neonatal neutropenia and leukocyte-mediated transfusion reactions. A novel mechanism of protein attachment to cell membranes involving the covalent linkage of the protein through an oligosaccharide to phosphatidylinositol has recently been defined. Many proteins which are anchored to the cell membrane by this mechanism can be released by treatment with phosphatidylinositol-specific phospholipase C (PI-PLC). The 58-64-kDa human neutrophil surface protein which contains the NB1 antigen was labeled with 125I by using lactoperoxidase and examined for PI-PLC sensitivity. The 58-64-kDa protein was specifically released from the cell by treatment with PI-PLC, and the mobility of the protein under non-denaturing conditions using non-ionic detergent was increased by treatment with PI-PLC. Surface expression of the NB1 antigen was slightly up-regulated by treatment with the chemotactic peptide f-met-leu-phe. Removal of N-linked carbohydrates with endoglycosidase-F decreased the apparent molecular weight of the protein to approximately 45-kDa. The data suggest that most of the 58-64-kDa protein bearing the neutrophil-specific antigen NB1 is anchored to the membrane through a glycosyl-phosphatidylinositol linkage.

Antigens, Surface↗
PubMed1991

Comparison of the effectiveness of potential marrow donors recruited from apheresis donors or whole blood donors and through appeals to the general public.

Marrow transplants with phenotypically HLA-matched, unrelated donors have been used effectively to treat a number of diseases. Many blood centers have recruited HLA-typed apheresis blood donors into marrow donor registries. However, to build larger registries so that more patients may be treated with unrelated donor marrow transplants, whole blood donors and people who do not donate blood have been added to the registries. The marrow donor program at our blood center had 2844 potential donors, of whom 1725 were also apheresis donors, 608 were whole blood donors, and 511 were recruited from the general public as a result of community appeals for marrow donors for a specific patient. Over a 9-month period, 297 potential donors were asked to donate blood samples for HLA-DR typing or mixed lymphocyte culture (MLC) testing or to participate in an informational session, undergo a medical evaluation, and sign a statement indicating an intention to donate marrow for a specific patient. Overall, these requests were successfully completed by 75.5 percent of apheresis donors, 87.2 percent of whole blood donors, and 78.1 percent of the potential donors recruited through community appeals. Furthermore, there was no difference among the three groups in the portion of people who donated blood samples for HLA-DR typing or MLC testing. Fifteen of 18 apheresis donors who were found to match a specific donor signed a statement of intent to donate marrow, 2 apheresis donors were deferred for medical reasons, and 1 decided not to donate.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1990

Biochemical characterization of the neutrophil-specific antigen NB1.

Neutrophil-specific alloantibodies and the antigens they recognize are important in clinical medicine, but little is known about the structure of these antigens. Alloimmunization to the antigen NB1 is a clinically important cause of neonatal neutropenia and febrile transfusion reactions. To study the immunochemistry of the NB1 antigen, we prepared neutrophil plasma membranes and granules by nitrogen cavitation and differential centrifugation and then analyzed them by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting with alloantibodies to several neutrophil-specific antigens. Two different antisera to the neutrophil-specific antigen NB1 identified an approximately 55-Kd protein by immunoblotting on neutrophil membranes from four NB1-positive donors but not on neutrophil membranes from five NB1-negative donors. Four anti-NB1 antisera immunoprecipitated a 58- to 64-Kd protein from extracts of NB1-positive neutrophils surface-labeled with 125I using lactoperoxidase, but not from similarly treated NB1-negative neutrophils. Normal human serum did not immunoprecipitate or immunoblot any proteins from these same neutrophil preparations. The NB1 antigen was detected by immunoblotting in secondary granules but was not found in primary granules. The electrophoretic mobility of the antigen was decreased slightly by reduction, suggesting that intrachain disulfide bonds were present. After reduction, the antigen could no longer be recognized by anti-NB1 antisera, but treatment of the antigen with periodate had no effect on the ability of anti-NB1 antisera to recognize the antigen, suggesting that it is not a carbohydrate. The data suggest that the neutrophil-specific antigen NB1 is present on a 58- to 64-Kd surface glycoprotein that is also present in secondary granules, and that the NB1 epitope is not a carbohydrate but probably resides in the tertiary structure of the protein backbone.

Antigens, Surface↗
PubMed1990

Transfusion-related acute lung injury caused by an NB2 granulocyte-specific antibody in a patient with thrombotic thrombocytopenic purpura.

HLA and granulocyte-specific antibodies have been implicated in the production of transfusion-related acute lung injury (TRALI). Reported here is a case that suggests that the patient's preexisting condition may play an important role in determining whether TRALI develops upon transfusion of blood products containing anti-white cell (WBC) antibodies. A 29-year-old woman with thrombotic thrombocytopenic purpura (TTP) underwent an uneventful 1.5-volume plasma exchange, which was followed by the transfusion of 2 red cell (RBC) units. At the end of the second RBC transfusion, the patient developed clinical signs and symptoms of noncardiogenic pulmonary edema. Serologic studies demonstrated that the serum from the second RBC donor had no HLA antibodies but did have a granulocyte-specific antibody (anti-NB2) that caused the agglutination of the recipient's granulocytes, which were NB2 positive. Serum from the donor of the first RBC unit and serum from the donors of units used in the exchange had no HLA or granulocyte-specific antibodies that reacted with the recipient's WBCs. Because the donor implicated in this reaction had a history of 21 blood donations, none of which had been associated with a transfusion reaction, we suggest that the patient's preexisting condition played a significant role in this episode of TRALI, owing to the granulocyte-specific antibody.

Acute Disease↗
PubMed1989

Immunoblotting characterization of neutrophil antigenic targets in autoimmune neutropenia.

We characterized neutrophil autoantigens using an immunoblotting technique with antibodies obtained from patients with autoimmune neutropenia. These results were correlated with serologic characterization of the antibodies, using indirect immunofluorescence and leukoagglutination. Of the 17 sera immunoblotted, 16 showed discrete bands in the molecular weight range of 30 to 112. Three patients with Felty's syndrome reacted with an antigenic target of 80 to 84 Kd molecular mass, a finding not seen in any of the other patients studied. By serologic testing, none of the autoimmune sera showed serologic specificity for any known neutrophil-specific alloantigen. Using an anti-NA-1 serum, we identified antigenic targets at 40, 50, and 101 Kd in both NA-1-positive and NA-1-negative neutrophils. Ten of 17 autoimmune sera showed reactivity in this corresponding range. These studies demonstrate that immunoblotting may be used to identify antigenic targets in autoimmune neutropenia and may suggest a specificity of these antibodies not definable by serologic techniques. Correlation of immunoblot reactivity with disease states associated with immune neutropenia may be useful in the study of the pathogenesis of the different forms of autoimmune neutropenia.

Adolescent↗
PubMed1985

Sodium morrhuate stimulates granulocytes and damages erythrocytes and endothelial cells: probable mechanism of an adverse reaction during sclerotherapy.

Stimulated by a patient with dyspnea, thrombocytopenia, and leukopenia after sodium morrhuate sclerotherapy, we studied the effect of this agent on the plasma coagulation and complement systems, the formed elements of the blood, and cultured human endothelial cells. The addition of sodium morrhuate to citrated plasma did not cause clotting or shorten the prothrombin time or partial thromboplastin time. Incubation of a 1:100 dilution of the clinical sodium morrhuate preparation in heparinized plasma led to a modest rise in [C3a]. The addition of the drug (dilutions 1:50 to 1:300) to granulocytes caused prompt aggregation (and, at the higher concentrations, granulocyte cytotoxicity [trypan blue exclusion; lactate dehydrogenase release]), but the same dilutions failed to aggregate platelets. However, 0.05% morrhuate added to washed red blood cells caused a prompt 84.0% (+/- 0.8% SEM) hemolysis, rendering the supernatant buffer a potent platelet aggregant. Not only was this sclerosing agent toxic to granulocytes and red cells, but a 1:1000 dilution of the drug also caused the destruction of 35.5% (+/- 6.6%) of cultured endothelial cells as measured by chromium 51 release. Three other agents in current use (ethanolamine oleate, sodium tetradecyl sulfate, and polidocanol) were studied and found to cause effects qualitatively similar to those of sodium morrhuate. We conclude that these drugs cause phlebosclerosis not primarily through induction of plasma coagulation, but by directly damaging endothelium and red cells, triggering platelets, and aggregating granulocytes at the venous wall endothelium. These effects likely derive from the surfactant properties of sodium morrhuate as well as its high arachidonate content.(ABSTRACT TRUNCATED AT 250 WORDS)

Blood Coagulation↗