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Biomedical subjects

W Riesen

Publications and source records attributed to W Riesen.

At least 109 records · Page 6Linked to original sources

Restriction of immunoglobulin heterogeneity, autoimmunity and serum protein levels in aged people.

Ninety-one sera of persons above 80 years of age were screened for autoantibody activity against lipoproteins (anti-LDL 7, anti-HDL 6 positive), for rheumatoid factor activity (Latex 14, Waaler-Rose 7 positive) and for antinuclear factors (11 positive). Among the sera with autoantibody activity 29 percent showed deviations of the normal kappa/lambda ratio of immunoglobulins, as opposed to 22 percent of the sera without detected autoantibody activity. In 3 percent of the sera an M component was detected. Determination of the alpha1-acid glycoprotein, alpha1-antitrypsin, haptoglobin, haemopexin, complement component C3c and C4, IgG, IgA and IgM levels showed significant increases in alpha-, and beta-globulins as well as in IgG and IgA in sera of the aged persons as compared to a normal population between 20 and 60 years old. No significant difference was noted between the gamma-globulin concentration in sera of aged persons with or without autoantibody activity. The evaluation of the relationship between serum protein levels and alterations of the kappa/lambda ratio indicated that the alpha- and the beta-globulins were significantly raised in sera with altered kappa/lambda ratios, whereas, with the exception of M component containing sera the gamma-globulin levels seemed not significantly affected by changes in this ratio.

Aged↗

[Thrombocytopenia in Waldenstrom's disease with specific antithrombocytic properties of the IgM paraprotein].

The serum of a patient suffering from thrombocytopenia associated with Waldenström's macroglobulinemia was found to contain an IgM paraprotein with unusual characteristics. Following isolation of this IgM paraprotein, dilutions up to 0.01 mg/ml caused immunofluorescence of thrombocytes from man, sheep, rabbit, and horse. In control studies with isolated IgM paraprotein from another non-thrombocytopenic patient with Waldenström's disease, positive immunofluorescence could be elicited only when a 1000-fold greater concentration of the paraprotein was used. The IgM paraprotein from our thrombocytopenic patient and that from the control patient showed comparable differences in immunofluorescence of thrombocytes and megacaryocytes when bone marrow smears were used for incubation. Further studies following papain cleavage of the IgM paraprotein with antithrombocytic activity showed that the combining activity was located in the Fab fragment. This observation characterizes the IgM paraprotein from our patient as an antibody directed to a substance in human and animal thrombocytes. Paraproteins with antibody-like activity for thrombocytes have not been identified previously; the present observation suggests that this mechanism should be considered a possible cause of thrombocytopenia associated with macroglobulinemia.

Blood Platelets↗

An IgM Waldenström with specificity against phosphorylcholine.

Anti-phosphorylcholine specificity has recently been shown to occur with relatively high incidence among IgA myeloma proteins secreted by oil-induced plasma cell tumors in the BALB/c strain of mice. A similar screening of human myeloma sera indicates that in man activity for phosphorylcholine is very rare. Among 904 human sera containing IgG, IgA, and IgM M-components only one reacted with phosphorylcholine-containing antigens. This serum was obtained from a patient with macroglobulinemia Waldenström. The active homogeneous protein could be isolated by affinity chromatography using a Sepharose-phosphorylcholine immunoadsorbent. It was an IgM immunoglobulin; the light chains were of the kappa type. The association constant for the reaction with phosphorylcholine was homogeneous and equalled 6.4 times 10-4 l. mol-1 at 25 degrees and 8.1 times 10-4 l. mol-1 at 2 degrees, indicating that the binding reaction is exothermic. The valences of the pentamer IgM, the 7S IgM subunit produced by reduction with cysteine, and the Fab fragment obtained by cleavage with papain were 10, 2, and 1, respectively. By all criteria available for antibody-like binding such as high specificity, restriction of the binding sites to the Fab part of the molecule and correct stoichiometry this IgM exhibits the fundamental characteristics associated with conventionally induced antibodies.

Aged↗

Autoantibodies with antilipoprotein specificity and hypolipoproteinemia in patients with cancer.

Sera from 151 patients with a variety of cancers were screened for antibody-like activity against lipoproteins. Eighteen % of the sera exhibited activity against autologous and homologous high-density lipoproteins and 3% exhibited activity autologous and homologous low-density lipoprotiens. Antibody-like binding was proven by its restriction to the Fab fragment of IgG. The reactive part of the lipoprotein molecule was shown to be the appoprotein. Quantiation of the serum lipoproteins indicated that thehigh-density lipoprotien concentration in the sera of cancer patients was significantly lower (psmaller than 0.01) when antibody was present. These observation suggest that autoimmune mechanisms may be responsible for the decreased high-density lipoprotein serum levels in some patients with cancer.

Antigen-Antibody Reactions↗