Search PubMed⌕ Search

Biomedical subjects

L Schrieber

Publications and source records attributed to L Schrieber.

61 records · Page 4Linked to original sources
PubMed1983

Quantitation and detection of isotypes of anti-SS-B antibodies by ELISA and Farr assays using affinity purified antigens. An approach to the investigation of Sjögren's syndrome and systemic lupus erythematosus.

Affinity purified SS-B was characterized as a protein with immunoreactive polypeptides of 40K and 29K. A modified Farr assay and an enzyme linked immunosorbent assay (ELISA) were 100- to 1,000-fold more sensitive than immunodiffusion and showed an association with the systemic manifestations of primary sicca syndrome and Sjögren's syndrome with systemic lupus erythematosus. The ELISA was sufficiently sensitive to detect class specific antibodies in saliva and lymphocyte culture supernatants.

Adult↗
PubMed1983

In vivo fate of 125I SS-B (La) injected into mice.

The fate of the radiolabelled soluble cellular antigen SS-B (La) was compared with that of other 125I-labelled proteins of known molecular weight (MW) and electrostatic charge, following i.v. injection into BALB/c mice. The plasma half-life of 125I-SS-B was 3 min, while that of 125I-bovine serum albumin (similar MW and electrostatic charge) was 270 min. 125I-heat-aggregated IgG (MW greater than 1 x 10(6)) and 125I-7S human IgG (MW 168,000) had plasma half-lives of 40 min and greater than 300 min, respectively. Liver and kidney showed preferential uptake of 125I-SS-B, followed by a rapid decrease in radioactivity. During this time low MW, trichloroacetic acid (TCA) soluble, material appeared in urine. This suggests a specific uptake mechanism followed by a catabolic phase. These studies demonstrate that normal mice remove 125I-SS-B rapidly from the circulation and then degrade it. This rapid antigen elimination may protect against the induction of potentially harmful autoantibody responses.

Animals↗
PubMed1982

Tissue distribution of IgG Fc receptors.

The mechanism causing deposition of circulating immune complexes is largely unknown. The possible role of tissue IgG Fc receptors in immune complex localization has been evaluated using IgG coated ox RBC (ox erythrocyte antisera [EA]) as indicator particles. Cryostat tissue sections of normal human synovium, skin, kidney, choroid plexus, lung and uveal tract were examined for the presence of IgG Fc receptors, with human spleen used as a positive control. Ox EA were shown to bind to splenic red pulp. This binding could be almost completely blocked by heat aggregated human IgG. In none of the other normal tissues examined were IgG Fc receptors demonstrated. To investigate the possibility that inflamed tissues express Fc receptors, biopsy specimens of rheumatoid synovium and skin demonstrating vasculitis were studied. No ox EA binding to these tissues was noted. We concluded that IgG Fc receptors are probably not present in tissues that are targets for immune complex deposition and are therefore unlikely to play a role in this process.

Animals↗
PubMed1979

Tissue C3b receptors.

Using fluorescein-labelled S. typhi coated with C3b (FBC) the presence of a receptor for C3b in normal human glomeruli has been confirmed. A quantitative system, counting the number of FBC bound per unit area of glomerulus, has been developed. Experimental variables have been studied to determine optimal conditions for FBC binding. Glomerular FBC binding has been shown to be dependent on FBC concentration, temperature and time of tissue incubation. A standardized procedure has been adopted. Using this technique we have examined a number of target tissues, including synovium, skin, lung, choroid plexus and uveal tract, which are frequently affected in systemic immune complex diseases. No evidence of this receptor has been found in these tissues. These results suggest a mechanism different from the C3b receptor operating to localise immune complexes in these non-renal sites.

Choroid Plexus↗