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K E Edelberg

Publications and source records attributed to K E Edelberg.

3 recordsLinked to original sources

S-antigen in the developing retina and pineal gland: a monoclonal antibody study.

Spleen cells of BALB/c mice, previously immunized with bovine retinal S-antigen, were fused with Sp2/0-Ag14 mouse myeloma cells. Two monoclonal antibodies (MAbs) MAbA9-C6 (IgG2a isotype) and MAbA1-G5 (IgG1 isotype) were selected on the basis of reactivity in an ELISA and immunofluorescent assay. In radioimmunoassay MAbA9-C6 and MAbA1-G5 do not compete and appear to define unrelated epitopes of S-antigen. Both MAbs reacted in the ELISA assay, whereas only MAbA9-C6 bound to S-antigen in fixed tissue sections. Because MAbA9-C6 was useful for immunocytochemistry, it was studied in more detail. MAbA9-C6 bound to all vertebrate retinas tested including human, bovine, guinea pig, and mice. The immunoreactivity of MAbA9-C6 also was studied in the developing rat retina and pineal gland. In the morphologically undifferentiated retina, assessed by conventional light microscopy, there was an incomplete separation of the outer neuroblastic cells. However, in the same retina a distinct zone, corresponding to S-antigen immunoreactivity, was present indicating antigenic differentiation with regard to S-antigen at this stage of retinal development. In the pineal gland, S-antigen immunoreactivity was first observed in the three day old rat and at all stages examined thereafter. The usefulness of these two MAbs in the study of the embryologic development of the retina and of the antigenic epitopes of S-antigen is discussed.

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Human retinal S-antigen. Isolation, purification, and characterization.

S-antigen, a highly pathogenic agent for the inducation of experimental autoimmune uveitis ( EAU ), was obtained in a pure state from human retina by conventional salt fractionation, molecular sieve and ion exchange chromatography. The physical and chemical properties of the purified protein including the molecular weight, isoelectric point and amino acid composition were determined. The physical properties of the purified human retinal S-antigen were similar, but not identical, to those previously reported for bovine retinal S-antigen (J Immunol 119:1949, 1977). Following the injection of 50 micrograms of human retinal S-antigen into the footpads of guinea pigs, EAU was documented both clinically and histopathologically. The relationship between S-antigen, uveitis, and the pineal gland is discussed.

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Metastatic choroidal melanoma. Hepatic binding protein reactivity toward a liver-metastasizing clone.

A clone of B16 malignant melanoma cells with a preference for metastasis to the liver was isolated and characterized. The parent tumor cells (F1) were injected in the tail vein of C57BL/6 mice, and the resultant liver colonizing cells were isolated and then subcultured for two to three weeks. The cells were then reinjected into the next series of mice. After five such passages, a clone (L4) of melanoma cells was obtained that metastasized almost exclusively to the liver. A hepatic binding protein (HBP) was isolated from rabbit liver that agglutinated neuraminidase-treated F1 and L4 malignant melanoma cells. Different agglutination titers found between the parent and liver-metastasizing clone demonstrated differences in cell-surface properties between the parent tumor and the liver-metastasizing clone. These results demonstrate that malignant melanoma cells can be selected for preferential liver metastasis and can be recognized and agglutinated by specific HBPs. Metastasis from human uveal malignant melanoma may occur by similar mechanisms.

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