lewis-x-antigen and Plasmacytoma

lewis-x-antigen has been researched along with Plasmacytoma* in 2 studies

Other Studies

2 other study(ies) available for lewis-x-antigen and Plasmacytoma

ArticleYear
Tumor location using F(ab')2 mu from a monoclonal IgM antibody: pharmacokinetics.
    Journal of nuclear medicine : official publication, Society of Nuclear Medicine, 1985, Volume: 26, Issue:3

    A monoclonal IgM antibody (anti-SSEA-1) and its divalent antigen-binding peptic fragment [F(ab')2 mu] were compared as in vivo tumor localization reagents in mouse teratocarcinomas. F(ab')2 mu is cleared more rapidly than whole antibody from the whole body, blood, and all tested organs (t1/2 for whole antibody approximately 18 hr; t1/2 for F(ab')2 mu, 12 hr). A corresponding average improvement in tumor-to-tissue ratio is observed 48 hr after injection and earlier. However, the affinity of the F(ab')2 mu for antigen is much lower, and a smaller fraction of the antibody fragment is retained in the tumor than with whole antibody. The fragment was not retained by animals bearing nonantigenic tumors.

    Topics: Animals; Antibodies, Monoclonal; Antigens, Neoplasm; Glycolipids; Immunoglobulin Fab Fragments; Immunoglobulin M; Iodine Radioisotopes; Kinetics; Lewis X Antigen; Mice; Mice, Inbred BALB C; Neoplasms, Experimental; Plasmacytoma; Radionuclide Imaging; Teratoma; Time Factors

1985
Exposure by desialylation of myeloid antigens on acute lymphoblastic leukemia cells.
    Journal of the National Cancer Institute, 1984, Volume: 73, Issue:1

    The 3-fucosyl-N-acetyllactosamine structure, a sugar sequence contained in the human milk oligosaccharide lacto-N-fucopentaose III, is recognized by most of the granulocyte-specific monoclonal antibodies (MoAb) reported in the literature, including the six MoAb from our laboratory. Blast cells from patients with acute myeloblastic leukemia (AML) displayed a heterogeneous reaction pattern when they were exposed to MoAb against this moiety, and the proportion of reactive cells in individual cell samples was highly variable. The intensity of the reaction was strongly enhanced by neuraminidase treatment of AML blasts, and reactive structures were exposed on previously negative AML blast cells. Surprisingly, this granulocyte-associated antigen was exposed by desialylation not only on malignant myeloid precursor cells but also on common acute lymphoblastic leukemia cells. No such effect was seen when normal peripheral blood lymphocytes, lymphocytes from patients with chronic lymphatic leukemia, or blast cells from patients with B-cell acute lymphoblastic leukemia, acute erythroid leukemia, and acute megakaryoblastic leukemia were treated with neuraminidase.

    Topics: Animals; Antibodies, Monoclonal; Antigens, Neoplasm; Blood Platelets; Cell Line; Epitopes; Humans; Hybridomas; Immunoglobulin M; Leukemia, Lymphoid; Leukocytes; Lewis X Antigen; Mice; Mice, Inbred BALB C; Neuraminidase; Oligosaccharides; Plasmacytoma; Reference Values; Sialic Acids

1984