Sloan-kettering Institute for Cancer Research

Sloan-kettering Institute

Other

Karl Welte

Roland Mertelsmann

Janice L Gabrilove

Erich Platzer

Malcolm A Moore

Salvatore Venuta

Malcolm A S Moore

Lloyd J Old

Alan N Houghton

Paul B Chapman

Peter Ralph

Glenn Miller

Roland Mertelsm

Roland Mertelsman

Highly purified Pluripotent hematopoietic colony-stimulating factor (pluripotent CSF), a glycoprotein (MW 19,600) constitutively produced by human tumor cells has been highly purified from low serum-containing conditioned medium to apparant homogeneity. Pluripotent CSF supports the growth of human mixed colonies (CFU-GEMM), granulocyte-macrophage colonies (CFU-GM), early erythroid colonies (BFU-E) and induces differentiation of human leukemic cells. The specific activity of the purified pluripotent CSF in the CFU-GM assay is 1.5&#xd7;10U/mg protein.

Human pluripotent hematopoietic colony stimulating factor, method of production and use

Highly purified Pluripotent hematopoietic colon-stimulating factor (pluripotent CSF), a glycoprotein (MW ) constitutively produced by human tumor cells has been highly purified from low serum-containing conditioned medium to apparent homogeneity. Pluripotent CSF supports the growth of human mixed colonies (CFU-GEMM), granulocyte-macrophage colonies (CFU-GM) early erythroid colonies (BFU-E) and induces differentiation of human leukemic cells. The specific activity of the purified pluripotent CSF in the CFU-GM assay is U/mg protein.

Human pluripotent hematopoietic colony stimulating factor, method of use

Highly purified Pluripotent hematopoietic colony-stimulating factor (pluripotent CSF), a glycoprotein (MW 19,600) constitutively produced by human tumor cells has been highly purified from low serum-containing conditioned medium to apparant homogeneity. Pluripotent CSF supports the growth of human mixed colonies (CFU-GEMM), granulocyte-macrophage colonies (CFU-GM), early erythroid colonies (BFU-E) and induces differentiation of human leukemic cells. The specific activity of the purified pluripotent CSF in the CFU-GM assay is 1.5.times.10.sup.8 U/mg protein.

Human pluripotent hematopoietic colony stimulating factor and cell line

This invention provides a composition comprising a therapeutically effective amount of purified human interleukin-2 and a pharmaceutically acceptable carrier.

Highly purified interleukin-2 and method

Method of producing human pluripotent hematopoietic colony stimulating

Pharmacological preparations comprising human pluripotent hematopoietic

Method of administering human pluripotent hematopoietic colony

Human pluripotent hematopoietic colony stimulating factor

Cell surface gangliosides are presumed to play a role in cell growth and differentiation. Using monoclonal antibodies directed against G.sub.D3, a disialoganglioside expressed predominantly by cells of neuroectodermal origin, we have found that G.sub.D3 is expressed by a subpopulation of cells of the immune system including: a) fetal thymocytes in subcortical regions and near vessels, 2) lymph node lymphocytes in interfollicular areas and near vessels, and 3) a small subset of T cells in the peripheral blood. Mouse monoclonal antibodies (two IgGs, one IgM and F(ab').sub.2 fragments) reacting with G.sub.D3 were found to stimulate proliferation of T cells derived from peripheral blood. Proliferation induced by binding to G.sub.D3 could be augmented by exogenous IL-2, PMA, PHA or Protein A.

Compositions and method for treatment of cancer using monoclonal

Interleukin 2 (IL 2; T-cell growth factor), produced with and without costimulation by Burkitt's lymphoma line Daudi, is highly purified approximately over 37,000-fold to apparent homogeneity from lymphocyte-conditioned medium derived from normal human blood cells by (NH.sub.4).sub.2 SO.sub.4 -precipitation, ion-exchange chromatogr

Purified interleukin 2

Interleukin 2 (IL 2; T-cell growth factor), produced with and without costimulation by Burkitt's lymphoma line Daudi, is highly purified approximately over 37,000-fold to apparent homogeneity from lymphocyte-conditioned medium derived from normal huma

Process for preparing purified interleukin-2

Interleukin 2 (IL 2; T-cell growth factor), produced with and without costimulation by Burkitt's lympho

Uses of interleukin-2

Interleukin 2 (IL 2; T-cell growth factor), produced with and without costimulation by Burkitt's lymphoma line Daudi, is highly purified approximately over 37,000-fold to apparent homogeneity from lymphocyte-conditioned medium derived from normal human blood cells by (NH.sub.4).sub.2 SO.sub.4 -precipitation, ion-exchange chromatography, gel filtration and hydrophobic chromatography. hp IL-2 is free of pyrogens, B cell inducing factor, B cell growth factor, interferon, CSF, and thymocyte differentiating factor. Nature IL 2 produced in the absence of Daudi cells has a molecular weight of about 26,000 daltons as measured by gel filtration and yields IL 2 having two molecular weights of about 16,000 and 17,000 daltons after denaturation as measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. IL 2 produced in the presence of Daudi cells shows a molecular weight of approximately 14,500 daltons as measured by both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This highly purified IL 2 is shown to correct immunodeficiency states in vitro and in vivo, especially in human patients. It shows value in the treatment of AIDS and immunodeficiency resulting from chemotherpy of cancer, as well as transplantation disorders such as graft versus host disease.

Highly purified human interleukin 2 and method

Highly purified T cell replacing factor (TRF or BIF) essentially free of IL-2 and Interferon activities is obtained in the invention. BIF is useful for treatment of immunoregulatory disorders and/or stimulation of production of immunoglobulins. A method for production of BIF and BGF is described. B cell lines for BIF assays are described as well as an assay for B cell receptor variants and a method for obtaining B cell variants from a variety of source materials.

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New York, NY, United States of America

Karl Welte