Abstract: Modified macrophage immune cells are provided for treatment of cancer and other diseases. In particular said macrophages express chimeric antigen receptors (CAR). The single chain variable fragment (scFv) may be directed against thymidine kinase 1 (TK1) or hypoxanthine guanine phosphoribosyltransferase (HPRT). The signaling domain may be derived from a Toll-like receptor (TLR).

Abstract: Modified macrophage immune cells are provided for treatment of cancer and other diseases.

Abstract: Modified T-cells have paratopes against human TK1 epitopes, are made by producing monoclonal antibodies that are specific to TK1, creating chimeric antigen receptors (CARs) by fusion of the single-chain variable fragments (scFv) of the monoclonal antibodies to T-cell signalling domains, and transducing the CARs to the T-cells.

Abstract: Described herein are chimeric receptors. Chimeric receptors comprise a cytoplasmic domain; a transmembrane domain; and an extracellular domain. In embodiments, the cytoplasmic domain comprises a cytoplasmic portion of a receptor that when activated polarizes a macrophage. In further embodiments, a wild-type protein comprising the cytoplasmic portion does not comprise the extracellular domain of the chimeric receptor. In embodiments, the binding of a ligand to the extracellular domain of the chimeric receptor activates the intracellular portion of the chimeric receptor. Activation of the intracellular portion of the chimeric receptor may polarize the macrophage into an M1 or M2 macrophage.

Abstract: A nucleic acid encoding a chimeric antigen receptor (CAR) comprising a single-chain variable fragment (scFv) operatively linked to a signaling domain that polarizes a macrophage to an M1 macrophage; wherein the nucleic acid is operatively linked to a macrophage specific promoter; and wherein the scFv is specific for a human antigen. Monocytes or macrophages comprising such a nucleic acid.

Abstract: Described herein are macrophages or macrophage precursor cells lacking functional expression of MHC genes. The macrophages may express HLA-G or a modified MHC gene that does not elicit an immune response in an allogeneic subject but remains recognized by NK cells. The cells may further comprise a chimeric antigen receptor.

Abstract: Described herein are chimeric receptors. Chimeric receptors comprise a cytoplasmic domain; a transmembrane domain; and an extracellular domain. In embodiments, the cytoplasmic domain comprises a cytoplasmic portion of a receptor that when activated polarizes a macrophage. In further embodiments, a wild-type protein comprising the cytoplasmic portion does not comprise the extracellular domain of the chimeric receptor. In embodiments, the binding of a ligand to the extracellular domain of the chimeric receptor activates the intracellular portion of the chimeric receptor. Activation of the intracellular portion of the chimeric receptor may polarize the macrophage into an M1 or M2 macrophage.

Abstract: Modified T-cells have paratopes against human TK1 epitopes, are made by producing monoclonal antibodies that are specific to TK1, creating chimeric antigen receptors (CARs) by fusion of the single-chain variable fragments (scFv) of the monoclonal antibodies to T-cell signalling domains, and transducing the CARs to the T-cells.

Abstract: Modified T-cells have paratopes against human TK1 epitopes, are made by producing monoclonal antibodies that are specific to TK1, creating chimeric antigen receptors (CARs) by fusion of the single-chain variable fragments (scFv) of the monoclonal antibodies to T-cell signalling domains, and transducing the CARs to the T-cells.

Abstract: Described herein are chimeric receptors. Chimeric receptors comprise a cytoplasmic domain; a transmembrane domain; and an extracellular domain. In embodiments, the cytoplasmic domain comprises a cytoplasmic portion of a receptor that when activated polarizes a macrophage. In further embodiments, a wild-type protein comprising the cytoplasmic portion does not comprise the extracellular domain of the chimeric receptor. In embodiments, the binding of a ligand to the extracellular domain of the chimeric receptor activates the intracellular portion of the chimeric receptor. Activation of the intracellular portion of the chimeric receptor may polarize the macrophage into an M1 or M2 macrophage.

Abstract: Modified T-cells have paratopes against human TK1 epitopes, are made by producing monoclonal antibodies that are specific to TK1, creating chimeric antigen receptors (CARs) by fusion of the single-chain variable fragments (scFv) of the monoclonal antibodies to T-cell signalling domains, and transducing the CARs to the T-cells.

Abstract: Modified T-cells have paratopes against human TK1 epitopes, are made by producing monoclonal antibodies that are specific to TK1, creating chimeric antigen receptors (CARs) by fusion of the single-chain variable fragments (scFv) of the monoclonal antibodies to T-cell signalling domains, and transducing the CARs to the T-cells.

Abstract: Modified T-cells have paratopes against human TK1 epitopes, are made by producing monoclonal antibodies that are specific to TK1, creating chimeric antigen receptors (CARs) by fusion of the single-chain variable fragments (scFv) of the monoclonal antibodies to T-cell signalling domains, and transducing the CARs to the T-cells.

Abstract: Modified T-cells have paratopes against human TK1 epitopes, are made by producing monoclonal antibodies that are specific to TK1, creating chimeric antigen receptors (CARs) by fusion of the single-chain variable fragments (scFv) of the monoclonal antibodies to T-cell signalling domains, and transducing the CARs to the T-cells.

Abstract: Modified macrophage immune cells are provided for treatment of cancer and other diseases.

Abstract: Compositions and methods are provided for the diagnosis, treatment, and medical management of cancers. The methods include the use of antibodies and other binding molecules that specifically bind to one or more nucleotide salvage pathway enzymes (SPEs) selected from the group consisting of adenine phosphoribosyltransferase (APRT), hypoxanthine-guanine phosphoribosyltransferase (HGPRT), deoxycytidine kinase (dCK); and thymidine kinase 1 (TK1) and complexes comprising SPEs, for detection of the SPE(s) on or in cancer cells and/or on or in body fluids and tissues of cancer patients. Binding of SPEs is useful in the methods provided herein for diagnosing cancer, determining prognosis of cancer and assessing the effectiveness of cancer treatments. Immunoassay systems for use in the methods are also provided, including sandwich immunoassays. In addition, an amino acid sequence comprising a novel TK1 binding site is provided, as well as nucleotide sequences encoding it.

Abstract: Compositions and methods are provided for the diagnosis, treatment, and medical management of cancers. The methods include the use of antibodies and other binding molecules that specifically bind to one or more nucleotide salvage pathway enzymes (SPEs) selected from the group consisting of adenine phosphoribosyltransferase (APRT), hypoxanthine-guanine phosphoribosyltransferase (HGPRT), deoxycytidine kinase (dCK); and thymidine kinase 1 (TK1) and complexes comprising SPEs, for detection of the SPE(s) on or in cancer cells and/or on or in body fluids and tissues of cancer patients. Binding of SPEs is useful in the methods provided herein for diagnosing cancer, determining prognosis of cancer and assessing the effectiveness of cancer treatments. Immunoassay systems for use in the methods are also provided, including sandwich immunoassays. In addition, an amino acid sequence comprising a novel TK1 binding site is provided, as well as nucleotide sequences encoding it.