Abstract: A method is disclosed for altering the redox equilibrium of a transmembrane receptor-like protein tyrosine phosphatase (RPTP), particularly a type IIa RPTP, by chemically modulating the activity through contact of such an enzyme with a diaryl boron compound that preferentially reacts with an RPTP in an oxidized state (CyS-OH). This redox modulation is most readily observed and put to use by assaying the inhibition of the phosphatase activity of the RPTP. Such an assay can be carried out on an enzyme in vitro or by contacting the enzyme in a living organism (in vivo). A useful diaryl boron compound corresponds in structure to Formula I in which Ar-1, Ar-2, R1, R2, R3 and R4 are defined within. A pharmaceutical composition containing a useful diaryl boron compound is also disclosed, as are particularly preferred diaryl boron compounds.

Abstract: A method is disclosed for altering the redox equilibrium of a transmembrane receptor-like protein tyrosine phosphatase (RPTP), particularly a type IIa RPTP, by chemically modulating the activity through contact of such an enzyme with a diaryl boron compound that preferentially reacts with an RPTP in an oxidized state (CyS-OH). This redox modulation is most readily observed and put to use by assaying the inhibition of the phosphatase activity of the RPTP. Such an assay can be carried out on an enzyme in vitro or by contacting the enzyme in a living organism (in vivo). A useful diaryl boron compound corresponds in structure to Formula I in which Ar-1, Ar-2, R1, R2, R3 and R4 are defined within. A pharmaceutical composition containing a useful diaryl boron compound is also disclosed, as are particularly preferred diaryl boron compounds.

Abstract: A method is disclosed for altering the redox equilibrium of a transmembrane receptor-like protein tyrosine phosphatase (RPTP), particularly a type IIa RPTP, by chemically modulating the activity through contact of such an enzyme with a diaryl boron compound that preferentially reacts with an RPTP in an oxidized state (CyS-OH). This redox modulation is most readily observed and put to use by assaying the inhibition of the phosphatase activity of the RPTP. Such an assay can be carried out on an enzyme in vitro or by contacting the enzyme in a living organism (in vivo). A useful diaryl boron compound corresponds in structure to Formula I in which Ar-1, Ar-2, R1, R2, R3 and R4 are defined within. A pharmaceutical composition containing a useful diaryl boron compound is also disclosed, as are particularly preferred diaryl boron compounds.

Abstract: A method for formulating A250, a biologically active substance and fraction of wheat germ ferment/fermented wheat germ extract (FWGE), including formulation A250, the processes for their production, the pharmaceutical preparations containing them, and their uses.

Abstract: Biologically active substances and fractions of wheat germ ferment/fermented wheat germ extract (FWGE), including formulation A250, the processes for their production, the pharmaceutical preparations containing them, and their uses.

Abstract: Proteins are identified from human breast tumor cell lines (MDA-MB-231, T-47D and T-47D/Met) that interact specifically with the substrate-trapping mutant form of Density Enhanced Phosphatase-1 (DEP-1). These proteins include the functional component p120 catenin (p120ctn), the adaptor protein Gab 1, and the HGF/SF receptor Met. The invention relates to isolated complexes comprising DEP-1 polypeptides in specific association with Met, Gab 1, or p120ctn, identified herein as DEP-1 substrate polypeptides. Screening assays for agents that alter DEP-1 interaction with DEP-1 substrate polypeptides are also disclosed, as are methods for altering biological signals in cells that are transduced via DEP-1 pathways.

Abstract: Novel Type III density enhanced protein tyrosine phosphatases are disclosed and exemplified by human DEP-1 enzyme. Polynucleotides encoding huDEP-1 are disclosed, along with methods and materials for production of the same by recombinant procedures. Binding molecules specific for DEP-1 are also disclosed as useful for modulating the biological activities of DEP-1.

Abstract: Proteins are identified from human breast tumor cell lines (MDA-MB-231, T-47D and T-47D/Met) that interact specifically with the substrate-trapping mutant form of Density Enhanced Phosphatase-1 (DEP-1). These proteins include the functional component p120 catenin (p120ctn), the adaptor protein Gab 1, and the HGF/SF receptor Met. The invention relates to isolated complexes comprising DEP-1 polypeptides in specific association with Met, Gab 1, or p120ctn, identified herein as DEP-1 substrate polypeptides. Screening assays for agents that alter DEP-1 interaction with DEP-1 substrate polypeptides are also disclosed, as are methods for altering biological signals in cells that are transduced via DEP-1 pathways.

Abstract: Compositions and methods relating to small interfering RNA (siRNA) polynucleotides are provided as pertains to modulation of biological signal transduction. Shown are siRNA polynucleotides that interfere with expression of TCPTP, a member of the protein tyrosine phosphatase (PTP) class of enzymes that mediate signal transduction. In certain preferred embodiments siRNA modulate signal transduction pathways comprising human or murine TCPTP and, in certain further embodiments, insulin receptor, c-jun kinase (JNK) and/or Jak2. Modulation of TCPTP-mediated biological signal transduction has uses in diseases associated with defects in cell proliferation, cell differentiation and/or cell survival, such as metabolic disorders (including diabetes and obesity), cancer, autoimmune disease, infectious and inflammatory disorders and other conditions.

Abstract: Compositions and methods relating to PTP1B associated disorders are provided, based on the discovery that a Y-box protein binding site is present as a transcription enhancer sequence in the promoter region situated upstream (i.e., 5′ to) of the human PTP1B gene. This site, situated at nucleotides −155 through −132 of the human PTP1B gene, mediates specific binding interactions with the YB-1 transcription regulatory factor, a member of the Y-box family of proteins. YB-1-targeted antisense constructs reduced PTP1B expression levels, providing an alternative to PTP1B active-site directed regulation of PTP1B activity.

Abstract: The invention relates to a method of identifying any protein tyrosine phosphatase (PTP) that undergoes reversible modification of PTP active site invariant cysteine within a cell, such that the phosphatase is transiently protected from irreversible active site invariant cysteine-directed PTP inactivating agents. Methods related to regulation of PTPs by reactive oxygen species (ROS) in a cellular environment are provided. Multiple PTPs are shown to be reversibly oxidized and inactivated following treatment of cells with H2O2 or with physiological stimuli that promote ROS formation, and inhibition of PTP function is shown to contribute to ROS-induced mitogenesis. Transient oxidation of the PTP catalytic site invariant cysteine is exploited in methods to identify which of multiple candidate PTPs are components of a given biological signal transduction pathway, without a requirement for first specifically purifying any particular candidate PTP.

Abstract: Novel Type III density enhanced protein tyrosine phosphatases are disclosed and exemplified by human DEP-1 enzyme. Polynucleotides encoding huDEP-1 are disclosed, along with methods and materials for production of the same by recombinant procedures. Binding molecules specific for DEP-1 are also disclosed as useful for modulating the biological activities of DEP-1.

Abstract: DNA which encodes a protein homologous to the protein tyrosine phosphatases (PTPases) which catalyze the dephosphorylation of proteins in which tyrosyl residues have been phosphorylated through the action of a protein kinase. The protein, which appears as if it will localize to focal adhesions, is also the subject of the present invention. In particular, it relates to CDNA encoding a protein, referred to as PTPH1.

Abstract: Novel Type III density enhanced protein tyrosine phosphatases are disclosed and exemplified by human DEP-1 enzyme. Polynucleotides encoding huDEP-1 are disclosed, along with methods and materials for production of the same by recombinant procedures. Binding molecules specific for DEP-1 are also disclosed as useful for modulating the biological activities of DEP-1.

Abstract: An antibody is provided that is specific for a PTPH1 protein, a phosphatase that dephosphorylates phosphotyrosine residues in phosphoproteins having tyrosyl residues that are phosphorylated by tyrosine kinases. The PTPH1 protein localizes to focal adhesions, a major site of action for oncogenic protein tyrosine kinases. PTPH1 overexpression may counter the effects of oncogenic protein tyrosine kinases, such as those of transforming viruses, by interfering with or reversing cell transformation that is associated with the activity of a protein tyrosine kinase.

Abstract: DNA which encodes a protein homologous to the protein tyrosine phosphatases (PTPases) which catalyze the dephosphorylation of proteins in which tyrosyl residues have been phosphorylated through the action of a protein kinase. The protein, which appears as if it will localize to focal adhesions, is also the subject of the present invention. In particular, it relates to cDNA encoding a protein, referred to as PTPH1.

Abstract: Novel Type III density enhanced protein tyrosine phosphatases are disclosed and exemplified by human DEP-1 enzyme. Polynucleotides encoding huDEP-1 are disclosed, along with methods and materials for production of the same by recombinant procedures. Binding molecules specific for DEP-1 are also disclosed as useful for modulating the biological activities of DEP-1.

Abstract: DNA which encodes a protein homologous to the protein tyrosine phosphatases (PTPases) which catalyze the dephosphorylation of proteins in which tyrosyl residues have been phosphorylated through the action of a protein kinase. The protein, which appears as if it will localize to focal adhesions, is also the subject of the present invention. In particular, it relates to cDNA encoding a protein, referred to as PTPH1.Overexpression of PTPH1 may be a powerful approach to countering the effects of oncogenic protein tyrosine kinases, such as those of transforming viruses, and interfering with or reversing cell transformation. This would provide a means of preventing or reversing abnormally high levels of phosphotyrosine associated with any disease or condition, such as preventing or reversing malignancy associated with the activity of a protein tyrosine kinase.

Abstract: DNA which encodes a protein homologous to the protein tyrosine phosphatases (PTPases) which catalyze the dephosphorylation of proteins in which tyrosyl residues have been phosphorylated through the action of a protein kinase. The protein, which appears as if it will localize to focal adhesions, is also the subject of the present invention. In particular, it relates to cDNA encoding a protein, referred to as PTPH1.