78 results about "Furin" patented technology

This patent discloses compositions and methods of use thereof to normalize the blood glucose levels of patients with type 2 diabetes. It relates particularly to a plasmid comprising a chicken β actin promoter and enhancer; a modified GLP-1 (7-37) cDNA (pβGLP1), carrying a furin cleavage site, which is constructed and delivered into a cell for the expression of active GLP-1.

An isolated chimeric GLP-1 nucleic acid sequence encoding a human pro-insulin leader, a glucagon-like peptide-1 (GLP-1), and a furin cleavable site between the human pro-insulin leader sequence and the GLP-1 is provided. Also provided is an isolated modified chimeric GLP-1 nucleic acid sequence encoding a human pro-insulin leader, a glucagon-like peptide-1 (GLP-1), and a furin cleavable site between the human pro-insulin leader sequence and the GLP-1. Recombinant expression vectors comprising the chimeric GLP-1 nucleic acid sequences, which produce GLP-1 constitutively are provided, as are human cells transfected with such an expression vector in combination with an expression vector comprising a proinsulin nucleic acid sequence and an expression vector comprising a furin and a glucose-regulatable TGF-alpha promoter. Methods of producing human GLP-1 constitutively are provided as are method of producing GLP-1 and insulin or in a glucose-dependent manner using such transfected cells. Methods of treating a subject having Type II diabetes and methods of treating a subject prone to hyperglycemia or suffering from hyperglycemia are provided in which transfected cells produce human GLP-1 and insulin in a glucose-dependent manner. Also provided are methods of reducing weight in a subject by implanting into the subject transfected cells which produce human GLP-1 and insulin in a glucose-dependent manner.

The present invention provides methods of specifically targeting compounds to cells overexpressing matrix metalloproteinases, plasminogen activators, or plasminogen activator receptors, by administering a compound and a mutant protective antigen protein comprising a matrix metalloproteinase or a plasminogen activator-recognized cleavage site in place of the native protective antigen furin-recognized cleavage site, wherein the mutant protective antigen is cleaved by a matrix metalloproteinase or a plasminogen activator overexpressed by the cell, thereby translocating into the cell a compound comprising a lethal factor polypeptide comprising a protective antigen binding site.

Modified, furin resistant human TSLP polypeptides and polynucleotides encoding the modified human TSLP polypeptides are provided. Pharmaceutical compositions, B and T cell activation agents, assays and methods of use are also described.

The present invention relates to a method for producing a mature von Willebrand Factor (VWF) from von Willebrand Factor pro-peptide comprising the steps:immobilizing VWF pro-peptide on an ion exchange resin,incubating the immobilized VWF pro-peptide with furin to obtain immobilized mature VWF, andisolating mature VWF from the ion exchange resin by elution.

The invention provides a SARS-CoV-2 mutant strain S protein and a subunit vaccine thereof. A furin cleavage site 682-RRAR-685 between the S1 subunit and the S2 subunit of the SARS-CoV-2 mutant strain S protein is replaced with a flexible protein linker; the linker is (GGCAGCGCCAGC), or (GGCGGCGGCAGC)n, or (GGCGGCGGCGGCAGC)n, or (GGC)n; or the linker is GSAS or (GGGS)n or (GGGGS)n or (G)n, wherein n is greater than or equal to 1 and less than or equal to 3, and n is an integer; the amino acid sequence of the SARS-CoV-2 mutant strain S protein is as shown in SEQ ID NO: 2 or as shown in SEQ ID NO: 4. The S protein has great potential as a vaccine antigen for coping with the SARS-CoV-2 mutant strain.

Non-activated tissue-regeneration polypeptides (TRPs) and their preparation methods are disclosed. The TRPs include: a protein transduction domain (PTD) making the polypeptides to permeate a cell membrane without cell membrane receptors; a furin activation domain (FAD) which has at least one proprotein convertase cleavage site and which can be cleaved by the proprotein convertase and activate a tissue regeneration domain (TRD) in cells; and a tissue regeneration domain (TRD) which can be activated by the proprotein convertase cleavage of the FAD to stimulate the growth or formation of tissues or to induce the regeneration of tissues. The TRPs can be mass-produced by cultured bacteria, such as recombinant E. coli, are in a non-activated state before in vivo administration, and their separation, purification, handling, storage and administration are simple and convenient. The in vivo administration of the TRPs is useful to stimulate the formation or regeneration of tissues, such as bones or cartilages, or to improve the fibrosis and cirrhosis of organs, such as kidneys, liver, lungs and heart by pharmacological mechanisms completely different from those of prior rhBMPs or TGF-β proteins.

A foot and mouth disease virus (FMDV) vaccine and method for producing same is described wherein the N terminal portion of the FMDV polyprotein, encoding the four structural proteins, 1A, 1B, 1C, and 1D, are each separated by a non-FMDV protease, preferably a cellular protease, for example, furin. The expression system may be transformed into a cell expressing the non-FMDV protease and the resulting particles recovered for use as a vaccine.