2 results about "Site specific mutation" patented technology

According to the application of the reagent for detecting the phosphorylation level of the S202 and T205 sites of the MAPT protein in preparation of the renal fibrosis diagnosis product, the function research of the MAPT protein is expanded from the traditional field of glomerular podocytes to renal tubular epithelial cells and the fibrosis pathological process of the renal tubular epithelial cells for the first time, and a brand new direction of the MAPT protein in renal disease research is opened up. Different from the conventional general research means which only depends on overall gene knockout or overexpression, the method provided by the invention realizes accurate analysis of the function of the MAPT key phosphorylation site by using the site-specific mutant. Through a systematic function determination experiment, the invention discloses an anti-intuition biological rule with great theoretical significance: although phosphorylation of the sites S202 and T205 obviously drives the fibrosis process of the renal tubular epithelial cells, the fibrosis phenotype cannot be improved by simulating the dephosphorylation state (S202A / T205A mutant) of the sites.

The application discloses application of a reagent for detecting phosphorylation levels of MAPT protein S202 and T205 sites in preparation of a kidney fibrosis diagnosis product, and first extends function research of the MAPT protein from a traditional glomerular podocyte field to a renal tubular epithelial cell and a fibrosis pathological process thereof, and opens up a brand-new direction of the MAPT protein in kidney disease research. Unlike previous general research means which only depend on whole gene knockout or overexpression, the application realizes accurate analysis of functions of key phosphorylation sites of the MAPT protein by using site-specific mutants. Through systematic function determination experiments, the application discloses a counterintuitive biological law with great theoretical significance: although S202 and T205 site phosphorylation significantly drives a fibrosis process of the renal tubular epithelial cell, simulation of a dephosphorylation state (S202A / T205A mutant) cannot improve the fibrosis phenotype.