Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.23.5 (cathepsin D)
 4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Current topics are presented on four urinary proteins under investigations with special emphasis on importance of preanalytical sampling and assay standardization. These comprise of albumin, protein 1 (P1), beta 2-microglobulin (beta 2-m), and Type IV collagen. Microalbuminuria is an essential marker for early diabetic nephropathy. The author is trying to reduce the discrepancy of urinary albumin value with value assignment from CRM470, BCR international reference material, to calibrator in each assay system. At the same time nonspecific binding of the protein on urine containers were found, which can cause the discrepancy. Furthermore structure of albumin both in calibrator and urine is important. Protein 1 is a low molecular weight nonglycoprotein of 14 kDa isolated from pathologic urine. Marked sex-related difference was noted in urine, being higher in male than female. This is due to the contamination from prostate. Its localization was finally demonstrated with immunohistochemical staining and a RT-PCR method. With the same methods the protein is demonstrated to be synthesized in female prostate. beta 2-m is easily degraded in acid urine. Employing various immunochemical methods and analyses of its amino acid sequences, we successfully identified cathepsin D as one of acid proteases responsible for the degradation. Urinary measurement of type IV collagen is now clinically under use for an independent marker for early diabetic nephropathy. Nonspecific elevation was observed in urine with UTI, in which mechanisms is should be clarified.
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PMID:[Current topics on urinary proteins: human albumin, protein 1, beta 2-microglobulin, and type IV collagen]. 1216 72

Efficacious vaccines require antigens that elicit productive immune system activation. Antigens that afford robust antibody production activate both B and T cells. Elucidating the antigen properties that enhance B-T cell communication is difficult with traditional antigens. We therefore used ring-opening metathesis polymerization to access chemically defined, multivalent antigens containing both B and T cell epitopes to explore how antigen structure impacts B cell and T cell activation and communication. The bifunctional antigens were designed so that the backbone substitution level of each antigenic epitope could be quantified using (19)F NMR. The T cell peptide epitope was appended so that it could be liberated in B cells via the action of the endosomal protease cathepsin D, and this design feature was critical for T cell activation. Antigens with high BCR epitope valency induce greater BCR-mediated internalization and T cell activation than did low valency antigens, and these high-valency polymeric antigens were superior to protein antigens. We anticipate that these findings can guide the design of more effective vaccines.
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PMID:Multivalent Antigens for Promoting B and T Cell Activation. 2597 17