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)

Insulin degrading enzymes of rat liver cytosol, the so-called insulin and glucagon degrading proteinase (IGP, EC 3.4.23.5), and two forms of the insulin degrading thiol-protein-disulfide oxidoreductase/isomerase (glutathione-insulin transhydrogenase, TPO, EC 1.8.4.2/5.3.4.1) were separated from each other and partially purified on DEAE-Sephadex. The highly purified proteinase was obtained by polyacrylamide gel electrophoresis of the DEAE-Sephadex-purified enzyme fraction and was used to produce monospecific antibodies to the IGP in rabbits. Strong evidence is given that the insulin and glucagon degrading proteinase is an autonomous enzyme existing in addition to the TPO forms in the cytosol of the liver. Combined action of the proteinase and the TPO system on radioiodinated insulin under various conditions in vitro revealed an independent and non-sequential degradation of insulin by these two enzyme systems.
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PMID:The insulin and glucagon degrading proteinase of rat liver. Separation of the proteinase from the thiol-proteindisulfide oxidoreductases. 637 96

Cathepsin D (EC 3.4.23.5), the insulin and glucagon degrading proteinase (IGP, EC 3.4.22.-) and the thiol-protein disulfide oxidoreductase (TPO, EC 1.8.4.2, 5.3.4.1) participate in the intracellular protein degradation, the last one also in post-protein-synthetic processing. The distribution of these enzymes was determined in isolated liver parenchymal cells, Kupffer cells and endothelial cells by means of immunochemical methods in order to further characterize these cell types. The cathepsin D content, expressed as microgram enzyme per mg protein, is about 3 fold higher in endothelial cells and about 5 to 24 fold higher in Kupffer cells than in parenchymal cells. This result confirms an earlier report which is based on the activity determination. The TPO concentration is highest in parenchymal cells with half of that concentration in Kupffer cells and one third in endothelial cells. About 0.5% of the total liver protein is represented by this enzyme. The IGP has been found to be totally absent in non-parenchymal cells. It represents, therefore, together with the glucose-6-phosphatase a valuable marker enzyme for parenchymal cells of rat liver.
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PMID:Distribution of thiol-protein disulfide oxidoreductase, insulin-glucagon proteinase and cathepsin D in different cell types of the rat liver. 644 77