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)

Six proteolytic enzymes were assayed for activity in quaking CNS in examining the hypothesis that increased proteolytic activity contributes to the hypomyelination characteristics of this mutant. Cathepsin B-like enzyme, cathepsin D, neutral proteinase, calcium-activated neutral proteinase, prolyl endopeptidase, and diaminopeptidase II were assayed in whole homogenate of brain or spinal cord and each was found to have activity similar to that in normal mice. These results do not support a relationship between proteolysis and the genetic defect and suggest that other factors should be investigated to delineate the pathogenesis of this mutant.
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PMID:Proteolysis in quaking mouse brain and spinal cord. 301 Jan 46

The activities of a number of peptide-degrading enzymes were compared in homogenates of GH3 cells and rat anterior pituitaries. The enzymes studied were prolyl endopeptidase (EC 3.4.21.26), a soluble metalloendopeptidase, pyroglutamyl peptide hydrolase (EC 3.4.11.8), a multicatalytic protease complex, cathepsin B (EC 3.4.22.1), cathepsin D (EC 3.4.23.5), aminopeptidase (EC 3.4.11.2), and a membrane-bound neutral metalloendopeptidase (EC 3.4.24.11). Specific substrates were used to measure the activities, and active-site-directed inhibitors were used to verify the identities of the enzymes studied. Of the two lysosomal enzymes studied, cathepsin B, the enzyme with the highest activity in both preparations, had 5 times the activity in GH3 cell homogenates as in anterior pituitary homogenates. Cathespin D had a somewhat higher activity in the anterior pituitary homogenates than in the GH3 cell homogenates. Soluble metalloendopeptidase and prolyl endopeptidase, both cytoplasmic enzymes, had about twice the activity in GH3 cell homogenates as in anterior pituitary homogenates. Membrane-bound neutral metalloendopeptidase in the GH3 cell homogenates had 25% of the activity of the anterior pituitary homogenates. Of the two TRH-degrading enzymes, the activity of prolyl endopeptidase in GH3 cell homogenates was about 25 times higher than that of pyroglutamyl peptide hydrolase. Since the secretory function of the pituitary is in part controlled by neuropeptides, the knowledge of the enzyme profiles of the GH3 cells and the anterior pituitary should be of value in studying the metabolism of neuropeptides and peptide hormones in these systems.
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PMID:Peptide-degrading enzymatic activities in GH3 cells and rat anterior pituitary homogenates. 636 4

The metabolism of LVVH7, an endogenous peptide obtained by cathepsin D hydrolysis of the beta chain of hemoglobin, was studied, in vitro, in the presence of cytosol of rat kidney and compared with angiotensin IV. High metabolic activity was found against these two peptides (half life time < 2 min) in this subcellular fraction. The main products of LVVH7 metabolism by renal cytosol are VVH7, H7 and LVVH6 suggesting both aminopeptidase and carboxypeptidase activities. The use of PEP inhibitor in kidney cytosol permitted to demonstrate the major role of prolyl endopeptidase (PEP) in LVVH7 degradation. This fact was reinforced by a kinetic study investigated with purified enzyme (Km/Vmax about 238 mM-1 s-1 and close to that observed for angiotensin related peptides).
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PMID:In vitro metabolism of LVV-Hemorphin-7 by renal cytosol and purified prolyl endopeptidase. 1461 92