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)

Cathepsin D is a cysteine endopeptidase that belongs to the lysosomal enzyme family. The aim of the study was to evaluate the enzyme immunoexpression and activity in selected male genital organs in mature Wistar rats. The activity of cathepsin D was measured spectrophotometrically in homogenates of the testis, epididymis, seminal vesicle and prostate. Immunohistochemical staining was also performed in the ductus deferens. Enzyme activity was found in the following sequence: testis>epididymis>dorsal prostatic lobe>seminal vesicle>lateral prostatic lobe>ventral prostatic lobe. Although there were differences in enzyme activity between various organs of the male reproductive system, cathepsin D immunoreactivity was seen exclusively in the Sertoli and Leydig cells in the testis.
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PMID:The activity and immunoexpression of cathepsin D in rat male reproductive organs. 1677 97

Some of the phenotypes of mice deficient for the lysosomal cysteine endopeptidase cathepsin L (Ctsl) are characterized by large dysmorphic vesicles in the cytoplasm. Specifically, the heart (dilative cardiomyopathy), the thyroid (impaired thyroglobulin processing) and keratinocytes (periodic hair loss and epidermal hyperproliferation) are affected. We hypothesized that the formation of aberrant vesicles is owing to defects in macroautophagy. Therefore, primary mouse embryonic fibroblasts (MEF), which were derived from Ctsl(-/-) animals crossed with mice transgenic for the autophagy marker GFP-LC3, were investigated. Ctsl(-/-) MEF show increased number and size of vesicular structures belonging to the 'acidic' cellular compartment and are also characterized by GFP-LC3. Induction of autophagy by nutrient starvation or rapamycin treatment showed no significant impairment of the initiation of autophagy, the formation of autophagosomes or autophagosome-lysosome fusion in Ctsl(-/-) MEF, but co-localization of GFP-LC3 and Lamp1 revealed unusually large autophagolysosomes filled with Lamp1. Furthermore, the soluble lysosomal enzyme cathepsin D was elevated in Ctsl(-/-) MEF. Thus, degradation of autophagolysosomal content is impaired in the absence of Ctsl. This could slow the turnover of autophagolysosomes and result in accumulation of the dysmorphic and 'acidic' vesicles that were previously described in the context of the pathological phenotypes of Ctsl(-/-) mice.
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PMID:Impaired turnover of autophagolysosomes in cathepsin L deficiency. 2053 83