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)

The role which two proteolytic enzymes (cathepsin D, CD and calcium-activated protease, CAP) might play in the early anabolic and subsequent catabolic phases of skeletal muscle protein metabolism was investigated in rats fed normal and protein-deficient (50 g/kg) diets. Enzyme measurements were performed on crude homogenate and subcellular fractions of mixed thigh muscle. In normal pregnancy there was no evidence that the changes in muscle protein mass which occurred were assisted by changes in the activities of CD or CAP. CAP activity was, however, reduced throughout protein-deficient pregnancy. Electron micrographs of gastrocnemius muscle samples taken on day 21 of pregnancy suggested increased lysosome numbers in the protein-deficient animals. However, the specific activity of CD in the muscle microsomal-mitochondrial fraction from these animals showed decreased specific activity. Thus, neither CD nor CAP play any major role in releasing amino acids from maternal skeletal muscle for placental and fetal use during protein deficiency. Changes in CAP activity in early pregnancy may indirectly help to protect the fetus from protein deficiency by allowing maternal protein mass to accumulate early in pregnancy for catabolism and use at a later stage.
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PMID:Cathepsin D and calcium-activated protease activities in skeletal muscle of normal and protein-deficient pregnant rats. 631 33

We have compared the DNase I hypersensitivity of the regulatory region of two estrogen-regulated genes, pS2 and cathepsin D in hormone-dependent and -independent breast carcinoma cell lines. This strategy allowed the identification of two important control regions, one in pS2 and the other in cathepsin D genes. In the hormone-dependent MCF7 cell line, within the pS2 gene 5'-flanking region, we detected two major DNase I hypersensitive sites, induced by estrogens and/or IGFI: pS2-HS1, located in the proximal promoter and pS2-HS4, located -10.5 Kb from the CAP site, within a region that has not been cloned. The presence of these two DNase I hypersensitive sites correlates with pS2 expression. Interestingly in MCF7 cells, estrogens and IGFI induced indistinguishable chromatin structural changes over the pS2 regulatory region, suggesting that the two transduction-pathways converge to a unique chromatin target. In two cell lines that do not express pS2, MDA MB 231, a hormone-independent cell line that lacks the estrogen receptor alpha, and HE5, a cell line derived from MDA MB 231 by transfection that expresses estrogen receptor alpha, there was only one hormone-independent DNase I hypersensitive site. This site, pS2-HS2, was located immediately upstream of pS2-HS1. In MCF7 cells, two major DNase I hypersensitive sites were present in the 5'-flanking sequences of the cathepsin D gene, which is regulated by estrogens in these cells. These sites, catD-HS2 and catD-HS3, located at positions -2.3 Kb and -3.45 Kb, respectively, were both hormone-independent. A much weaker site, catD-HS1, covered the proximal promoter. In MDA MB 231 cells, that express cathepsin D constitutively, we detected an additional strong hormone-independent DNase I hypersensitive site, catD-HS4, located at position -4.3 Kb. This region might control the constitutive over-expression of cathepsin D in hormone-independent breast cancer cells. All together, these data demonstrate that a local reorganization of the chromatin structure over pS2 and cathepsin D promoters accompanies the establishment of the hormone-independent phenotype of the cells.
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PMID:Chromatin structure of the regulatory regions of pS2 and cathepsin D genes in hormone-dependent and -independent breast cancer cell lines. 992 10

A monoclonal antibody (MAb; MAb CAP1) that was reactive with extracellular aspartic proteinase of Candida albicans (CAP) was produced. The MAb showed strong sensitivity and reactivity to CAP but not to the aspartic proteinases of Candida parapsilosis, Candida tropicalis, and Aspergillus fumigatus or to human cathepsin D or porcine pepsin. The epitope of the CAP recognized by the MAb was the proteinaseous part of CAP and the putative epitope of the MAb was located in the Asp77 to Gly103 sequence. This antibody could be useful for the characterization of CAP and would be a valuable probe for the detection of CAP antigen in the sera of patients with invasive candidiasis.
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PMID:Production, characterization, and epitope mapping of a monoclonal antibody against aspartic proteinase of Candida albicans. 1022 50