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 antimetastatic activity of adriamycin in combination with proteinase inhibitors was investigated in mice bearing the metastatic tumors L1210 leukemia, Lewis lung carcinoma or M5076 sarcoma. Leupeptin, a cathepsin B inhibitor, when administered as a single agent was devoid of antimetastatic activity but some therapeutic activity was noted in mice with Lewis lung carcinoma when the agent was administered in combination with adriamycin. Pepstatin A, a cathepsin D inhibitor, had no effect as a single agent in mice with L1210 leukemia but displayed some antimetastatic activity in mice with Lewis lung carcinoma. In mice with M5076 sarcoma the combination of pepstatin A and adriamycin resulted in antimetastatic activity significantly greater than that observed with each agent alone. These results suggest that combinations of proteinase inhibitors with antitumor drugs such as adriamycin, might result in more effective antimetastatic treatment.
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PMID:Antimetastatic activity of adriamycin in combinations with proteinase inhibitors in mice. 233 38

The proteolytic activity in homogenates and extracts of subcellular fractions prepared from subcutaneous Lewis lung carcinoma was determined using proteins and synthetic peptides as substrates. The presence of cathepsin D, plasminogen activator, cathepsin B-, cathepsin G- and elastase-like enzymes was observed. No difference was revealed between the proteolytic activity in homogenates of Lewis lung carcinoma, at the growth stage examined, and in homogenates of normal lung. High specific activities were found in the lysosomal extract, whereas decreasing activities were found in the nuclear extract, the homogenate and the postlysosomal mitochondrial supernatant; no active or trypsin-activatable collagenase activity was detected. The presence in the tumor tissue of these enzymatic activities is in agreement with their proposed role in the process of metastasis. The lack of differences between homogenates of tumor and normal lung tissue suggests that the use of whole cells is required to selectively study tumor proteinases specifically involved in tumor malignancy.
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PMID:Methodologic problems encountered in the assay of proteinases in Lewis lung carcinoma, a mouse metastasizing tumor. 629 35

The aim of the study was an assessment of some lysosomal enzymes activity in serum and in tumors of patients with lung cancer histopathologically confirmed as squamous cell lung carcinoma. The first group constisted of 10 patients with stage II of the disease and the second group consisted of 11 patients with stage III of the disease. Lysosomal enzymes activities were assayed in serum before surgery and on the 10th day after surgery in serum and in tumors. Arylsuphatase, cathepsin D and acid phosphatase activities were higher in the patients serum than in that of the control group. The decrease of arylsulphatase and cathepsin D activities after surgery was statistically significant in both groups of patients, but the cathepsin D activity was still 3 times higher in patients than in those from the control group. The decrease of acid phosphatase activity after surgery was about 50% in both groups of patients and this decrease was statistically significant. The arylsulphatase and acid phosphatase activity in tumors was nearly 3 times higher in stage III patients than it was in stage II patients, but the cathepsin D activity was nearly the same in both patient groups. Higher lysosomal enzyme activity may be a useful factor in diagnosing and monitoring of lung cancer. However, further investigations are needed.
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PMID:Activity of some lysosomal enzymes in serum and in tumors of patients with squamous cell lung carcinoma. 1204 53

To investigate the proteomic background of malignancies of the pleura, we examined and compared the proteomic profile of malignant pleural mesothelioma (MPM)(10 cases), lung adenocarcinoma (11 cases), squamous cell carcinoma of the lung (13 cases), pleomorphic carcinoma of the lung (3 cases) and synovial sarcoma (6 cases). Cellular proteins were extracted from specific populations of tumor cells recovered by laser microdissection. The extracted proteins were labeled with CyDye DIGE Fluor saturation dyes and subjected to two-dimensional difference gel electrophoresis (2D-DIGE) using a large format electrophoresis device. Among 3875 protein spots observed, the intensity of 332 was significantly different (Wilcoxon p value less than 0.05) and with more than two-fold inter-sample-group average difference between the different histology groups. Among these 332, 282 were annotated by LC-MS/MS and included known biomarker proteins for MPM, such as calretinin, as well as proteins previously uncharacterized in MPM. Tissue microarray immunohistochemistry revealed that the expression of cathepsin D was lower in MPM than in lung adenocarcinoma (15% vs. 44% of cases respectively in immunohistochemistry). In conclusion, we examined the protein expression profile of MPM and other lung malignancies, and identified cathepsin D to distinguish MPM from most popular lung cancer such as lung adenocarcinoma.
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PMID:Proteomic study of malignant pleural mesothelioma by laser microdissection and two-dimensional difference gel electrophoresis identified cathepsin D as a novel candidate for a differential diagnosis biomarker. 2205 4