Localization of cathepsin B in two human lung cancer cell lines
| Autor: | G Trefz, Tamara T. Lah, H Spring, Eberhard Spiess, W Ebert, Erdel M, S Habermaas |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Pathology
medicine.medical_specialty Lung Neoplasms Histology Fluorescent Antibody Technique Cathepsin D Adenocarcinoma Biology Cathepsin B Cell Line Cathepsin H Tumor Cells Cultured Adenocarcinoma of the lung medicine Humans Fibroblast Cathepsin S Cell Membrane Fibroblasts medicine.disease Immunohistochemistry Molecular biology medicine.anatomical_structure Cell culture Carcinoma Squamous Cell Anatomy Lysosomes Intracellular |
| Zdroj: | Journal of Histochemistry & Cytochemistry. 38:1313-1321 |
| ISSN: | 1551-5044 0022-1554 |
| DOI: | 10.1177/38.9.2201737 |
| Popis: | We demonstrated the cysteine proteinase cathepsin B in two human lung tumor cell lines by cytochemical and immunocytochemical methods. The cell lines were derived from a squamous cell carcinoma of the lung (HS-24) and a metastasis to the adrenal gland from an adenocarcinoma of the lung (SB-3). For comparison and control, normal human lung fibroblasts cells (Wi-38) were also investigated. Intracellular cathepsin B activity was detected in all three cell lines. SB-3 and the normal fibroblast cells showed almost equal cathepsin B activity, which was considerably stronger than that in the HS-24 cells. Specific inhibitors for cathepsin B (E64, leupeptin, antipain) suppressed its activity completely. Stefin A, the physiological cathepsin B inhibitor, was less effective; this might depend on its limited penetrability into living cells. Localization of the cathepsin B was performed by conventional immunofluorescence microscopy and laser scanning microscopy. With specific anti-cathepsin B antibodies, the enzyme was localized in HS-24, SB-3, and Wi-38 fibroblast cells within perinuclear granules representing the lysosomal compartment. In the SB-3 cells, we additionally localized a minor fraction of the enzyme bound to the plasma membrane in a speckled distribution, accessible to the antibodies from the outside. This direct demonstration of cathepsin B distribution supports biochemical data about the dual localization of the enzyme in tumor cells. It also supports the possibility of a direct involvement of cathepsin B in the degradation of the extracellular matrix, and thus a contribution of the enzyme in invasion and metastasis. |
| Databáze: | OpenAIRE |
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