Biomedical subjects
Publications and source records attributed to H Ostrowska.
Ethanol and acetaldehyde inhibited the activity of cathepsin A. In vitro ethanol did not release cathepsin A from liver lysosomes whereas acetaldehyde of high concentration did. Intoxication of rats with ethanol and acetaldehyde evoked a transient increase of free and bound cathepsin A.
Activity of cathepsin A was determined in placenta, fetal membranes and amniotic fluid as well in normal pregnancy as in complicated pregnancy by EPH-gestosis. Measurement of activity was done by N-CbZ-L-glutamyl-tyrosine with pH 5.5. Compared with normal pregnancy activity of cathepsin A was lower in the three materials of EPH-gestosis.
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Several lysosomal proteases including cathepsins B, D, H and L have been found to play a role in the metastasis of tumor cells. However, up to now no information on the role of cathepsin A, a lysosomal multifunctional peptidase, in the proliferative, invasive, and metastatic potential of malignant tumors has been available. In the present study we compared the activity of cathepsin A in lysates of 34 human melanocytic tumors: primary (n = 12) and metastatic (n = 5) malignant melanoma, dysplastic pigmented nevi (n = 6) and pigmented nevi without evidence of dysplastic melanocytes (n = 11). The carboxypeptidase activity of cathepsin A was assayed at pH 5.0 with its specific substrate Cbz-Phe-Ala. The amount of released C-terminal alanine was measured by the ninhydrin method. We found that lysates of primary malignant melanoma lesions exhibited significantly higher cathepsin A activity than lysates of dysplastic and normal pigmented nevi. The cathepsin A activity in lysates of metastatic lesions of malignant melanoma was significantly higher than in primary focus lysates. It seems that cathepsin A may play a role in malignant transformation and metastatic dissemination of malignant melanoma.