Cathepsin B and L activities in gastric cancer tissue: Correlation with histological findings

Immunostained cathepsins B and L correlate with depth of invasion and different metastatic pathways in early stage gastric carcinoma

“…Although the immunohistochemical method provides a semiquantitative assessment of the protein level, our findings confirmed the previous observations showing cathepsins were rich in tumor tissues. Elevated cathepsins also are observed in poorly differentiated adenocarcinomas, 24,25 whereas our data showed no differences in histologic type. This discrepancy might be due to the numbers of cases studied, the grade of progression of the tumors, and the methods used to evaluate the proteases.…”

“…9,10 High levels of expression have been reported not only in tumor tissues, 21,22 but in sera and urine of patients with gastric carcinoma. 23 Using synthetic substrates, Watanabe et al 24 measured the enzymatic activities of both cathepsins in 29 gastric carcinoma tissues. They showed that the activities in the cancer tissues were higher than those in surrounding noncancerous mucosa; furthermore, greater cathepsin B activity was observed in lymph node positive tumors.…”

Lysosomes in cell death

“…For example, increased expression and activity of cathepsin B and/or cathepsin D have been observed in breast (Castiglioni et al, 1994), colorectal (Campo et al, 1994;Meyer et al, 1997), gastric (Watanabe et al, 1989), lung (Sukoh et al, 1994), prostate (Sinha et al, 1995), and thyroid cancers (Shuja and Murnane, 1996), as well as in different brain tumors, including gliomas and meningiomas (Rempel et al, 1994;Levicar et al, 2003), and the magnitude of expression has often prognostic significance. Many authors have suggested that enhanced secretion of these proteases by exocytosis promotes cancer growth, invasion, and metastasis by promoting degradation of extracellular connective matrices and angiogenesis (Koblinski et al, 2000).…”

Modulation of cystatin C expression impairs the invasive and tumorigenic potential of human glioblastoma cells

“…Stefin A is one of such inhibitors inversely related to malignancy; reduced expression of stein A mRNA and protein has been linked to a reduction in its inhibitory capacity against cysteine proteinases (Sloane, 1990;Sloane et al, 1990). Several reports have focused on the role of cysteine proteases (Terada et al, 1995;Sukoh et al, 1994;Watanabe et al, 1989;Murnane et al, 1991;Sheahan et al, 1989;Mort et al, 1980;Sloane, 1990) or cysteine protease inhibitors (Lah et al, 1992) in cancer. In general, a large number of normal and abnormal processes are controlled by maintaining a balance between proteinases and their inhibitors (Bobek and Levine, 1992).…”