We are analyzing https://link.springer.com/article/10.1007/bf02737885.

Title:
Cathepsins as effector proteases in hepatocyte apoptosis | Cell Biochemistry and Biophysics
Description:
Cathepsins B and D appear to act as part of the effector protease cascade in hepatocyte apoptosis, both in bile salt-induced apoptosis and CPT-induced apoptosis of hepatocellular cancer cell lines. It is important to note that these proteases do not appear to participate in many models of apoptosis studied to date; in fact, cathepsin inhibitors have been used as negative controls to show that enzymes other than caspases are not involved in apoptosis. In particular, it has been shown that cathepsin B inhibitors do not prevent many models of apoptosis in lymphocytes (43). Further, our experiments have shown that not all models of hepatocyte apoptosis are mediated by cathepsins. For example, staurosporine-induced apoptosis is not inhibited by cathepsin B inhibitors in primary hepatocytes or in cell lines stably transfected with the cathepsin B antisense construct. Although the signaling pathways leading to activation of cathepsins B and D in hepatocyte apoptosis are not completely understood, we hypothesize that a caspase 8-like protein may be involved proximal to cathepsins D and B (Fig. 6). The precise mechanism by which cathepsin B is translocated from lysosomes to “apoptotic targets” is currently under investigation in our laboratory. Because of the relative promiscuity of cathepsin B as protease, it is likely that it is involved in nonspecific protein degradation in apoptotic bodies; however, cathepsin B has also been shown to degrade certain specific proteins, such as histones, which may be directly relevant to the apoptotic process. Further evaluation of the role of cathepsins B and D in apoptosis should include the determination of specific proteolytic targets that result in the biochemical and morphologic manifestations of apoptosis.
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google, scholar, cas, pubmed, article, apoptosis, cathepsin, cell, bile, gores, protease, cathepsins, roberts, death, proteases, hepatocyte, inhibitors, human, privacy, cookies, content, research, saltinduced, activation, mechanism, apoptotic, access, rat, bronk, mort, publish, search, effector, adjei, hepatocytes, mach, cells, biol, chem, processing, data, information, log, journal, gregory, cancer, lines, models, involved, shown,

Topics {✒️}

month download article/chapter mort1/fadd-interacting protease death-inducing signaling complex hepatobiliary diseases—basic research bile salt-induced apoptosis fadd-homologous ice/ced-3 bile acid-induced apoptosis article cell biochemistry full article pdf privacy choices/manage cookies bile duct ligation human hepatoma cells hepatic injury induced toxic bile salts bile acid transport cpt-induced apoptosis staurosporine-induced apoptosis signaling pathways leading mature enzyme relies active cell death normal rat livers hep 3b cells protease-dependent pathway protease cascade contributes target protease specificity family protease requirements european economic area basic biological phenomenon wild-type p53 hormone dependent tissues secondary palatine shelves multicenter controlled trial mature formin vitro falk symposium series93 dna topoisomerase poisons viral serpin crm delayed neuronal death cultured endothelial cells conditions privacy policy proteolytic processingin vitro effector protease cascade lysosomal cysteine proteinases apoptotic exit effort lysosomal cysteine proteases cancer metastasis rev accepting optional cookies hepatocyte apoptosis published wide ranging implications primary biliary cirrhosis basic research

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         headline:Cathepsins as effector proteases in hepatocyte apoptosis
         description:Cathepsins B and D appear to act as part of the effector protease cascade in hepatocyte apoptosis, both in bile salt-induced apoptosis and CPT-induced apoptosis of hepatocellular cancer cell lines. It is important to note that these proteases do not appear to participate in many models of apoptosis studied to date; in fact, cathepsin inhibitors have been used as negative controls to show that enzymes other than caspases are not involved in apoptosis. In particular, it has been shown that cathepsin B inhibitors do not prevent many models of apoptosis in lymphocytes (43). Further, our experiments have shown that not all models of hepatocyte apoptosis are mediated by cathepsins. For example, staurosporine-induced apoptosis is not inhibited by cathepsin B inhibitors in primary hepatocytes or in cell lines stably transfected with the cathepsin B antisense construct. Although the signaling pathways leading to activation of cathepsins B and D in hepatocyte apoptosis are not completely understood, we hypothesize that a caspase 8-like protein may be involved proximal to cathepsins D and B (Fig. 6). The precise mechanism by which cathepsin B is translocated from lysosomes to “apoptotic targets” is currently under investigation in our laboratory. Because of the relative promiscuity of cathepsin B as protease, it is likely that it is involved in nonspecific protein degradation in apoptotic bodies; however, cathepsin B has also been shown to degrade certain specific proteins, such as histones, which may be directly relevant to the apoptotic process. Further evaluation of the role of cathepsins B and D in apoptosis should include the determination of specific proteolytic targets that result in the biochemical and morphologic manifestations of apoptosis.
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      headline:Cathepsins as effector proteases in hepatocyte apoptosis
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         Biological and Medical Physics
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