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, bile, cell, gores, protease, cathepsins, roberts, inhibitors, death, proteases, hepatocyte, human, saltinduced, rat, bronk, mort, content, research, effector, adjei, activation, mechanism, apoptotic, access, references, mach, cells, biol, chem, log, publish, gregory, lines, models, involved, shown, hepatocytes, caspase, protein, proteolytic, liver, hepatic, kerr, rev,

Topics {✒️}

loading [mathjax]/jax/output/html-css/config privacy choices/manage cookies mort1/fadd-interacting protease death-inducing signaling complex fadd-homologous ice/ced-3 hepatobiliary diseases—basic research bile salt-induced apoptosis hepatic injury induced bile acid-induced apoptosis article cell biochemistry full article pdf bile duct ligation human hepatoma cells toxic bile salts conditions privacy policy bile acid transport human liver cathepsin bcl-2 family proteins signaling pathways leading mature enzyme relies author correspondence cpt-induced apoptosis staurosporine-induced apoptosis normal rat livers active cell death hep 3b cells protease-dependent pathway protease cascade contributes target protease specificity family protease requirements 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 support cancel contracts delayed neuronal death unique caspase 8-cathepsin cultured endothelial cells proteolytic processingin vitro lysosomal cysteine proteinases effector protease cascade wide ranging implications primary biliary cirrhosis hepatocyte apoptosis published specific proteolytic targets

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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
      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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         Cathepsin B
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         Hepatocellular carcinoma
         Topoisomerase inhibitors
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         general
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         Cell Biology
         Biological and Medical Physics
         Biophysics
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