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.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Telecommunications
Science

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 7,625,932 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We can't tell how the site generates income.

While many websites aim to make money, others are created to share knowledge or showcase creativity. People build websites for various reasons. This could be one of them. Link.springer.com has a revenue plan, but it's either invisible or we haven't found it.

Keywords {🔍}

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

Schema {🗺️}

WebPage:
      mainEntity:
         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.
         datePublished:
         dateModified:
         pageStart:71
         pageEnd:88
         sameAs:https://doi.org/10.1007/BF02737885
         keywords:
            Bile salts
            Cathepsin B
            Cathepsin D
            Hepatocellular carcinoma
            Topoisomerase inhibitors
            Biochemistry
            general
            Pharmacology/Toxicology
            Biotechnology
            Cell Biology
            Biological and Medical Physics
            Biophysics
         image:
         isPartOf:
            name:Cell Biochemistry and Biophysics
            issn:
               1559-0283
               1085-9195
            volumeNumber:30
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Humana Press
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Lewis R. Roberts
               affiliation:
                     name:Center for Basic Research in Digestive Diseases
                     address:
                        name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Philip N. Adjei
               affiliation:
                     name:Center for Basic Research in Digestive Diseases
                     address:
                        name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Gregory J. Gores
               affiliation:
                     name:Center for Basic Research in Digestive Diseases
                     address:
                        name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      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.
      datePublished:
      dateModified:
      pageStart:71
      pageEnd:88
      sameAs:https://doi.org/10.1007/BF02737885
      keywords:
         Bile salts
         Cathepsin B
         Cathepsin D
         Hepatocellular carcinoma
         Topoisomerase inhibitors
         Biochemistry
         general
         Pharmacology/Toxicology
         Biotechnology
         Cell Biology
         Biological and Medical Physics
         Biophysics
      image:
      isPartOf:
         name:Cell Biochemistry and Biophysics
         issn:
            1559-0283
            1085-9195
         volumeNumber:30
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Humana Press
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Lewis R. Roberts
            affiliation:
                  name:Center for Basic Research in Digestive Diseases
                  address:
                     name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Philip N. Adjei
            affiliation:
                  name:Center for Basic Research in Digestive Diseases
                  address:
                     name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Gregory J. Gores
            affiliation:
                  name:Center for Basic Research in Digestive Diseases
                  address:
                     name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Cell Biochemistry and Biophysics
      issn:
         1559-0283
         1085-9195
      volumeNumber:30
Organization:
      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Center for Basic Research in Digestive Diseases
      address:
         name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
         type:PostalAddress
      name:Center for Basic Research in Digestive Diseases
      address:
         name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
         type:PostalAddress
      name:Center for Basic Research in Digestive Diseases
      address:
         name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Lewis R. Roberts
      affiliation:
            name:Center for Basic Research in Digestive Diseases
            address:
               name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
               type:PostalAddress
            type:Organization
      name:Philip N. Adjei
      affiliation:
            name:Center for Basic Research in Digestive Diseases
            address:
               name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
               type:PostalAddress
            type:Organization
      name:Gregory J. Gores
      affiliation:
            name:Center for Basic Research in Digestive Diseases
            address:
               name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
      name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
      name:Division of Gastroenterology, Mayo Clinic and Mayo Foundation, Center for Basic Research in Digestive Diseases, Rochester
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(123)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

3.97s.

LINK . SPRINGER . COM {}