Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves bid cleavage
Photodynamic therapy (PDT) protocols employing lysosomal sensitizers induce apoptosis via a mechanism that causes cytochrome c release prior to loss of mitochondrial membrane potential (ΔΨ m ). The current study was designed to determine how lysosomal photodamage initiates mitochondrial-mediated apo...
Gespeichert in:
Veröffentlicht in: | Cell death and differentiation 2002-09, Vol.9 (9), p.934-944 |
---|---|
Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 944 |
---|---|
container_issue | 9 |
container_start_page | 934 |
container_title | Cell death and differentiation |
container_volume | 9 |
creator | Reiners Jr, J J Caruso, J A Mathieu, P Chelladurai, B Yin, X-M Kessel, D |
description | Photodynamic therapy (PDT) protocols employing lysosomal sensitizers induce apoptosis via a mechanism that causes cytochrome
c
release prior to loss of mitochondrial membrane potential (ΔΨ
m
). The current study was designed to determine how lysosomal photodamage initiates mitochondrial-mediated apoptosis in murine hepatoma 1c1c7 cells. Fluorescence microscopy demonstrated that the photosensitizer N-aspartyl chlorin e6 (NPe6) localized to the lysosomes. Irradiation of cultures preloaded with NPe6 induced the rapid destruction of lysosomes, and subsequent cleavage/activation of Bid, pro-caspases-9 and -3. Pro-caspase-8 was not activated. Release of cytochrome
c
occurred at about the time of Bid cleavage and preceded the loss of ΔΨ
m
. Extracts of purified lysosomes catalyzed the
in vitro
cleavage of cytosolic Bid, but not pro-caspase-3 activation. Pharmacological inhibition of cathepsin B, L and D activities did not suppress Bid cleavage or pro-caspases-9 and -3 activation. These studies demonstrate that photodamaged lysosomes trigger the mitochondrial apoptotic pathway by releasing proteases that activate Bid. |
doi_str_mv | 10.1038/sj.cdd.4401048 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4569095</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>998134081</sourcerecordid><originalsourceid>FETCH-LOGICAL-c519t-9bf15f4261735a6a6741e65965ce7bd0d5b61d4296cf0c2cb3e90e74ee51ac853</originalsourceid><addsrcrecordid>eNp1kUuLFDEUhYMozkO3LiW4cFc9SVUelY0gg47CgDCM65BKbnVXk0rKpLqG_vem7cbRgVkl5Hw5514OQu8oWVHStFd5u7LOrRgjlLD2BTqnTIqKM9K8LPeGk0oRJs_QRc5bQoiQSrxGZ7SmLZWMnaPxDjyYDDj22O7naDcpjoAtNsFhY-dhMfMQw0GeUqysyVOhK4X76H18GMIa-32OOY7G42kT5-jMaNaAh7BEv0DG3eCwLRlLeX2DXvXGZ3h7Oi_Rz69f7q-_Vbc_br5ff76tLKdqrlTXU96zWlDZcCOMkIyC4EpwC7JzxPFOUMdqJWxPbG27BhQByQA4NbblzSX6dPSddt0IzkKYk_F6SsNo0l5HM-j_lTBs9DoumnGhiDoYfDwZpPhrB3nW45AteG8CxF3WsiaE0z9JH56A27hLoSynayplTXmrCrQ6QjbFnBP0fyehRB9q1HmrS436VGP58P7f-R_xU28FuDoCuUhhDekx9hnL3-wPq5E</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217721589</pqid></control><display><type>article</type><title>Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves bid cleavage</title><source>MEDLINE</source><source>SpringerLink Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Reiners Jr, J J ; Caruso, J A ; Mathieu, P ; Chelladurai, B ; Yin, X-M ; Kessel, D</creator><creatorcontrib>Reiners Jr, J J ; Caruso, J A ; Mathieu, P ; Chelladurai, B ; Yin, X-M ; Kessel, D</creatorcontrib><description>Photodynamic therapy (PDT) protocols employing lysosomal sensitizers induce apoptosis via a mechanism that causes cytochrome
c
release prior to loss of mitochondrial membrane potential (ΔΨ
m
). The current study was designed to determine how lysosomal photodamage initiates mitochondrial-mediated apoptosis in murine hepatoma 1c1c7 cells. Fluorescence microscopy demonstrated that the photosensitizer N-aspartyl chlorin e6 (NPe6) localized to the lysosomes. Irradiation of cultures preloaded with NPe6 induced the rapid destruction of lysosomes, and subsequent cleavage/activation of Bid, pro-caspases-9 and -3. Pro-caspase-8 was not activated. Release of cytochrome
c
occurred at about the time of Bid cleavage and preceded the loss of ΔΨ
m
. Extracts of purified lysosomes catalyzed the
in vitro
cleavage of cytosolic Bid, but not pro-caspase-3 activation. Pharmacological inhibition of cathepsin B, L and D activities did not suppress Bid cleavage or pro-caspases-9 and -3 activation. These studies demonstrate that photodamaged lysosomes trigger the mitochondrial apoptotic pathway by releasing proteases that activate Bid.</description><identifier>ISSN: 1350-9047</identifier><identifier>EISSN: 1476-5403</identifier><identifier>DOI: 10.1038/sj.cdd.4401048</identifier><identifier>PMID: 12181744</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Apoptosis ; Apoptosis - drug effects ; Apoptosis - physiology ; BH3 Interacting Domain Death Agonist Protein ; Biochemistry ; Biomedical and Life Sciences ; Carrier Proteins - drug effects ; Carrier Proteins - metabolism ; Caspase 8 ; Caspase 9 ; Caspases - drug effects ; Caspases - metabolism ; Cathepsin D - drug effects ; Cathepsin D - metabolism ; Cell Biology ; Cell Cycle Analysis ; Cell death ; Cell Extracts - pharmacology ; Cytochrome ; Cytochrome c Group - drug effects ; Cytochrome c Group - metabolism ; Enzyme Inhibitors - pharmacology ; Enzyme Precursors - drug effects ; Enzyme Precursors - metabolism ; Life Sciences ; Lysosomes - drug effects ; Lysosomes - enzymology ; Lysosomes - ultrastructure ; Medicine ; Mice ; Mitochondria - drug effects ; Mitochondria - enzymology ; Mitochondria - ultrastructure ; Neoplasms - enzymology ; Neoplasms - physiopathology ; Neoplasms - therapy ; original-paper ; Photochemotherapy ; Photodynamic therapy ; Porphyrins - pharmacology ; Porphyrins - radiation effects ; Stem Cells ; Tumor Cells, Cultured</subject><ispartof>Cell death and differentiation, 2002-09, Vol.9 (9), p.934-944</ispartof><rights>Macmillan Publishers Limited 2002</rights><rights>Copyright Nature Publishing Group Sep 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c519t-9bf15f4261735a6a6741e65965ce7bd0d5b61d4296cf0c2cb3e90e74ee51ac853</citedby><cites>FETCH-LOGICAL-c519t-9bf15f4261735a6a6741e65965ce7bd0d5b61d4296cf0c2cb3e90e74ee51ac853</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/sj.cdd.4401048$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/sj.cdd.4401048$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12181744$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reiners Jr, J J</creatorcontrib><creatorcontrib>Caruso, J A</creatorcontrib><creatorcontrib>Mathieu, P</creatorcontrib><creatorcontrib>Chelladurai, B</creatorcontrib><creatorcontrib>Yin, X-M</creatorcontrib><creatorcontrib>Kessel, D</creatorcontrib><title>Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves bid cleavage</title><title>Cell death and differentiation</title><addtitle>Cell Death Differ</addtitle><addtitle>Cell Death Differ</addtitle><description>Photodynamic therapy (PDT) protocols employing lysosomal sensitizers induce apoptosis via a mechanism that causes cytochrome
c
release prior to loss of mitochondrial membrane potential (ΔΨ
m
). The current study was designed to determine how lysosomal photodamage initiates mitochondrial-mediated apoptosis in murine hepatoma 1c1c7 cells. Fluorescence microscopy demonstrated that the photosensitizer N-aspartyl chlorin e6 (NPe6) localized to the lysosomes. Irradiation of cultures preloaded with NPe6 induced the rapid destruction of lysosomes, and subsequent cleavage/activation of Bid, pro-caspases-9 and -3. Pro-caspase-8 was not activated. Release of cytochrome
c
occurred at about the time of Bid cleavage and preceded the loss of ΔΨ
m
. Extracts of purified lysosomes catalyzed the
in vitro
cleavage of cytosolic Bid, but not pro-caspase-3 activation. Pharmacological inhibition of cathepsin B, L and D activities did not suppress Bid cleavage or pro-caspases-9 and -3 activation. These studies demonstrate that photodamaged lysosomes trigger the mitochondrial apoptotic pathway by releasing proteases that activate Bid.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis - drug effects</subject><subject>Apoptosis - physiology</subject><subject>BH3 Interacting Domain Death Agonist Protein</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Carrier Proteins - drug effects</subject><subject>Carrier Proteins - metabolism</subject><subject>Caspase 8</subject><subject>Caspase 9</subject><subject>Caspases - drug effects</subject><subject>Caspases - metabolism</subject><subject>Cathepsin D - drug effects</subject><subject>Cathepsin D - metabolism</subject><subject>Cell Biology</subject><subject>Cell Cycle Analysis</subject><subject>Cell death</subject><subject>Cell Extracts - pharmacology</subject><subject>Cytochrome</subject><subject>Cytochrome c Group - drug effects</subject><subject>Cytochrome c Group - metabolism</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Enzyme Precursors - drug effects</subject><subject>Enzyme Precursors - metabolism</subject><subject>Life Sciences</subject><subject>Lysosomes - drug effects</subject><subject>Lysosomes - enzymology</subject><subject>Lysosomes - ultrastructure</subject><subject>Medicine</subject><subject>Mice</subject><subject>Mitochondria - drug effects</subject><subject>Mitochondria - enzymology</subject><subject>Mitochondria - ultrastructure</subject><subject>Neoplasms - enzymology</subject><subject>Neoplasms - physiopathology</subject><subject>Neoplasms - therapy</subject><subject>original-paper</subject><subject>Photochemotherapy</subject><subject>Photodynamic therapy</subject><subject>Porphyrins - pharmacology</subject><subject>Porphyrins - radiation effects</subject><subject>Stem Cells</subject><subject>Tumor Cells, Cultured</subject><issn>1350-9047</issn><issn>1476-5403</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp1kUuLFDEUhYMozkO3LiW4cFc9SVUelY0gg47CgDCM65BKbnVXk0rKpLqG_vem7cbRgVkl5Hw5514OQu8oWVHStFd5u7LOrRgjlLD2BTqnTIqKM9K8LPeGk0oRJs_QRc5bQoiQSrxGZ7SmLZWMnaPxDjyYDDj22O7naDcpjoAtNsFhY-dhMfMQw0GeUqysyVOhK4X76H18GMIa-32OOY7G42kT5-jMaNaAh7BEv0DG3eCwLRlLeX2DXvXGZ3h7Oi_Rz69f7q-_Vbc_br5ff76tLKdqrlTXU96zWlDZcCOMkIyC4EpwC7JzxPFOUMdqJWxPbG27BhQByQA4NbblzSX6dPSddt0IzkKYk_F6SsNo0l5HM-j_lTBs9DoumnGhiDoYfDwZpPhrB3nW45AteG8CxF3WsiaE0z9JH56A27hLoSynayplTXmrCrQ6QjbFnBP0fyehRB9q1HmrS436VGP58P7f-R_xU28FuDoCuUhhDekx9hnL3-wPq5E</recordid><startdate>20020901</startdate><enddate>20020901</enddate><creator>Reiners Jr, J J</creator><creator>Caruso, J A</creator><creator>Mathieu, P</creator><creator>Chelladurai, B</creator><creator>Yin, X-M</creator><creator>Kessel, D</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020901</creationdate><title>Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves bid cleavage</title><author>Reiners Jr, J J ; Caruso, J A ; Mathieu, P ; Chelladurai, B ; Yin, X-M ; Kessel, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c519t-9bf15f4261735a6a6741e65965ce7bd0d5b61d4296cf0c2cb3e90e74ee51ac853</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Apoptosis - drug effects</topic><topic>Apoptosis - physiology</topic><topic>BH3 Interacting Domain Death Agonist Protein</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Carrier Proteins - drug effects</topic><topic>Carrier Proteins - metabolism</topic><topic>Caspase 8</topic><topic>Caspase 9</topic><topic>Caspases - drug effects</topic><topic>Caspases - metabolism</topic><topic>Cathepsin D - drug effects</topic><topic>Cathepsin D - metabolism</topic><topic>Cell Biology</topic><topic>Cell Cycle Analysis</topic><topic>Cell death</topic><topic>Cell Extracts - pharmacology</topic><topic>Cytochrome</topic><topic>Cytochrome c Group - drug effects</topic><topic>Cytochrome c Group - metabolism</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Enzyme Precursors - drug effects</topic><topic>Enzyme Precursors - metabolism</topic><topic>Life Sciences</topic><topic>Lysosomes - drug effects</topic><topic>Lysosomes - enzymology</topic><topic>Lysosomes - ultrastructure</topic><topic>Medicine</topic><topic>Mice</topic><topic>Mitochondria - drug effects</topic><topic>Mitochondria - enzymology</topic><topic>Mitochondria - ultrastructure</topic><topic>Neoplasms - enzymology</topic><topic>Neoplasms - physiopathology</topic><topic>Neoplasms - therapy</topic><topic>original-paper</topic><topic>Photochemotherapy</topic><topic>Photodynamic therapy</topic><topic>Porphyrins - pharmacology</topic><topic>Porphyrins - radiation effects</topic><topic>Stem Cells</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reiners Jr, J J</creatorcontrib><creatorcontrib>Caruso, J A</creatorcontrib><creatorcontrib>Mathieu, P</creatorcontrib><creatorcontrib>Chelladurai, B</creatorcontrib><creatorcontrib>Yin, X-M</creatorcontrib><creatorcontrib>Kessel, D</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell death and differentiation</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reiners Jr, J J</au><au>Caruso, J A</au><au>Mathieu, P</au><au>Chelladurai, B</au><au>Yin, X-M</au><au>Kessel, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves bid cleavage</atitle><jtitle>Cell death and differentiation</jtitle><stitle>Cell Death Differ</stitle><addtitle>Cell Death Differ</addtitle><date>2002-09-01</date><risdate>2002</risdate><volume>9</volume><issue>9</issue><spage>934</spage><epage>944</epage><pages>934-944</pages><issn>1350-9047</issn><eissn>1476-5403</eissn><abstract>Photodynamic therapy (PDT) protocols employing lysosomal sensitizers induce apoptosis via a mechanism that causes cytochrome
c
release prior to loss of mitochondrial membrane potential (ΔΨ
m
). The current study was designed to determine how lysosomal photodamage initiates mitochondrial-mediated apoptosis in murine hepatoma 1c1c7 cells. Fluorescence microscopy demonstrated that the photosensitizer N-aspartyl chlorin e6 (NPe6) localized to the lysosomes. Irradiation of cultures preloaded with NPe6 induced the rapid destruction of lysosomes, and subsequent cleavage/activation of Bid, pro-caspases-9 and -3. Pro-caspase-8 was not activated. Release of cytochrome
c
occurred at about the time of Bid cleavage and preceded the loss of ΔΨ
m
. Extracts of purified lysosomes catalyzed the
in vitro
cleavage of cytosolic Bid, but not pro-caspase-3 activation. Pharmacological inhibition of cathepsin B, L and D activities did not suppress Bid cleavage or pro-caspases-9 and -3 activation. These studies demonstrate that photodamaged lysosomes trigger the mitochondrial apoptotic pathway by releasing proteases that activate Bid.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>12181744</pmid><doi>10.1038/sj.cdd.4401048</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1350-9047 |
ispartof | Cell death and differentiation, 2002-09, Vol.9 (9), p.934-944 |
issn | 1350-9047 1476-5403 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4569095 |
source | MEDLINE; SpringerLink Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
subjects | Animals Apoptosis Apoptosis - drug effects Apoptosis - physiology BH3 Interacting Domain Death Agonist Protein Biochemistry Biomedical and Life Sciences Carrier Proteins - drug effects Carrier Proteins - metabolism Caspase 8 Caspase 9 Caspases - drug effects Caspases - metabolism Cathepsin D - drug effects Cathepsin D - metabolism Cell Biology Cell Cycle Analysis Cell death Cell Extracts - pharmacology Cytochrome Cytochrome c Group - drug effects Cytochrome c Group - metabolism Enzyme Inhibitors - pharmacology Enzyme Precursors - drug effects Enzyme Precursors - metabolism Life Sciences Lysosomes - drug effects Lysosomes - enzymology Lysosomes - ultrastructure Medicine Mice Mitochondria - drug effects Mitochondria - enzymology Mitochondria - ultrastructure Neoplasms - enzymology Neoplasms - physiopathology Neoplasms - therapy original-paper Photochemotherapy Photodynamic therapy Porphyrins - pharmacology Porphyrins - radiation effects Stem Cells Tumor Cells, Cultured |
title | Release of cytochrome c and activation of pro-caspase-9 following lysosomal photodamage involves bid cleavage |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-19T12%3A07%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Release%20of%20cytochrome%20c%20and%20activation%20of%20pro-caspase-9%20following%20lysosomal%20photodamage%20involves%20bid%20cleavage&rft.jtitle=Cell%20death%20and%20differentiation&rft.au=Reiners%20Jr,%20J%20J&rft.date=2002-09-01&rft.volume=9&rft.issue=9&rft.spage=934&rft.epage=944&rft.pages=934-944&rft.issn=1350-9047&rft.eissn=1476-5403&rft_id=info:doi/10.1038/sj.cdd.4401048&rft_dat=%3Cproquest_pubme%3E998134081%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=217721589&rft_id=info:pmid/12181744&rfr_iscdi=true |