File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Protein kinase C inhibition induces DNA fragmentation in COLO 205 cells which is blocked by cysteine protease inhibition but not mediated through caspase-3

TitleProtein kinase C inhibition induces DNA fragmentation in COLO 205 cells which is blocked by cysteine protease inhibition but not mediated through caspase-3
Authors
Issue Date2003
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexcr
Citation
Experimental Cell Research, 2003, v. 289 n. 1, p. 1-10 How to Cite?
AbstractEnhancing apoptosis to remove abnormal cells has potential in reversing cancerous processes. Caspase-3 activation generally accompanies apoptosis and its substrates include enzymes responsible for DNA fragmentation and isozymes of protein kinase C (PKC). Recent data, however, question its obligatory role in apoptosis. We have examined whether modulation of PKC activity induces apoptosis in COLO 205 cells and the role of caspase-3. Proliferation ([ 3H]thymidine) and apoptosis (DNA fragmentation and FACS) of COLO 205 cells were measured in response to PKC activation and inhibition. Caspase-3 activity was assayed and the effects of its inhibition with Ac-DEVD-cmk, and the effect of other protease inhibitors, on apoptosis were determined. PKC activation and inhibition both reduced DNA synthesis and induced DNA fragmentation. As PKC inhibitors induced DNA fragmentation more rapidly than PKC activators and failed to block activator effects, we conclude that it is PKC down-regulation (i.e., inhibition) after activator exposure that mediates apoptosis. Increases in caspase-3 activity occurred during apoptosis but apoptosis was not blocked by caspase inhibition. By contrast, the cysteine protease inhibitor, E-64d, blocked apoptosis. Cysteine proteases not of the caspase family may either act more closely to the apoptotic process than caspases or lie on an alternative, more active pathway. © 2003 Elsevier Science (USA). All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/76319
ISSN
2015 Impact Factor: 3.378
2015 SCImago Journal Rankings: 1.900
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLewis, AEen_HK
dc.contributor.authorWong, BCYen_HK
dc.contributor.authorLangman, MJSen_HK
dc.contributor.authorEggo, MCen_HK
dc.date.accessioned2010-09-06T07:19:58Z-
dc.date.available2010-09-06T07:19:58Z-
dc.date.issued2003en_HK
dc.identifier.citationExperimental Cell Research, 2003, v. 289 n. 1, p. 1-10en_HK
dc.identifier.issn0014-4827en_HK
dc.identifier.urihttp://hdl.handle.net/10722/76319-
dc.description.abstractEnhancing apoptosis to remove abnormal cells has potential in reversing cancerous processes. Caspase-3 activation generally accompanies apoptosis and its substrates include enzymes responsible for DNA fragmentation and isozymes of protein kinase C (PKC). Recent data, however, question its obligatory role in apoptosis. We have examined whether modulation of PKC activity induces apoptosis in COLO 205 cells and the role of caspase-3. Proliferation ([ 3H]thymidine) and apoptosis (DNA fragmentation and FACS) of COLO 205 cells were measured in response to PKC activation and inhibition. Caspase-3 activity was assayed and the effects of its inhibition with Ac-DEVD-cmk, and the effect of other protease inhibitors, on apoptosis were determined. PKC activation and inhibition both reduced DNA synthesis and induced DNA fragmentation. As PKC inhibitors induced DNA fragmentation more rapidly than PKC activators and failed to block activator effects, we conclude that it is PKC down-regulation (i.e., inhibition) after activator exposure that mediates apoptosis. Increases in caspase-3 activity occurred during apoptosis but apoptosis was not blocked by caspase inhibition. By contrast, the cysteine protease inhibitor, E-64d, blocked apoptosis. Cysteine proteases not of the caspase family may either act more closely to the apoptotic process than caspases or lie on an alternative, more active pathway. © 2003 Elsevier Science (USA). All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexcren_HK
dc.relation.ispartofExperimental Cell Researchen_HK
dc.subject.meshAgeden_HK
dc.subject.meshAlkaloidsen_HK
dc.subject.meshAmino Acid Chloromethyl Ketones - pharmacologyen_HK
dc.subject.meshAprotinin - pharmacologyen_HK
dc.subject.meshBenzophenanthridinesen_HK
dc.subject.meshBenzyl Compounds - pharmacologyen_HK
dc.subject.meshCaspase 3en_HK
dc.subject.meshCaspases - genetics - metabolismen_HK
dc.subject.meshCell Division - drug effects - geneticsen_HK
dc.subject.meshCell Transformation, Neoplastic - genetics - metabolismen_HK
dc.subject.meshColonic Neoplasms - drug therapy - enzymology - geneticsen_HK
dc.subject.meshCysteine Endopeptidases - drug effects - metabolismen_HK
dc.subject.meshCysteine Proteinase Inhibitors - pharmacologyen_HK
dc.subject.meshDNA - biosynthesisen_HK
dc.subject.meshDNA Fragmentation - drug effects - geneticsen_HK
dc.subject.meshDipeptides - pharmacologyen_HK
dc.subject.meshDown-Regulation - drug effects - physiologyen_HK
dc.subject.meshHumansen_HK
dc.subject.meshHydrocarbons, Fluorinated - pharmacologyen_HK
dc.subject.meshLeucine - analogs & derivatives - pharmacologyen_HK
dc.subject.meshLeupeptins - pharmacologyen_HK
dc.subject.meshMaleen_HK
dc.subject.meshPepstatins - pharmacologyen_HK
dc.subject.meshPhenanthridines - pharmacologyen_HK
dc.subject.meshProtein Kinase C - antagonists & inhibitors - metabolismen_HK
dc.subject.meshPyridines - pharmacologyen_HK
dc.subject.meshTumor Cells, Cultureden_HK
dc.titleProtein kinase C inhibition induces DNA fragmentation in COLO 205 cells which is blocked by cysteine protease inhibition but not mediated through caspase-3en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-4827&volume=289&issue=1&spage=1&epage=10&date=2003&atitle=Protein+kinase+C+inhibition+induces+DNA+fragmentation+in+COLO+205+cells+which+is+blocked+by+cysteine+protease+inhibition+but+not+mediated+through+caspase-3en_HK
dc.identifier.emailWong, BCY:bcywong@hku.hken_HK
dc.identifier.authorityWong, BCY=rp00429en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0014-4827(03)00219-2en_HK
dc.identifier.pmid12941599en_HK
dc.identifier.scopuseid_2-s2.0-0043164778en_HK
dc.identifier.hkuros99182en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0043164778&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume289en_HK
dc.identifier.issue1en_HK
dc.identifier.spage1en_HK
dc.identifier.epage10en_HK
dc.identifier.isiWOS:000185167100001-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLewis, AE=7403488048en_HK
dc.identifier.scopusauthoridWong, BCY=7402023340en_HK
dc.identifier.scopusauthoridLangman, MJS=7102542271en_HK
dc.identifier.scopusauthoridEggo, MC=7006000548en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats