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Sökning: onr:"swepub:oai:DiVA.org:liu-15136" > Intrinsic differenc...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003819naa a2200457 4500
001oai:DiVA.org:liu-15136
003SwePub
008081017s2010 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:121244547
024a https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-151362 URI
024a https://doi.org/10.1002/hed.213172 DOI
024a http://kipublications.ki.se/Default.aspx?queryparsed=id:1212445472 URI
040 a (SwePub)liud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Nilsson, Cathrine,d 1978-u Linköpings universitet,Experimentell patologi,Hälsouniversitetet4 aut0 (Swepub:liu)catni27
2451 0a Intrinsic differences in cisplatin sensitivity of head and neck cancer celllines correlates to lysosomal pH
264 c 2009-12-22
264 1b John Wiley & Sons,c 2010
338 a print2 rdacarrier
500 a The previous status of this article was Manuscript and the working title was Radiation and cisplatin sensitivity in head and neck cancer cells with stem cell properties.
520 a Cisplatin is part of the treatment regime of head and neck squamous cell carcinomas (HNSCC). In order to predict the clinical outcome of the treatment, markers for evaluation of the intrinsic cisplatin sensitivity are inquired. In this study we characterize the lysosomal compartment and compare cisplatin sensitivity in five HNSCC lines and normal oral keratinocytes (NOKs). Cisplatin sensitivity differed 3-fold between the least and most sensitive cell lines, and the cisplatin LD50 correlated significantly to lysosomal pH, which varied from 4.3 in NOKs to 4.9 in the most resistant HNSCC line. Lysosomes are acidified by the V0V1-ATPase complex located in the lysosomal membrane. Interestingly, in cell lines exhibiting high lysosomal pH, we found decreased expression of the V0V1-ATPase B2 subunit, possibly explaining the defective acidification. In all cell lines, exposure to cisplatin caused activation of caspase-3. Cisplatin exposure was accompanied by lysosomal membrane permeabilization and inhibition of the llysosomal cathepsins B, D and L partly prevented cell death. No correlation between cisplatin sensitivity and expression of cathepsins B, D and L or secretion of their respective proforms into the culture medium was found in the cell lines studied. We conclude that lysosomal pH and expression of V0V1-ATPase subunits are possible future markers of intrinsic cisplatin sensitivity.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Cell- och molekylärbiologi0 (SwePub)301082 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Cell and Molecular Biology0 (SwePub)301082 hsv//eng
653 a apoptosis
653 a cathepsin
653 a chemotherapy resistance
653 a lysosome
653 a V0V1-ATPase
653 a Cell biology
653 a Cellbiologi
700a Roberg, Karinu Östergötlands Läns Landsting,Linköpings universitet,Oto-Rhino-Laryngologi,Hälsouniversitetet,Öronkliniken US4 aut0 (Swepub:liu)karro26
700a Grafström, Roland C.u Karolinska Institutet4 aut
700a Öllinger, Karinu Östergötlands Läns Landsting,Linköpings universitet,Experimentell patologi,Hälsouniversitetet,Klinisk patologi och klinisk genetik4 aut0 (Swepub:liu)karol56
710a Linköpings universitetb Experimentell patologi4 org
773t Head and Neckd : John Wiley & Sonsg 32:9, s. 1185-1194q 32:9<1185-1194x 1043-3074x 1097-0347
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-15136
8564 8u https://doi.org/10.1002/hed.21317
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:121244547

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