File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Induction of matrix metalloproteinases by Epstein-Barr virus latent membrane protein 1 isolated from nasopharyngeal carcinoma

TitleInduction of matrix metalloproteinases by Epstein-Barr virus latent membrane protein 1 isolated from nasopharyngeal carcinoma
Authors
KeywordsLatent membrane protein
Matrix metalloproteinase
Nasopharyngeal carcinoma
Issue Date2007
PublisherElsevier France, Editions Scientifiques et Medicales. The Journal's web site is located at http://www.elsevier.com/locate/biopha
Citation
Biomedicine And Pharmacotherapy, 2007, v. 61 n. 9 SPEC. ISS., p. 520-526 How to Cite?
AbstractEpstein-Barr virus latent infection is associated with human malignancies including Burkitt's lymphoma, gastric carcinoma and the highly invasive nasopharyngeal carcinoma (NPC). Increased expression of EBV latent membrane protein 1, LMP1, is correlated with tumor progression and metastasis in NPC. LMP1 induces cellular proteins including cytokines and matrix metalloproteinases (e.g., MMP1, MMP2 and MMP9). MMPs are endopeptidases involved in the degradation of extracellular matrix proteins; and their upregulation in cancer implicates their potential role in tumor metastasis. In light of the role of LMP1 in cytokine dysregulation and the fact that MMPs are regulated by cytokines, we examined whether LMP1 promotes NPC metastasis via the induction of MMPs. To delineate the oncogenic role of LMP1 in NPC, we first investigated the induction of MMP1, MMP2, MMP3 and MMP9 in LMP1-positive NPC tumor samples (n = 15) by quantitative RT-PCR. We showed a significant induction of MMP1 and MMP3 transcripts in the EBV LMP1-positive NPC tissues, compared with biopsies obtained from the adjacent non-tumor tissues. To investigate the role of LMP1 in MMP expression in NPC, we cloned the LMP1 gene from NPC samples and transiently expressed it in MRC5 cells (human lung fibroblasts). Following transfection, a time-dependent elevation of endogenous MMP3 expression was found in the LMP1-transfectants by quantitative RT-PCR and Western analysis. Taken together, we observed that MMP3 is upregulated in LMP1-positive NPC tumors and LMP1-expression in fibroblasts is associated with MMP3 and cytokine expression. Our results suggest that LMP1 may contribute to invasiveness of NPC cells via the expression of MMP3 in fibroblasts. © 2007 Elsevier Masson SAS. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/79996
ISSN
2015 Impact Factor: 2.326
2015 SCImago Journal Rankings: 0.787
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLee, DCWen_HK
dc.contributor.authorChua, DTTen_HK
dc.contributor.authorWei, WIen_HK
dc.contributor.authorSham, JSTen_HK
dc.contributor.authorLau, ASYen_HK
dc.date.accessioned2010-09-06T08:01:10Z-
dc.date.available2010-09-06T08:01:10Z-
dc.date.issued2007en_HK
dc.identifier.citationBiomedicine And Pharmacotherapy, 2007, v. 61 n. 9 SPEC. ISS., p. 520-526en_HK
dc.identifier.issn0753-3322en_HK
dc.identifier.urihttp://hdl.handle.net/10722/79996-
dc.description.abstractEpstein-Barr virus latent infection is associated with human malignancies including Burkitt's lymphoma, gastric carcinoma and the highly invasive nasopharyngeal carcinoma (NPC). Increased expression of EBV latent membrane protein 1, LMP1, is correlated with tumor progression and metastasis in NPC. LMP1 induces cellular proteins including cytokines and matrix metalloproteinases (e.g., MMP1, MMP2 and MMP9). MMPs are endopeptidases involved in the degradation of extracellular matrix proteins; and their upregulation in cancer implicates their potential role in tumor metastasis. In light of the role of LMP1 in cytokine dysregulation and the fact that MMPs are regulated by cytokines, we examined whether LMP1 promotes NPC metastasis via the induction of MMPs. To delineate the oncogenic role of LMP1 in NPC, we first investigated the induction of MMP1, MMP2, MMP3 and MMP9 in LMP1-positive NPC tumor samples (n = 15) by quantitative RT-PCR. We showed a significant induction of MMP1 and MMP3 transcripts in the EBV LMP1-positive NPC tissues, compared with biopsies obtained from the adjacent non-tumor tissues. To investigate the role of LMP1 in MMP expression in NPC, we cloned the LMP1 gene from NPC samples and transiently expressed it in MRC5 cells (human lung fibroblasts). Following transfection, a time-dependent elevation of endogenous MMP3 expression was found in the LMP1-transfectants by quantitative RT-PCR and Western analysis. Taken together, we observed that MMP3 is upregulated in LMP1-positive NPC tumors and LMP1-expression in fibroblasts is associated with MMP3 and cytokine expression. Our results suggest that LMP1 may contribute to invasiveness of NPC cells via the expression of MMP3 in fibroblasts. © 2007 Elsevier Masson SAS. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier France, Editions Scientifiques et Medicales. The Journal's web site is located at http://www.elsevier.com/locate/biophaen_HK
dc.relation.ispartofBiomedicine and Pharmacotherapyen_HK
dc.rightsBiomedicine & Pharmacotherapy. Copyright © Elsevier France, Editions Scientifiques et Medicales.en_HK
dc.subjectLatent membrane proteinen_HK
dc.subjectMatrix metalloproteinaseen_HK
dc.subjectNasopharyngeal carcinomaen_HK
dc.titleInduction of matrix metalloproteinases by Epstein-Barr virus latent membrane protein 1 isolated from nasopharyngeal carcinomaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0753-3322&volume=61&spage=520&epage=526&date=2007&atitle=Induction+of+matrix+metalloproteinases+by+Epstein-Barr+virus+latent+membrane+protein+1+isolated+from+Nasopharyngeal+carcinomaen_HK
dc.identifier.emailChua, DTT: dttchua@hkucc.hku.hken_HK
dc.identifier.emailWei, WI: hrmswwi@hku.hken_HK
dc.identifier.emailLau, ASY: asylau@hku.hken_HK
dc.identifier.authorityChua, DTT=rp00415en_HK
dc.identifier.authorityWei, WI=rp00323en_HK
dc.identifier.authorityLau, ASY=rp00474en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.biopha.2007.08.007en_HK
dc.identifier.pmid17913445-
dc.identifier.scopuseid_2-s2.0-35348913957en_HK
dc.identifier.hkuros138664en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-35348913957&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume61en_HK
dc.identifier.issue9 SPEC. ISS.en_HK
dc.identifier.spage520en_HK
dc.identifier.epage526en_HK
dc.identifier.isiWOS:000251067600002-
dc.publisher.placeFranceen_HK
dc.identifier.scopusauthoridLee, DCW=15751156000en_HK
dc.identifier.scopusauthoridChua, DTT=7006773480en_HK
dc.identifier.scopusauthoridWei, WI=7403321552en_HK
dc.identifier.scopusauthoridSham, JST=24472255400en_HK
dc.identifier.scopusauthoridLau, ASY=7202626202en_HK
dc.identifier.citeulike5938583-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats