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Article: A novel anti-mycobacterial function of mitogen-activated protein kinase phosphatase-1

TitleA novel anti-mycobacterial function of mitogen-activated protein kinase phosphatase-1
Authors
Issue Date2009
PublisherBioMed Central Ltd. The Journal's web site is located at http://www.biomedcentral.com/bmcimmunol/
Citation
Bmc Immunology, 2009, v. 10 How to Cite?
AbstractBackground: Mycobacterium tuberculosis (MTB) is a major cause of morbidity and mortality in the world. To combat against this pathogen, immune cells release cytokines including tumor necrosis factor-α (TNF-α), which is pivotal in the development of protective granulomas. Our previous results showed that Bacillus Calmette Guerin (BCG), a mycobacterium used as a model to investigate the immune response against MTB, stimulates the induction of TNF-α via mitogen-activated protein kinase (MAPK) in human blood monocytes. Since MAPK phosphatase-1 (MKP-1) is known to regulate MAPK activities, we examined whether MKP-1 plays a role in BCG-induced MAPK activation and cytokine expression.Results: Primary human blood monocytes were treated with BCG and assayed for MKP-1 expression. Our results demonstrated that following exposure to BCG, there was an increase in the expression of MKP-1. Additionally, the induction of MKP-1 was regulated by p38 MAPK and extracellular signal-regulated kinase 1 and 2 (ERK1/2). Surprisingly, when MKP-1 expression was blocked by its specific siRNA, there was a significant decrease in the levels of phospho-MAPK (p38 MAPK and ERK1/2) and TNF-α inducible by BCG.Conclusions: Since TNF-α is pivotal in granuloma formation, the results indicated an unexpected positive function of MKP-1 against mycobacterial infection as opposed to its usual phosphatase activity. © 2009 Cheung et al; licensee BioMed Central Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/80139
ISSN
2015 Impact Factor: 2.161
2015 SCImago Journal Rankings: 1.087
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCheung, BKWen_HK
dc.contributor.authorYim, HCHen_HK
dc.contributor.authorLee, NCMen_HK
dc.contributor.authorLau, ASYen_HK
dc.date.accessioned2010-09-06T08:02:51Z-
dc.date.available2010-09-06T08:02:51Z-
dc.date.issued2009en_HK
dc.identifier.citationBmc Immunology, 2009, v. 10en_HK
dc.identifier.issn1471-2172en_HK
dc.identifier.urihttp://hdl.handle.net/10722/80139-
dc.description.abstractBackground: Mycobacterium tuberculosis (MTB) is a major cause of morbidity and mortality in the world. To combat against this pathogen, immune cells release cytokines including tumor necrosis factor-α (TNF-α), which is pivotal in the development of protective granulomas. Our previous results showed that Bacillus Calmette Guerin (BCG), a mycobacterium used as a model to investigate the immune response against MTB, stimulates the induction of TNF-α via mitogen-activated protein kinase (MAPK) in human blood monocytes. Since MAPK phosphatase-1 (MKP-1) is known to regulate MAPK activities, we examined whether MKP-1 plays a role in BCG-induced MAPK activation and cytokine expression.Results: Primary human blood monocytes were treated with BCG and assayed for MKP-1 expression. Our results demonstrated that following exposure to BCG, there was an increase in the expression of MKP-1. Additionally, the induction of MKP-1 was regulated by p38 MAPK and extracellular signal-regulated kinase 1 and 2 (ERK1/2). Surprisingly, when MKP-1 expression was blocked by its specific siRNA, there was a significant decrease in the levels of phospho-MAPK (p38 MAPK and ERK1/2) and TNF-α inducible by BCG.Conclusions: Since TNF-α is pivotal in granuloma formation, the results indicated an unexpected positive function of MKP-1 against mycobacterial infection as opposed to its usual phosphatase activity. © 2009 Cheung et al; licensee BioMed Central Ltd.en_HK
dc.languageengen_HK
dc.publisherBioMed Central Ltd. The Journal's web site is located at http://www.biomedcentral.com/bmcimmunol/en_HK
dc.relation.ispartofBMC Immunologyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong Licenseen_HK
dc.subject.meshAnti-Bacterial Agents - pharmacology-
dc.subject.meshCysteine - analogs and derivatives - pharmacology-
dc.subject.meshDual Specificity Phosphatase 1 - physiology-
dc.subject.meshLipopolysaccharides - pharmacology-
dc.subject.meshMycobacterium bovis - physiology-
dc.titleA novel anti-mycobacterial function of mitogen-activated protein kinase phosphatase-1en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1471-2172&volume=64&spage=1&epage=10&date=2009&atitle=A+novel+anti-mycobacterial+function+of+mitogen-activated+protein+kinase+phosphatase-1en_HK
dc.identifier.emailLau, ASY:asylau@hku.hken_HK
dc.identifier.authorityLau, ASY=rp00474en_HK
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1186/1471-2172-10-64en_HK
dc.identifier.pmid20017901-
dc.identifier.pmcidPMC2804704-
dc.identifier.scopuseid_2-s2.0-74549115190en_HK
dc.identifier.hkuros168937en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-74549115190&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume10en_HK
dc.identifier.isiWOS:000273589500001-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridCheung, BKW=9634391200en_HK
dc.identifier.scopusauthoridYim, HCH=15752404600en_HK
dc.identifier.scopusauthoridLee, NCM=35317609700en_HK
dc.identifier.scopusauthoridLau, ASY=7202626202en_HK
dc.identifier.citeulike6430615-

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