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Article: MAPK mediates Hsp25 signaling in incisor development
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TitleMAPK mediates Hsp25 signaling in incisor development
 
AuthorsLee, MJ1
Cai, J1
Kwak, SW1
Cho, SW1
Harada, H2
Jung, HS1
 
Issue Date2009
 
PublisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00418/index.htm
 
CitationHistochemistry And Cell Biology, 2009, v. 131 n. 5, p. 593-603 [How to Cite?]
DOI: http://dx.doi.org/10.1007/s00418-009-0568-2
 
AbstractRodent incisors are continuously growing teeth that include all stages of amelogenesis. Understanding amelogenesis requires investigations of the genes and their gene products control the ameloblast phenotype. One of the mechanisms related to tooth differentiation is mitogen-activated protein kinase (MAPK) signaling. The extracellular-signal regulated kinase (ERK)/mitogen-activated protein kinase kinase (MEK) cascade is associated with mechanisms that control the cell cycle and cell survival. However, the roles of cascades in incisor development remain to be determined. In this study, we investigated incisor development and growth in the mouse based on MAPK signaling. Moreover, heat-shock protein (Hsp)-25 is well known to be a useful marker of odontoblast differentiation. We used anisomycin (a protein-synthesis inhibitor that activates MAPKs) and U0126 (a MAPK inhibitor that blocks ERK1/2 phosphorylation) to examine the role of MAPKs in Hsp25 signaling in the development of the mouse incisor. We performed immunohistochemistry and in vitro culture using incisor tooth germ, and found that phospho-ERK (pERK), pMEK, and Hsp25 localized in developing incisor ameloblasts and anisomycin failed to produce incisor development. In addition, Western blotting results showed that anisomycin stimulated the phosphorylation of ERK, MEK, and Hsp25, and that some of these proteins were blocked by the U0126. These findings suggest that MAPK signals play important roles in incisor formation, differentiation, and development by mediating Hsp25 signaling. © 2009 Springer-Verlag.
 
ISSN0948-6143
2013 Impact Factor: 2.927
 
DOIhttp://dx.doi.org/10.1007/s00418-009-0568-2
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLee, MJ
 
dc.contributor.authorCai, J
 
dc.contributor.authorKwak, SW
 
dc.contributor.authorCho, SW
 
dc.contributor.authorHarada, H
 
dc.contributor.authorJung, HS
 
dc.date.accessioned2012-10-25T04:52:51Z
 
dc.date.available2012-10-25T04:52:51Z
 
dc.date.issued2009
 
dc.description.abstractRodent incisors are continuously growing teeth that include all stages of amelogenesis. Understanding amelogenesis requires investigations of the genes and their gene products control the ameloblast phenotype. One of the mechanisms related to tooth differentiation is mitogen-activated protein kinase (MAPK) signaling. The extracellular-signal regulated kinase (ERK)/mitogen-activated protein kinase kinase (MEK) cascade is associated with mechanisms that control the cell cycle and cell survival. However, the roles of cascades in incisor development remain to be determined. In this study, we investigated incisor development and growth in the mouse based on MAPK signaling. Moreover, heat-shock protein (Hsp)-25 is well known to be a useful marker of odontoblast differentiation. We used anisomycin (a protein-synthesis inhibitor that activates MAPKs) and U0126 (a MAPK inhibitor that blocks ERK1/2 phosphorylation) to examine the role of MAPKs in Hsp25 signaling in the development of the mouse incisor. We performed immunohistochemistry and in vitro culture using incisor tooth germ, and found that phospho-ERK (pERK), pMEK, and Hsp25 localized in developing incisor ameloblasts and anisomycin failed to produce incisor development. In addition, Western blotting results showed that anisomycin stimulated the phosphorylation of ERK, MEK, and Hsp25, and that some of these proteins were blocked by the U0126. These findings suggest that MAPK signals play important roles in incisor formation, differentiation, and development by mediating Hsp25 signaling. © 2009 Springer-Verlag.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationHistochemistry And Cell Biology, 2009, v. 131 n. 5, p. 593-603 [How to Cite?]
DOI: http://dx.doi.org/10.1007/s00418-009-0568-2
 
dc.identifier.citeulike4088213
 
dc.identifier.doihttp://dx.doi.org/10.1007/s00418-009-0568-2
 
dc.identifier.epage603
 
dc.identifier.issn0948-6143
2013 Impact Factor: 2.927
 
dc.identifier.issue5
 
dc.identifier.pmid19225803
 
dc.identifier.scopuseid_2-s2.0-63949085382
 
dc.identifier.spage593
 
dc.identifier.urihttp://hdl.handle.net/10722/169558
 
dc.identifier.volume131
 
dc.languageeng
 
dc.publisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00418/index.htm
 
dc.publisher.placeGermany
 
dc.relation.ispartofHistochemistry and Cell Biology
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAmeloblasts - Cytology - Drug Effects - Metabolism
 
dc.subject.meshAnimals
 
dc.subject.meshAnisomycin - Pharmacology
 
dc.subject.meshButadienes - Pharmacology
 
dc.subject.meshCell Line
 
dc.subject.meshExtracellular Signal-Regulated Map Kinases - Drug Effects - Metabolism
 
dc.subject.meshHeat-Shock Proteins - Drug Effects - Metabolism
 
dc.subject.meshIncisor - Drug Effects - Growth & Development - Metabolism
 
dc.subject.meshKi-67 Antigen - Drug Effects - Metabolism
 
dc.subject.meshMap Kinase Kinase Kinases - Drug Effects - Metabolism
 
dc.subject.meshMice
 
dc.subject.meshMice, Inbred Icr
 
dc.subject.meshNeoplasm Proteins - Drug Effects - Metabolism
 
dc.subject.meshNitriles - Pharmacology
 
dc.subject.meshOrgan Culture Techniques
 
dc.subject.meshRats
 
dc.subject.meshSignal Transduction - Drug Effects - Physiology
 
dc.titleMAPK mediates Hsp25 signaling in incisor development
 
dc.typeArticle
 
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Author Affiliations
  1. Yonsei University
  2. Iwate Medical University