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
2011 Impact Factor: 2.588
2011 SCImago Journal Rankings: 0.474
DOIhttp://dx.doi.org/10.1007/s00418-009-0568-2
ReferencesReferences in Scopus
DC Field
Value
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
2011 Impact Factor: 2.588
2011 SCImago Journal Rankings: 0.474
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
Author Affiliations
  1. Yonsei University
  2. Iwate Medical University