Gastrulation EMT Is Independent of P-Cadherin Downregulation

Persistent Link:
http://hdl.handle.net/10150/614679
Title:
Gastrulation EMT Is Independent of P-Cadherin Downregulation
Author:
Moly, Pricila K.; Cooley, James R.; Zeltzer, Sebastian L.; Yatskievych, Tatiana A.; Antin, Parker B. ( 0000-0001-9066-7412 )
Affiliation:
Univ Arizona, Dept Cellular & Mol Med
Issue Date:
2016-04-20
Publisher:
Public Library of Science
Citation:
Gastrulation EMT Is Independent of P-Cadherin Downregulation 2016, 11 (4):e0153591 PLOS ONE
Journal:
PLOS ONE
Rights:
© 2016 Moly et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Collection Information:
This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
Abstract:
Epithelial-mesenchymal transition (EMT) is an evolutionarily conserved process during which cells lose epithelial characteristics and gain a migratory phenotype. Although downregulation of epithelial cadherins by Snail and other transcriptional repressors is generally considered a prerequisite for EMT, recent studies have challenged this view. Here we investigate the relationship between E-cadherin and P-cadherin expression and localization, Snail function and EMT during gastrulation in chicken embryos. Expression analyses show that while E-cadherin transcripts are detected in the epiblast but not in the primitive streak or mesoderm, P-cadherin mRNA and protein are present in the epiblast, primitive and mesoderm. Antibodies that specifically recognize E-cadherin are not presently available. During EMT, P-cadherin relocalizes from the lateral surfaces of epithelial epiblast cells to a circumferential distribution in emerging mesodermal cells. Cells electroporated with an E-cadherin expression construct undergo EMT and migrate into the mesoderm. An examination of Snail function showed that reduction of Slug (SNAI2) protein levels using a morpholino fails to inhibit EMT, and expression of human or chicken Snail in epiblast cells fails to induce EMT. In contrast, cells expressing the Rho inhibitor peptide C3 rapidly exit the epiblast without activating Slug or the mesoderm marker N-cadherin. Together, these experiments show that epiblast cells undergo EMT while retaining P-cadherin, and raise questions about the mechanisms of EMT regulation during avian gastrulation.
ISSN:
1932-6203
DOI:
10.1371/journal.pone.0153591
Keywords:
EPITHELIAL-MESENCHYMAL TRANSITION; TRANSCRIPTION FACTOR SNAIL; EXPRESSION; GENE; CELLS; SLUG
Version:
Final published version
Sponsors:
This work was supported by NIH grant P41 HD064559 to PBA.
Additional Links:
http://dx.plos.org/10.1371/journal.pone.0153591

Full metadata record

DC FieldValue Language
dc.contributor.authorMoly, Pricila K.en
dc.contributor.authorCooley, James R.en
dc.contributor.authorZeltzer, Sebastian L.en
dc.contributor.authorYatskievych, Tatiana A.en
dc.contributor.authorAntin, Parker B.en
dc.date.accessioned2016-06-24T21:17:01Z-
dc.date.available2016-06-24T21:17:01Z-
dc.date.issued2016-04-20-
dc.identifier.citationGastrulation EMT Is Independent of P-Cadherin Downregulation 2016, 11 (4):e0153591 PLOS ONEen
dc.identifier.issn1932-6203-
dc.identifier.doi10.1371/journal.pone.0153591-
dc.identifier.urihttp://hdl.handle.net/10150/614679-
dc.description.abstractEpithelial-mesenchymal transition (EMT) is an evolutionarily conserved process during which cells lose epithelial characteristics and gain a migratory phenotype. Although downregulation of epithelial cadherins by Snail and other transcriptional repressors is generally considered a prerequisite for EMT, recent studies have challenged this view. Here we investigate the relationship between E-cadherin and P-cadherin expression and localization, Snail function and EMT during gastrulation in chicken embryos. Expression analyses show that while E-cadherin transcripts are detected in the epiblast but not in the primitive streak or mesoderm, P-cadherin mRNA and protein are present in the epiblast, primitive and mesoderm. Antibodies that specifically recognize E-cadherin are not presently available. During EMT, P-cadherin relocalizes from the lateral surfaces of epithelial epiblast cells to a circumferential distribution in emerging mesodermal cells. Cells electroporated with an E-cadherin expression construct undergo EMT and migrate into the mesoderm. An examination of Snail function showed that reduction of Slug (SNAI2) protein levels using a morpholino fails to inhibit EMT, and expression of human or chicken Snail in epiblast cells fails to induce EMT. In contrast, cells expressing the Rho inhibitor peptide C3 rapidly exit the epiblast without activating Slug or the mesoderm marker N-cadherin. Together, these experiments show that epiblast cells undergo EMT while retaining P-cadherin, and raise questions about the mechanisms of EMT regulation during avian gastrulation.en
dc.description.sponsorshipThis work was supported by NIH grant P41 HD064559 to PBA.en
dc.language.isoenen
dc.publisherPublic Library of Scienceen
dc.relation.urlhttp://dx.plos.org/10.1371/journal.pone.0153591en
dc.rights© 2016 Moly et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.subjectEPITHELIAL-MESENCHYMAL TRANSITIONen
dc.subjectTRANSCRIPTION FACTOR SNAILen
dc.subjectEXPRESSIONen
dc.subjectGENEen
dc.subjectCELLSen
dc.subjectSLUGen
dc.titleGastrulation EMT Is Independent of P-Cadherin Downregulationen
dc.typeArticleen
dc.contributor.departmentUniv Arizona, Dept Cellular & Mol Meden
dc.identifier.journalPLOS ONEen
dc.description.collectioninformationThis item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.en
dc.eprint.versionFinal published versionen
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