A role for E-cadherin in mouse primordial germ cell development.
In this study we show that mouse primordial germ cells and fetal germ cells at certain stages of differentiation express E-cadherin and alpha and beta catenins. Moreover, we demonstrate that the formation of germ cell aggregates that rapidly occurs when monodispersed germ cell populations are released from embryonic gonads in culture is E-cadherin mediated, developmentally regulated, and dependent on the sex of the germ cells. Immunoblotting analyses indicate that the lower ability to form aggregates of primordial germ cells in comparison to fetal germ cells is not due to gross changes in E-cadherin expression, altered association with beta catenin, or changes in beta catenin phosphorylation. Investigating possible functions of E-cadherin-mediated adhesion in primordial germ cell development, we found that E-cadherin-mediated adhesion may stimulate the motility of primordial germ cells. Moreover, treatment of primordial germ cells cultured on STO cell monolayers with an anti-E-cadherin antibody caused a significant decrease in their number and markedly reduced their ability to form colonies in vitro. The same in vitro treatment of explanted undifferentiated gonadal ridges cultured for 4 days results in decreased numbers and altered localization of the germ cell inside the gonads. Taken together these results suggest that E-cadherin plays an important role in primordial germ cell migration and homing and may act as a modulator of primordial germ cell development.
Di Carlo
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Department of Public Health and Cell Biology, University of Rome "Tor Vergata,", Rome, 00133, Italy.
De Felici
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D000818:Animals; D000911:Antibodies, Monoclonal / Q000494:pharmacology; D015820:Cadherins / Q000096:biosynthesis / Q000235:genetics / Q000276:immunology / Q000502:physiology*; D002118:Calcium / Q000494:pharmacology; D002448:Cell Adhesion; D002449:Cell Aggregation / Q000187:drug effects; D002454:Cell Differentiation; D002465:Cell Movement; D002478:Cells, Cultured; D003114:Colony-Forming Units Assay; D003571:Cytochalasin B / Q000494:pharmacology; D003598:Cytoskeletal Proteins / Q000096:biosynthesis / Q000235:genetics; D005260:Female; D018507:Gene Expression Regulation, Developmental; D005854:Germ Cells / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D006066:Gonads / Q000166:cytology / Q000196:embryology; D008297:Male; D051379:Mice; D010446:Peptide Fragments / Q000494:pharmacology; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D013696:Temperature; D015534:Trans-Activators; D014357:Trypsin / Q000494:pharmacology; D051178:alpha Catenin; D051176:beta Catenin
D000911:Antibodies, Monoclonal; C495267:CTNNB1 protein, mouse; D015820:Cadherins; C495272:Ctnna1 protein, mouse; D003598:Cytoskeletal Proteins; D010446:Peptide Fragments; D015534:Trans-Activators; D051178:alpha Catenin; D051176:beta Catenin; D003571:Cytochalasin B; D014357:Trypsin; D002118:Calcium