|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1994-8-12
|
|
pubmed:abstractText |
Treatment of Xenopus animal pole tissue with activin results in the induction of mesodermal cell types and a dramatic elongation of the tissue. The morphogenetic movements involved in the elongation appear similar to those in normal gastrulation, which is driven by cell rearrangement and cell intercalations. We have used this system to explore the potential regulation of cell-cell adhesion and cadherin function during morphogenesis. Quantitative blastomere aggregation assays revealed that activin induction reduced the calcium-dependent adhesion between blastomeres. Activin-induced blastomeres formed smaller aggregates, and a greater proportion of the population remained as single cells compared to uninduced blastomeres. The aggregation was mediated by C-cadherin because C-cadherin was present in the blastomeres during the aggregation assay, and monoclonal antibodies against C-cadherin inhibited the calcium-dependent aggregation of blastomeres. E-cadherin was not detectable until after the completion of the assay and, therefore, does not explain the adhesive differences between induced and uninduced blastomeres. L cells stably expressing C-cadherin (LC cells) were used to demonstrate that C-cadherin activity was specifically altered after activin induction. Blastomeres induced with activin bound fewer LC cells than uninduced blastomers. L cells not expressing C-cadherin did not adhere to blastomeres. The changes in C-cadherin-mediated adhesion occurred without detectable changes in the steady-state levels of C-cadherin or the amount of C-cadherin present on the surface of the cell. Immunoprecipitation of C-cadherin and its associated catenins revealed that the ratio of C-cadherin and the catenins was not altered by activin induction. These results demonstrate that activin decreases the adhesive function of existing C-cadherin molecules on the surface of blastomeres and suggest that decreased cadherin mediated cell-cell adhesion is associated with increased morphogenetic movement.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1310256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1419055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1423628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1581959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1639852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1649199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1811947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1840622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1879345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1893866,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1918163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-1999432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-2007622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-2015791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-2070412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-2211831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-2324197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-2335564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-2351067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-2472408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-2661563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-3058163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-3281256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-3315781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-3416359,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-3515198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-3817290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-6976838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-7600966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-8335696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-8338661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-8387530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-8408227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8034750-8425900
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Activins,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Catna1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Catnb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inhibins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/alpha Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/beta-catenin protein, Xenopus
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
0021-9525
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
126
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
519-27
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:8034750-Activins,
pubmed-meshheading:8034750-Animals,
pubmed-meshheading:8034750-Antibodies, Monoclonal,
pubmed-meshheading:8034750-Biological Assay,
pubmed-meshheading:8034750-Blastomeres,
pubmed-meshheading:8034750-Cadherins,
pubmed-meshheading:8034750-Calcium,
pubmed-meshheading:8034750-Cell Adhesion,
pubmed-meshheading:8034750-Cell Differentiation,
pubmed-meshheading:8034750-Cell Separation,
pubmed-meshheading:8034750-Cytoskeletal Proteins,
pubmed-meshheading:8034750-Ectoderm,
pubmed-meshheading:8034750-Inhibins,
pubmed-meshheading:8034750-L Cells (Cell Line),
pubmed-meshheading:8034750-Mice,
pubmed-meshheading:8034750-Morphogenesis,
pubmed-meshheading:8034750-Recombinant Fusion Proteins,
pubmed-meshheading:8034750-Trans-Activators,
pubmed-meshheading:8034750-Xenopus,
pubmed-meshheading:8034750-Xenopus Proteins,
pubmed-meshheading:8034750-alpha Catenin,
pubmed-meshheading:8034750-beta Catenin
|
|
pubmed:year |
1994
|
|
pubmed:articleTitle |
Regulation of C-cadherin function during activin induced morphogenesis of Xenopus animal caps.
|
|
pubmed:affiliation |
Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York 10021.
|
