| pubmed-article:6976838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6976838 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:6976838 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:6976838 | lifeskim:mentions | umls-concept:C0013936 | lld:lifeskim |
| pubmed-article:6976838 | lifeskim:mentions | umls-concept:C0007582 | lld:lifeskim |
| pubmed-article:6976838 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:6976838 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
| pubmed-article:6976838 | pubmed:issue | 3 Pt 1 | lld:pubmed |
| pubmed-article:6976838 | pubmed:dateCreated | 1982-4-12 | lld:pubmed |
| pubmed-article:6976838 | pubmed:abstractText | Compaction, a process of cell-cell adhesion between mouse blastomeres or between embryonal carcinoma (EC) cells requires calcium ions. A decompaction effect similar to that observed in the absence of Ca2+ is triggered by Fab fragments of rabbit anti-EC IgG. This effect occurs through the recognition of a specific cell-surface glycoprotein named uvomorulin. An 84,000 dalton fragment of uvomorulin (UMt) has been previously extracted by trypsin from EC cell membranes and purified. WE present evidence that effects of Ca2+ on compaction are transmitted through conformational changes in uvomorulin. First, Ca2+ protects UMt from further proteolysis by trypsin. Mn2+ and Sr2+ have similar effects, whereas this protection is reversed by La3+. Second, UMt can bind the monoclonal antibody De1 only in the presence of Ca2+ (half-binding at 10(-5) M Ca2+). This antigenic exposure also takes place in the presence of Mn2+ or Sr2+ and is reversed by La3+. Third, metal ions (Ca2+, Mn2+, Sr2+) that promote trypsin resistance and recognition by DE1 are found to trigger the compaction of morulae and EC cells. Metal ions (La3+) that reduce trypsin resistance and affinity for DE1 result in decompaction. | lld:pubmed |
| pubmed-article:6976838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6976838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6976838 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6976838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6976838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6976838 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:6976838 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:6976838 | pubmed:author | pubmed-author:JacobFF | lld:pubmed |
| pubmed-article:6976838 | pubmed:author | pubmed-author:HyafilFF | lld:pubmed |
| pubmed-article:6976838 | pubmed:author | pubmed-author:BabinetCC | lld:pubmed |
| pubmed-article:6976838 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6976838 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:6976838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6976838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6976838 | pubmed:pagination | 447-54 | lld:pubmed |
| pubmed-article:6976838 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:6976838 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:6976838 | pubmed:articleTitle | Cell-cell interactions in early embryogenesis: a molecular approach to the role of calcium. | lld:pubmed |
| pubmed-article:6976838 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6976838 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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