Source:http://linkedlifedata.com/resource/pubmed/id/11309369
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
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| pubmed:dateCreated |
2001-4-19
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| pubmed:abstractText |
Anhidrotic ectodermal dysplasia (EDA) is an X-linked disorder characterized by abnormal development of ectoderm and its appendices. The EDA gene encodes different isoforms of ectodysplasin, a transmembrane protein. The two longest isoforms, ectodysplasin-A1 and -A2, which differ by an insertion of two amino acids, are trimeric type II membrane proteins with an extracellular portion containing a short collagenous domain and a TNF ligand motif in the C-terminal region. We show that ectodysplasin is released from cells to the culture medium. Deletion constructs were used to localize the cleavage site and show that the putative recognition sequence of a furin-like enzyme is needed for the cleavage. Some EDA patients have missense mutations affecting this recognition sequence, suggesting that cleavage has biological significance in vivo. EDAR, a recently cloned member of the TNFR family and the product of the downless gene, is able to co-precipitate ectodysplasin, confirming that they form a ligand-receptor pair. In situ hybridization and immunostaining studies show that ectodysplasin and EDAR are expressed in adjacent or partially overlapping layers in the developing human skin. We conclude that as a soluble ligand, ectodysplasin is able to interact with EDAR and mediate signals needed for the development of ectodermal appendages.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/EDA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ectodysplasins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Tumor Necrosis Factor
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| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
0964-6906
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
|
| pubmed:volume |
10
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
953-62
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11309369-Animals,
pubmed-meshheading:11309369-Blotting, Western,
pubmed-meshheading:11309369-COS Cells,
pubmed-meshheading:11309369-Ectodermal Dysplasia,
pubmed-meshheading:11309369-Ectodysplasins,
pubmed-meshheading:11309369-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11309369-Gene Expression,
pubmed-meshheading:11309369-Humans,
pubmed-meshheading:11309369-Immunoenzyme Techniques,
pubmed-meshheading:11309369-Immunohistochemistry,
pubmed-meshheading:11309369-In Situ Hybridization,
pubmed-meshheading:11309369-Membrane Proteins,
pubmed-meshheading:11309369-Peptide Fragments,
pubmed-meshheading:11309369-Precipitin Tests,
pubmed-meshheading:11309369-Protein Binding,
pubmed-meshheading:11309369-Receptors, Tumor Necrosis Factor,
pubmed-meshheading:11309369-Skin,
pubmed-meshheading:11309369-Transfection
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| pubmed:year |
2001
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| pubmed:articleTitle |
Ectodysplasin is released by proteolytic shedding and binds to the EDAR protein.
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| pubmed:affiliation |
Department of Medical Genetics, Haartman Institute, Finnish Genome Center and Institute of Biotechnology, Viikki Biocenter, 00014 University of Helsinki, Helsinki, Finland.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|