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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2-3
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pubmed:dateCreated |
2001-6-14
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pubmed:abstractText |
Mutations in the PKD1 gene are responsible for 85% of cases of autosomal dominant polycystic kidney disease (ADPKD). This gene encodes a large membrane associated glycoprotein, polycystin-1, which is predicted to contain a number of extracellular protein motifs, including a C-type lectin domain between amino acids 403--532. We have cloned and expressed the PKD1 C-type lectin domain, and have demonstrated that it binds carbohydrate matrices in vitro, and that Ca(2+) is required for this interaction. This domain also binds to collagens type I, II and IV in vitro. This binding is greatly enhanced in the presence of Ca(2+) and can be inhibited by soluble carbohydrates such as 2-deoxyglucose and dextran. These results suggest that polycystin-1 may be involved in protein-carbohydrate interactions in vivo. The data presented indicate that there may a direct interaction between the PKD1 gene product and an ubiquitous extracellular matrix (ECM) protein.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/TRPP Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/polycystic kidney disease 1 protein
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
1536
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
161-76
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11406351-Amino Acid Sequence,
pubmed-meshheading:11406351-Calcium,
pubmed-meshheading:11406351-Carbohydrate Metabolism,
pubmed-meshheading:11406351-Carbohydrate Sequence,
pubmed-meshheading:11406351-Carbohydrates,
pubmed-meshheading:11406351-Cations, Divalent,
pubmed-meshheading:11406351-Cell Line,
pubmed-meshheading:11406351-Collagen,
pubmed-meshheading:11406351-Extracellular Matrix Proteins,
pubmed-meshheading:11406351-Humans,
pubmed-meshheading:11406351-Lectins,
pubmed-meshheading:11406351-Lectins, C-Type,
pubmed-meshheading:11406351-Molecular Sequence Data,
pubmed-meshheading:11406351-Proteins,
pubmed-meshheading:11406351-Recombinant Fusion Proteins,
pubmed-meshheading:11406351-Sequence Alignment,
pubmed-meshheading:11406351-Signal Transduction,
pubmed-meshheading:11406351-TRPP Cation Channels
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pubmed:year |
2001
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pubmed:articleTitle |
The polycystin-1 C-type lectin domain binds carbohydrate in a calcium-dependent manner, and interacts with extracellular matrix proteins in vitro.
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pubmed:affiliation |
Division of Life Sciences, King's College London, 150 Stamford Street, London SE1 9NN, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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