Source:http://linkedlifedata.com/resource/pubmed/id/14570569
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2003-10-22
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pubmed:abstractText |
Cadherins are transmembrane glycoproteins that mediate calcium-dependent cell-cell adhesion. The cadherin family is large and diverse, and proteins are considered to be members of this family if they have one or more cadherin repeats in their extracellular domain. Cadherin family members are the transmembrane components of a number of cellular junctions, including adherens junctions, desmosomes, cardiac junctions, endothelial junctions, and synaptic junctions. Cadherin function is critical in normal development, and alterations in cadherin function have been implicated in tumorigenesis. The strength of cadherin interactions can be regulated by a number of proteins, including the catenins, which serve to link the cadherin to the cytoskeleton. Cadherins have been implicated in a number of signaling pathways that regulate cellular behavior, and it is becoming increasingly clear that integration of information received from cell-cell signaling, cell-matrix signaling, and growth factor signaling determines ultimate cellular phenotype and behavior.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Armadillo Domain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Catenins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/delta catenin
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pubmed:status |
MEDLINE
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pubmed:issn |
1081-0706
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
207-35
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:14570569-Animals,
pubmed-meshheading:14570569-Armadillo Domain Proteins,
pubmed-meshheading:14570569-Cadherins,
pubmed-meshheading:14570569-Catenins,
pubmed-meshheading:14570569-Cell Adhesion,
pubmed-meshheading:14570569-Cell Adhesion Molecules,
pubmed-meshheading:14570569-Cell Communication,
pubmed-meshheading:14570569-Cell Transformation, Neoplastic,
pubmed-meshheading:14570569-Cytoskeletal Proteins,
pubmed-meshheading:14570569-Extracellular Matrix,
pubmed-meshheading:14570569-Humans,
pubmed-meshheading:14570569-Intercellular Junctions,
pubmed-meshheading:14570569-Phenotype,
pubmed-meshheading:14570569-Phosphoproteins,
pubmed-meshheading:14570569-Signal Transduction
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pubmed:year |
2003
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pubmed:articleTitle |
Cadherins as modulators of cellular phenotype.
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pubmed:affiliation |
Department of Oral Biology, College of Dentistry and Eppley Cancer Center, University of Nebraska Medical Center, Omaha, Nebraska 68198-7696, USA. mwheelock@unmc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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