Source:http://linkedlifedata.com/resource/pubmed/id/10585293
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2000-1-11
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| pubmed:abstractText |
Gicerin is a cell adhesion molecule in the immunoglobulin (Ig) superfamily and is expressed abundantly during development in the nervous system. It has homophilic cell adhesion activity and also has heterophilic binding activity with NOF (neurite outgrowth factor) and mediates neurite extension. There are two isoforms of gicerin, one with a short (s-gicerin) and the other with a longer cytoplasmic domain (l-gicerin). We have reported that s-gicerin possesses stronger activities than l-gicerin during cell aggregation, in NOF-binding, and in neurite extension. In this study, we established cell lines which expressed a mutant-gicerin whose cytoplasmic domain was deleted and we compared the above three biological activities of the mutant-gicerin with those of s- and l-gicerin. We found that the mutant-gicerin retained all these activities, but the activities were weaker than those of s-gicerin and almost the same as those of l-gicerin. We concluded that the cytoplasmic domain of gicerin is not essential for optimal adhesive activities of gicerin, but might be involved in the regulation of its activities.
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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/Antigens, CD146,
http://linkedlifedata.com/resource/pubmed/chemical/Avian Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/gicerin protein, Gallus gallus
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| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
0014-4827
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 1999 Academic Press.
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| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
253
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
697-703
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10585293-Amino Acid Sequence,
pubmed-meshheading:10585293-Animals,
pubmed-meshheading:10585293-Antigens, CD146,
pubmed-meshheading:10585293-Avian Proteins,
pubmed-meshheading:10585293-Carrier Proteins,
pubmed-meshheading:10585293-Cell Adhesion,
pubmed-meshheading:10585293-Cell Adhesion Molecules,
pubmed-meshheading:10585293-Cell Aggregation,
pubmed-meshheading:10585293-Cell Line,
pubmed-meshheading:10585293-Chick Embryo,
pubmed-meshheading:10585293-Ciliary Body,
pubmed-meshheading:10585293-Cytoplasm,
pubmed-meshheading:10585293-Fibroblasts,
pubmed-meshheading:10585293-Genes, Immunoglobulin,
pubmed-meshheading:10585293-Molecular Sequence Data,
pubmed-meshheading:10585293-Multigene Family,
pubmed-meshheading:10585293-Mutagenesis,
pubmed-meshheading:10585293-Neurites,
pubmed-meshheading:10585293-Neurons,
pubmed-meshheading:10585293-Plasmids,
pubmed-meshheading:10585293-Protein Structure, Tertiary,
pubmed-meshheading:10585293-Transfection
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| pubmed:year |
1999
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| pubmed:articleTitle |
Cytoplasmic domain is not essential for the cell adhesion activities of gicerin, an Ig-superfamily molecule.
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| pubmed:affiliation |
Department of Pharmacology, Osaka University School of Medicine, 2-2 Yamada-oka, Suita, Osaka, 565-0871, Japan. etaira@pharma1.med.osaka-u.ac.jp
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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