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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1984-9-4
|
| pubmed:abstractText |
The N-CAMs are a group of surface glycoproteins involved in adhesive interactions of neurones. Related molecules of the mouse nervous system, identified in our laboratory, have been called BSP-2 and shown to act as ligands in adhesion of neuroblastoma cells. Results presented in this report show that they are immunochemically identical with N-CAM. A monoclonal anti-(N-CAM) antibody, that recognized a determinant accessible only after permeabilization of intact cells, was used to define the mode of association of the N-CAMs with the plasma membrane. This antibody bound a 35 000-Mr fragment in lysates of trypsin-treated neuroblastoma cells. It is concluded that the antibody reacts with a transmembrane or cytoplasmic domain of the molecules. The same antibody recognized the Mr-180 000 and Mr-140 000 proteins but not the Mr-120 000 chain, which co-purify from adult mouse brain. The latter polypeptide was detected in the cytosol and could be partially released from brain membranes by osmotic shock. Part or all of the Mr-120 000 protein may thus lack a transmembrane segment. Our conclusion that the N-CAM forms of higher Mr are transmembrane proteins was further corroborated by our finding that they contain phosphoserine residues, which can be labeled with (32P)phosphate in intact neuroblastoma cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0014-2956
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
2
|
| pubmed:volume |
142
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
57-64
|
| pubmed:dateRevised |
2007-7-23
|
| pubmed:meshHeading |
pubmed-meshheading:6745267-Animals,
pubmed-meshheading:6745267-Antibodies, Monoclonal,
pubmed-meshheading:6745267-Antigens, Neoplasm,
pubmed-meshheading:6745267-Antigens, Surface,
pubmed-meshheading:6745267-Brain,
pubmed-meshheading:6745267-Brain Chemistry,
pubmed-meshheading:6745267-Cell Adhesion,
pubmed-meshheading:6745267-Cell Adhesion Molecules,
pubmed-meshheading:6745267-Cell Line,
pubmed-meshheading:6745267-Cell Membrane,
pubmed-meshheading:6745267-Cytoplasm,
pubmed-meshheading:6745267-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6745267-Membrane Proteins,
pubmed-meshheading:6745267-Mice,
pubmed-meshheading:6745267-Molecular Weight,
pubmed-meshheading:6745267-Neuroblastoma,
pubmed-meshheading:6745267-Neurons,
pubmed-meshheading:6745267-Phosphoserine,
pubmed-meshheading:6745267-Precipitin Tests,
pubmed-meshheading:6745267-Rats
|
| pubmed:year |
1984
|
| pubmed:articleTitle |
Studies on the transmembrane disposition of the neural cell adhesion molecule N-CAM. A monoclonal antibody recognizing a cytoplasmic domain and evidence for the presence of phosphoserine residues.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|