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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-12-17
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pubmed:abstractText |
Previously we described an embryonic cell surface glycoprotein, ESGp, associated with the t-embryonic lethal alleles of the mouse t complex. This antigen is expressed on the cell surface of both early mouse embryos and embryonal carcinoma (EC) cell lines. The antigen is localized to areas of cell-cell contact in EC lines and redistributes to the outer edges of the blastomeres during compaction, thereby indicating a potential role in embryonic cell-cell interaction. We now report that this t-complex-associated ESGp is homologous to the mouse lysosomal-associated membrane protein-1 (LAMP-1). Limited protein sequence analyses of the amino terminal and an internal peptide indicate considerable homology with the LAMP-1 protein. Biochemical parameters such as protein core size, sulfation and phosphorylation status, and resistance to proteolysis also demonstrate homology. While we detect only a single message with a mouse LAMP-1 cDNA probe via Northern blotting, Southern analyses indicate the existence of at least two homologous LAMP-1 genes. Additionally, we present evidence suggesting that ESGp/LAMP-1 serves as a substrate which may be differentially glycosylated by the activities of the gene products of the different t-lethal alleles.
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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/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Lamp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Lysosome-Associated Membrane...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
236
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
501-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9367635-Amino Acid Sequence,
pubmed-meshheading:9367635-Animals,
pubmed-meshheading:9367635-Antigens, CD,
pubmed-meshheading:9367635-Antigens, Differentiation,
pubmed-meshheading:9367635-Carcinoma, Embryonal,
pubmed-meshheading:9367635-Embryo, Mammalian,
pubmed-meshheading:9367635-Genes, Lethal,
pubmed-meshheading:9367635-Glycosylation,
pubmed-meshheading:9367635-Lysosome-Associated Membrane Glycoproteins,
pubmed-meshheading:9367635-Male,
pubmed-meshheading:9367635-Membrane Glycoproteins,
pubmed-meshheading:9367635-Mice,
pubmed-meshheading:9367635-Molecular Sequence Data,
pubmed-meshheading:9367635-Sequence Analysis,
pubmed-meshheading:9367635-Sequence Homology, Amino Acid,
pubmed-meshheading:9367635-Testis
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pubmed:year |
1997
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pubmed:articleTitle |
t-complex-associated embryonic surface antigen homologous to mLAMP-1. I. Biochemical and molecular analyses.
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pubmed:affiliation |
Department of Biological Sciences, University at Albany, New York 12222, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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