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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1988-8-30
|
| pubmed:abstractText |
The J1 glycoproteins have been shown to mediate neuron-astrocyte adhesion and appear in the nervous system as four species of Mr 160,000 (J1-160), 180,000 (J1-180), 200,000 (J1-200), and 220,000 (J1-220), respectively. Tenascin is a disulfide-linked oligomeric, extracellular matrix glycoprotein of subunit Mr 170,000, 190,000, 200,000, and 220,000, which has been proposed to promote epithelial cell proliferation. In view of the structural similarities of the molecules we have used immunohistochemical and immunochemical techniques to compare them. Immunohistochemically, polyclonal J1 and tenascin antibodies yielded identical staining patterns in non-nervous-system tissues, and staining could be completely blocked by preincubating the sera with purified tenascin. In the central nervous system all structures expressing tenascin immunoreactivity were also recognized by J1 antibodies. However, not all J1-positive structures were also tenascin-positive, indicating that J1 antibodies recognized additional epitopes not present on tenascin. Western-blot experiments performed with affinity-purified polyclonal J1 antibodies showed that J1 glycoproteins can be subdivided into two separate pairs, J1-160/180 and J1-200/220, which share a small degree of homology. Western-blot experiments and sequential immunoprecipitations on biosynthetically [35S]methionine- or 125I-radiolabeled J1 glycoproteins carried out with polyclonal J1 and tenascin antibodies demonstrated that J1-200/220 is immunochemically indistinguishable from tenascin. These observations suggest that one set of extracellular glycoproteins is associated with processes as different as neural histogenesis and carcinogenesis of mammary glands.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Matrix Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfur Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Tenascin
|
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0301-4681
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
37
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
104-14
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2456237-Animals,
pubmed-meshheading:2456237-Astrocytes,
pubmed-meshheading:2456237-Brain Chemistry,
pubmed-meshheading:2456237-Cell Adhesion Molecules, Neuronal,
pubmed-meshheading:2456237-Cerebellum,
pubmed-meshheading:2456237-Chromatography, Affinity,
pubmed-meshheading:2456237-Cross Reactions,
pubmed-meshheading:2456237-Electrophoresis,
pubmed-meshheading:2456237-Extracellular Matrix Proteins,
pubmed-meshheading:2456237-Fluorescent Antibody Technique,
pubmed-meshheading:2456237-Immunologic Techniques,
pubmed-meshheading:2456237-Iodine Radioisotopes,
pubmed-meshheading:2456237-Isotope Labeling,
pubmed-meshheading:2456237-Mice,
pubmed-meshheading:2456237-Mice, Inbred BALB C,
pubmed-meshheading:2456237-Nerve Tissue Proteins,
pubmed-meshheading:2456237-Proteins,
pubmed-meshheading:2456237-Rats,
pubmed-meshheading:2456237-Sulfur Radioisotopes,
pubmed-meshheading:2456237-Tenascin
|
| pubmed:year |
1988
|
| pubmed:articleTitle |
The high-molecular-weight J1 glycoproteins are immunochemically related to tenascin.
|
| pubmed:affiliation |
Department of Neurobiology, Heidelberg, Federal Republic of Germany.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|