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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1998-5-26
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pubmed:abstractText |
Protein tyrosine phosphatase zeta (PTPzeta/RPTPbeta) is a receptor-like protein tyrosine phosphatase specifically expressed in the brain. Alternative splicing produces three isoforms of this molecule: PTPzeta-A, the full-length form of PTPzeta; PTPzeta-B, the short form of PTPzeta; and PTPzeta-S, an extracellular variant. Here, we identified all these isoforms, including PTPzeta-B, as chondroitin sulfate proteoglycans, and characterized their carbohydrate modification and expression profiles in the rat brain. The level of PTPzeta-A expression was maintained during the prenatal period and decreased rapidly after birth. PTPzeta-S was expressed in a similar manner, although the postnatal decrease was gradual. In contrast, relatively constant amounts of PTPzeta-B were observed from embryonic day 13 (E13) through adulthood. PTPzeta-A and -S were constantly expressed only as proteoglycans during development, but a substantial amount of PTPzeta-B was detected in a non-proteoglycan form at E13-15. Moreover, PTPzeta-B did not contain LeX, HNK-1 carbohydrate, or keratan sulfate, although PTPzeta-A and -S were generally modified with these carbohydrates. L cells transfected with PTPzeta-A and -B cDNAs expressed these proteins as enzymatically active chondroitin sulfate proteoglycans. The PTPzeta-A and -B in L cells showed essentially similar localizations in cell cortical structures on immunofluorescence microscopy, although immature or processed forms of PTPzeta-A were accumulated additively in intracellular patchy structures. These results show that the three isoforms of PTPzeta are differentially regulated during development, and that the extracellular deleted region in PTPzeta-B is important for determination of carbohydrate modification.
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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, CD15,
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin Sulfates,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Keratan Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Ptprg protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptprg protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Ptprz1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptprz1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor-Like Protein Tyrosine...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
123
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
458-67
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:9538229-Animals,
pubmed-meshheading:9538229-Antigens, CD15,
pubmed-meshheading:9538229-Brain,
pubmed-meshheading:9538229-Chondroitin Sulfates,
pubmed-meshheading:9538229-DNA, Complementary,
pubmed-meshheading:9538229-Gene Expression Regulation, Developmental,
pubmed-meshheading:9538229-Immunohistochemistry,
pubmed-meshheading:9538229-Isoenzymes,
pubmed-meshheading:9538229-Keratan Sulfate,
pubmed-meshheading:9538229-L Cells (Cell Line),
pubmed-meshheading:9538229-Mice,
pubmed-meshheading:9538229-Nerve Tissue Proteins,
pubmed-meshheading:9538229-Neurons,
pubmed-meshheading:9538229-Protein Tyrosine Phosphatases,
pubmed-meshheading:9538229-Proteoglycans,
pubmed-meshheading:9538229-Rats,
pubmed-meshheading:9538229-Rats, Sprague-Dawley,
pubmed-meshheading:9538229-Receptor-Like Protein Tyrosine Phosphatases, Class 5,
pubmed-meshheading:9538229-Transfection
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pubmed:year |
1998
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pubmed:articleTitle |
Characterization and developmental regulation of proteoglycan-type protein tyrosine phosphatase zeta/RPTPbeta isoforms.
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pubmed:affiliation |
Division of Molecular Neurobiology, National Institute for Basic Biology, 38 Nishigonaka, Myodaiji-cho, Okazaki 444-8585, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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