Source:http://linkedlifedata.com/resource/pubmed/id/11169395
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rdf:type | |
lifeskim:mentions |
umls-concept:C0001613,
umls-concept:C0001629,
umls-concept:C0007776,
umls-concept:C0019630,
umls-concept:C0022655,
umls-concept:C0025148,
umls-concept:C0030956,
umls-concept:C0036588,
umls-concept:C0229951,
umls-concept:C1145667,
umls-concept:C1167622,
umls-concept:C1444754,
umls-concept:C1550278,
umls-concept:C1707271,
umls-concept:C1709694,
umls-concept:C1880371,
umls-concept:C2349209,
umls-concept:C2825311
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pubmed:issue |
12
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pubmed:dateCreated |
2001-1-25
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pubmed:abstractText |
Medullary thymic epithelial cells (mTEC) are able to present soluble antigens to CD4+ helper T cell lines, whereas cortical thymic epithelial cells (cTEC) are not (Mizuochi, T., et al., J. Exp. Med. 1992. 175: 1601-1605). In addition, class II heterodimers from mTEC migrated with apparently less relative molecular mass in SDS-PAGE than those from cTEC (Kasai, M., et al., Eur. J. Immunol. 1998. 28:1867-1876). To investigate the cause of the distinct migration profiles of class II heterodimers in both TEC types, class II heterodimer-associated peptides were analyzed by matrix-assisted laser desorption ionization mass spectrometry. Self peptides from cTEC were shown to vary moderately in length and to be highly diverse, including low amounts of CLIP (class II-associated invariant chain peptide) variants. On the other hand, self peptides from two mTEC consisted predominantly of two CLIP variants with exceptional C-terminal extensions. C-terminally overhanging residues of CLIP in mTEC may be responsible for the distinct migration of class II heterodimers in SDS-PAGE. Differences in migration of class II heterodimers on SDS gels was also observed in H2-DM+ vesicles isolated from both TEC. The possible contribution of self peptides bound to class II heterodimers in TEC to positive or negative selection of T cells in the thymus is discussed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-2980
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3542-51
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11169395-Amino Acid Sequence,
pubmed-meshheading:11169395-Animals,
pubmed-meshheading:11169395-Antigens, Differentiation, B-Lymphocyte,
pubmed-meshheading:11169395-Dimerization,
pubmed-meshheading:11169395-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:11169395-Epithelial Cells,
pubmed-meshheading:11169395-Histocompatibility Antigens Class II,
pubmed-meshheading:11169395-Mass Spectrometry,
pubmed-meshheading:11169395-Mice,
pubmed-meshheading:11169395-Molecular Sequence Data,
pubmed-meshheading:11169395-Rabbits,
pubmed-meshheading:11169395-Thymus Gland
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pubmed:year |
2000
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pubmed:articleTitle |
CLIP-derived self peptides bound to MHC class II molecules of medullary thymic epithelial cells differ from those of cortical thymic epithelial cells in their diversity, length, and C-terminal processing.
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pubmed:affiliation |
Department of Bacterial and Blood Products, National Institute of Infectious Diseases, Tokyo, Japan. kasai@nih.go.jp
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pubmed:publicationType |
Journal Article
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