Source:http://linkedlifedata.com/resource/pubmed/id/21753146
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2011-8-3
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pubmed:abstractText |
Galectin (Gal) family members are a type of soluble lectin, and they play important roles in immunomodulation. Their redundant roles have been proposed. We previously found that Gal-1 promotes the formation of Ab-secreting plasma cells, but B cells from Gal-1-deficient and control animals produce comparable amounts of Abs. In the current study, we used synthetic sulfomodified N-acetyllactosamine (LacNAc) analogs and short hairpin RNAs for Gal-8 to demonstrate a redundancy in the effects of Gal-1 and Gal-8 on plasma cell formation. Gal-1 and Gal-8 were both expressed during plasma cell differentiation, and both Gals promoted the formation of plasma cells. Gal-1 and Gal-8 bound better to mature B cells than to plasma cells, and the expression of glycosyltransferase enzymes changed during differentiation, with a decrease in mannosyl (?-1,6-)-glycoprotein ?-1,6-N-acetyl-glucosaminyltransferase and N-acetylglucosaminyltransferase-1 mRNAs in plasma cells. Synthetic sulfomodified Gal?1-3GlcNAc disaccharides (type 1 LacNAcs) selectively prevented Gal-8 binding, leading to a blockade of Ab production in Gal-1-deficient B cells. Furthermore, synthetic type 1 LacNAcs that were able to block the binding of both Gals greatly reduced the effect of exogenously added recombinant Gal-1 and Gal-8 on promoting Ab production. These results reveal a novel role for Gal-8 in collaboration with Gal-1 in plasma cell formation, and suggest the possibility of using distinct LacNAc ligands to modulate the function of Gals.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Sugars,
http://linkedlifedata.com/resource/pubmed/chemical/Galectin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Galectins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetyllactosamine,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetyllactosaminide...,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-1,6-mannosyl-glycoprotein...,
http://linkedlifedata.com/resource/pubmed/chemical/galectin-8, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1550-6606
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
187
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1643-52
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pubmed:meshHeading |
pubmed-meshheading:21753146-Amino Sugars,
pubmed-meshheading:21753146-Animals,
pubmed-meshheading:21753146-Antibody Formation,
pubmed-meshheading:21753146-Galectin 1,
pubmed-meshheading:21753146-Galectins,
pubmed-meshheading:21753146-Gene Expression Regulation,
pubmed-meshheading:21753146-Mice,
pubmed-meshheading:21753146-Mice, Knockout,
pubmed-meshheading:21753146-N-Acetylglucosaminyltransferases,
pubmed-meshheading:21753146-Plasma Cells
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pubmed:year |
2011
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pubmed:articleTitle |
Galectin-1 and galectin-8 have redundant roles in promoting plasma cell formation.
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pubmed:affiliation |
Institute and Department of Microbiology and Immunology, National Yang-Ming University, Taipei 112, Taiwan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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