Document Detail

Role of N-acetyl-D-galactosamine residue on B151K12-derived T cell-replacing factor (B151-TRF) molecule in B cell-receptor binding and -stimulating activity.
MedLine Citation:
PMID:  3897376     Owner:  NLM     Status:  MEDLINE    
The role of sugar moiety on T cell-replacing factor molecule derived from a monoclonal T cell hybridoma B151K12 (B151-TRF) was analyzed with respect to the interaction with receptor on B cells. The induction of B cell differentiation into Ig-secreting cells by B151-TRF was specifically inhibited by addition of N-acetyl-D-galactosamine (GalNAc) to culture. Such inhibition appeared to be attributed to the interference of GalNAc in the interaction of TRF with its receptor, because absorption of TRF activity with B cells was notably inhibited by the presence of GalNAc. To substantiate this point further, we established binding assay of B151-TRF molecule to the receptor on B cells by using 125I-labeled TRF fraction enriched by reversed-phase high-performance liquid chromatography and gel filtration. The results revealed that the binding of 125I-TRF molecule to the B cells was almost completely blocked by GalNAc. Moreover, the existence of GalNAc residue(s) on B151-TRF molecule was evidenced by the facts that 1) the TRF activity was eluted from lectin gels with specificity for GalNAc as revealed by the functional assay, and 2) the 125I-TRF molecule specifically bound to such lectin gels. Thus, the GalNAc residue(s) on B151-TRF molecule plays an important role in binding of TRF molecule to the receptor and in the stimulation of B cells. The molecular properties of B cell-stimulatory B151-TRF and its mode of interaction with corresponding receptor on B cells were discussed in the context of B151-TRF as a glycosylated lymphokine molecule and B151-TRF receptor as a carbohydrate-binding protein (animal lectin).
Y Takahama; S Ono; Y Hara; S Hayashi; K Dobashi; T Hamaoka
Related Documents :
20727586 - Control of highly migratory cells by microstructured surface based on transient change ...
2478346 - The interaction of hyaluronate with the cell surface: the hyaluronate receptor and the ...
12594226 - Cell surface expression of the melanocortin-4 receptor is dependent on a c-terminal di-...
3233306 - Time-dependent ligand current into a saturating cell performing chemoreception.
22695396 - Cell death. 1+1≠2.
23915336 - Investigation of the stability and cellular uptake of self-associated monoclonal antibo...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  135     ISSN:  0022-1767     ISO Abbreviation:  J. Immunol.     Publication Date:  1985 Oct 
Date Detail:
Created Date:  1985-10-16     Completed Date:  1985-10-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2534-40     Citation Subset:  AIM; IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Acetylgalactosamine / analysis,  pharmacology,  physiology*
B-Lymphocytes / immunology*,  metabolism
Binding, Competitive
Galactosamine / analogs & derivatives*
Hemolytic Plaque Technique
Hybridomas / metabolism
Immunosuppressive Agents / physiology
Leukemia, Experimental / metabolism
Lymphocyte Activation*
Lymphokines / analysis,  metabolism,  physiology*
Mice, Inbred BALB C
N-Acetylneuraminic Acid
Receptors, Antigen, B-Cell / metabolism*,  physiology
Sialic Acids / analysis
T-Lymphocytes / analysis,  metabolism*
Reg. No./Substance:
0/Immunosuppressive Agents; 0/Interleukin-5; 0/Lymphokines; 0/Receptors, Antigen, B-Cell; 0/Sialic Acids; 131-48-6/N-Acetylneuraminic Acid; 31022-50-1/Acetylgalactosamine; 7535-00-4/Galactosamine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Analysis of lymphocytes infiltrating the thyroid gland of Obese strain chickens.
Next Document:  Complement receptor type three-dependent degradation of opsonized erythrocytes by mouse macrophages.