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The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

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Results: 31 to 35 of 35

Publication Record


Exposure to topical bovine thrombin during surgery elicits a response against the xenogeneic carbohydrate galactose alpha1-3galactose.
Schoenecker JG, Hauck RK, Mercer MC, Parker W, Lawson JH
(2000) J Clin Immunol 20: 434-44
MeSH Terms: Administration, Topical, Animals, Antigens, Heterophile, Cattle, Coronary Artery Bypass, Disaccharides, Drug Contamination, Epitopes, Female, Glycoproteins, Hemagglutinins, Hemostatics, Humans, Male, Middle Aged, Models, Immunological, Species Specificity, Thrombin
Show Abstract · Added May 28, 2014
Exposure of humans to topical bovine thrombin has been associated with development of antibodies against bovine and human coagulation factors and blood coagulation abnormalities. However, the nature of this humoral response is unknown. In this study, numerous glycoproteins in the topical bovine thrombin were found to contain the Gal(alpha1)-3Gal epitope, which is known to be highly immunogenic. More importantly, Gal(alpha1)-3Gal is recognized by natural antibodies that are found in all normal individuals and are known to effectively mediate complement activation and subsequent destruction of xenogeneic tissues. Thus, primary exposure of normal individuals to topical bovine thrombin is expected to result in an immediate immune reaction against that reagent. Further, following exposure to topical bovine thrombin, the levels of anti-Gal(alpha1)-3Gal IgG rose to levels tenfold greater than the average level of natural anti-Gal(alpha1)-3Gal IgG in naive individuals. Thus, Gal(alpha1)-3Gal in topical bovine thrombin accounts for, at least in part, the highly immunogenic nature of this reagent.
0 Communities
1 Members
0 Resources
18 MeSH Terms
Differential immune response to carbohydrate epitopes on allo- and xenografts: implications for accommodation.
Tanemura M, Yin D, Chong A, Galili U
(2000) Transplant Proc 32: 991-3
MeSH Terms: Animals, Antibodies, Heterophile, Cell Membrane, Disaccharides, Epitopes, Galactosyltransferases, Humans, Isoantibodies, Kidney, Mice, Mice, Inbred C3H, Mice, Knockout, Models, Immunological, Spleen, Swine, T-Lymphocytes, T-Lymphocytes, Helper-Inducer, Transplantation, Heterologous, Transplantation, Homologous
Added December 10, 2013
0 Communities
1 Members
0 Resources
19 MeSH Terms
A molecular basis for how a single TCR interfaces multiple ligands.
Boesteanu A, Brehm M, Mylin LM, Christianson GJ, Tevethia SS, Roopenian DC, Joyce S
(1998) J Immunol 161: 4719-27
MeSH Terms: Amino Acid Sequence, Animals, Antigen Presentation, Antigens, Epitopes, H-2 Antigens, Ligands, Mice, Mice, Inbred BALB C, Mice, Inbred C57BL, Models, Immunological, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Peptide Library, Protein Binding, Protein Conformation, Receptors, Antigen, T-Cell, Structure-Activity Relationship, T-Lymphocytes, Cytotoxic
Show Abstract · Added October 2, 2015
CD8+ T cells respond to Ags when their clonotypic receptor, the TCR, recognizes nonself peptides displayed by MHC class I molecules. The TCR/ligand interactions are degenerate because, in its life time, the TCR interacts with self MHC class I-self peptide complexes during ontogeny and with self class I complexed with nonself peptides to initiate Ag-specific responses. Additionally, the same TCR has the potential to interact with nonself class I complexed with nonself peptides. How a single TCR interfaces multiple ligands remains unclear. Combinatorial synthetic peptide libraries provide a powerful tool to elucidate the rules that dictate how a single TCR engages multiple ligands. Such libraries were used to probe the requirements for TCR recognition by cloned CD8+ T cells directed against Ags presented by H-2Kb class I molecules. When H-2Kb contact residues were examined, position 3 of the peptides proved more critical than the dominant carboxyl-terminal anchor residue. Thus, secondary anchor residues can play a dominant role in determining the antigenicity of the epitope presented by class I molecules. When the four solvent-exposed potential TCR contact residues were examined, only one or two of these positions required structurally similar residues. Considerable structural variability was tolerated at the remaining two or three solvent-exposed residues of the Kb-binding peptides. The TCR, therefore, requires close physico-chemical complementarity with only a few amino acid residues, thus explaining why TCR/MHC interactions are of low affinity and degenerate.
0 Communities
1 Members
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20 MeSH Terms
Intrathymic delta selection events in gammadelta cell development.
Passoni L, Hoffman ES, Kim S, Crompton T, Pao W, Dong MQ, Owen MJ, Hayday AC
(1997) Immunity 7: 83-95
MeSH Terms: Animals, Cell Differentiation, Flow Cytometry, Gene Rearrangement, delta-Chain T-Cell Antigen Receptor, Mice, Mice, Inbred C57BL, Models, Immunological, Polymorphism, Restriction Fragment Length, Receptors, Antigen, T-Cell, alpha-beta, Receptors, Antigen, T-Cell, gamma-delta, T-Lymphocytes, Thymus Gland
Show Abstract · Added March 24, 2014
The major pathway of gammadelta cell development is shown to be regulated by in-frame rearrangements at the T cell receptor (TCR) delta locus. Such "delta selection" occurs at or around the same point in thymocyte development as selection for in-frame rearrangements at the TCRbeta locus. However, there are at least two major differences with beta selection: first, delta selection commonly involves selection on the cognate TCR chain, gamma, suggesting that there is no "preTgamma" chain of major biological significance; second, most gammadelta-selected thymocytes differentiate rather than proliferate. Nonetheless, some delta selection events seemingly facilitate thymocyte expansion, similar to alphabeta T cell development. In these cases, TCRgamma selection is less obvious. Furthermore, the capacity of individual gamma chains to facilitate gammadelta selection is shown to vary with developmental age. The results further clarify early T cell development at the beta selection/delta selection stage and place clear constraints on models of cell fate determination.
0 Communities
1 Members
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12 MeSH Terms
Alloreactivity, antigen recognition and T-cell selection: three diverse T-cell recognition problems with a common solution.
Joyce S, Nathenson SG
(1996) Immunol Rev 154: 59-103
MeSH Terms: Amino Acid Sequence, Animals, Histocompatibility Antigens Class I, Humans, Models, Immunological, Molecular Sequence Data, Protein Binding, Receptors, Antigen, T-Cell, T-Lymphocytes
Added October 2, 2015
0 Communities
1 Members
0 Resources
9 MeSH Terms