p815 mouse
Recently Published Documents


TOTAL DOCUMENTS

9
(FIVE YEARS 0)

H-INDEX

5
(FIVE YEARS 0)

1999 ◽  
Vol 93 (1) ◽  
pp. 46-58 ◽  
Author(s):  
Christopher P. Shelburne ◽  
Thomas F. Huff

1988 ◽  
Vol 167 (4) ◽  
pp. 1391-1405 ◽  
Author(s):  
J L Maryanski ◽  
P Pala ◽  
J C Cerottini ◽  
G Corradin

The specificity of peptide recognition by a number of Kd-restricted CTL clones specific for HLA-CW3 or HLA-A24 was investigated. The CTL clones were derived from DBA/2 (H-2d) mice immunized with syngeneic P815 mouse cells transfected with genes encoding HLA-CW3 or HLA-A24 class I molecules. We had previously shown that CTL clones that lysed P815-CW3 transfectant target cells could lyse P815 (HLA-) target cells incubated with synthetic CW3 peptides corresponding to the COOH-terminal end of the alpha 2 domain. In the present study, we found that Kd-restricted CTL clones that lysed P815-A24 transfectant target cells recognized a synthetic peptide from the same region (residues 170-182) of the A24 molecule. CW3 and A24 differ by only one amino acid within this region. Recognition of CW3 or A24 peptides corresponded exactly with lysis of P815-HLA transfectants both for clones that mutually exclusively lysed CW3 or A24 transfectant target cells and for CW3/A24 crossreactive CTL clones. The latter CTL clones that lysed both CW3 and A24 transfectant target cells showed a clear preference for the peptide corresponding to the immunizing HLA allele. The homologous CW3 and A24 peptides could compete with each other for recognition, in contrast to a peptide from the same region of HLA-B7. Peptides from the corresponding region of the endogenous Kd and Dd/Ld molecules could also inhibit recognition of CW3 and A24 peptides. Competition with peptides apparently occurred at the level of the target cell. These results are consistent with a model whereby MHC class I molecules position protein fragments or peptides for specific recognition by T cells.


1979 ◽  
Vol 34 (7-8) ◽  
pp. 558-564 ◽  
Author(s):  
Thomas L. J. Boehm ◽  
Dusan Drahovsky

Abstract A specific class of DNA sequences, the inverted repetitive sequences, forms a double-stranded structure within a single linear polynucleotide chain in denatured DNA. The reassociation process is unimolecular and occurs very fast. Quantitative analyses have shown that these sequences com-E rise about 4-5% of the nuclear DNA of various mammalian cells (P815 mouse mastocytoma, Hela, L cells, Raji and Chang cells, and human embryonic hepatocytes) and are interspersed within sequences of other degrees of repetitiveness.After labeling the cells with L-[Metnyl-3H]methionine and [14C]deoxycytidine, relative rates of enzymic DNA methylation were computed on the basis of 3H and 14C radioactivities found in py­ rimidine residues of the nuclear DNA. The results indicate that DNA of inverted repetitive sequences is methylated to a level about 50% higher than the ordinary repetitive sequences and to about 300% higher than the unique and intermediary sequences.The biological function of the inverted repeats as well as the role of their enzymic hypermethyl­ ation is unknown.


FEBS Letters ◽  
1978 ◽  
Vol 96 (1) ◽  
pp. 192-196 ◽  
Author(s):  
Françoise Bieri-Bonniot ◽  
Alfred R. Schuerch

Sign in / Sign up

Export Citation Format

Share Document