TY - JOUR
T1 - Production of murine leukemia RL♂1 rejection antigen peptide pRL1a by proteolysis of natural precursor pRL1b
AU - Ono, Toshiro
AU - Uenaka, Akiko
AU - Nakayama, Eiichi
N1 - Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1996/11
Y1 - 1996/11
N2 - In this study, we demonstrated that NH2-terminal Ser and Ile residues of pRL1b (SI-pRL1a) (SIIPGLPLSL) are not involved in the recognition by RL♂l-specific cytotoxic T lymphocyte. The sensitization activity observed with pRL1b (SI-pRL1a) was not greater than that of peptides substituted with irrelevant amino acids at these positions. In serum-free medium, pRL1a retained sensitization activity, but pRL1b (SI-pRL1a) did not. Furthermore, addition of bestatin to serum-containing medium blocked sensitization by pRL1b (SI-pRL1a). On the other hand, the addition of captopril enhanced it, probably by inhibiting the degradation of pRL1a by ACE, pRL1a-D peptide with D-Ile in place of the L-Ile residue of pRL1a (IPGLPLSL) showed sensitization, but SI-pRL1a2,3D peptide, which has D-Iles in place of the L-Ile residues of pRL1b (SI-pRL1a), and which was not cleaved between the two D-Iles, did not. The findings suggest that pRL1a is the antigenic peptide bound to L(d) molecules and pRL1b (SI-pRL1a) peptide is its natural precursor, which generates pRL1a via proteolysis.
AB - In this study, we demonstrated that NH2-terminal Ser and Ile residues of pRL1b (SI-pRL1a) (SIIPGLPLSL) are not involved in the recognition by RL♂l-specific cytotoxic T lymphocyte. The sensitization activity observed with pRL1b (SI-pRL1a) was not greater than that of peptides substituted with irrelevant amino acids at these positions. In serum-free medium, pRL1a retained sensitization activity, but pRL1b (SI-pRL1a) did not. Furthermore, addition of bestatin to serum-containing medium blocked sensitization by pRL1b (SI-pRL1a). On the other hand, the addition of captopril enhanced it, probably by inhibiting the degradation of pRL1a by ACE, pRL1a-D peptide with D-Ile in place of the L-Ile residue of pRL1a (IPGLPLSL) showed sensitization, but SI-pRL1a2,3D peptide, which has D-Iles in place of the L-Ile residues of pRL1b (SI-pRL1a), and which was not cleaved between the two D-Iles, did not. The findings suggest that pRL1a is the antigenic peptide bound to L(d) molecules and pRL1b (SI-pRL1a) peptide is its natural precursor, which generates pRL1a via proteolysis.
KW - Balb/c leukemia RL♂1
KW - Cytotoxic T lymphocyte
KW - Natural precursor peptide
KW - Protease
KW - Tumor rejection antigen peptide
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U2 - 10.1111/j.1349-7006.1996.tb03127.x
DO - 10.1111/j.1349-7006.1996.tb03127.x
M3 - Article
C2 - 9045946
AN - SCOPUS:0029959721
VL - 87
SP - 1165
EP - 1170
JO - Cancer Science
JF - Cancer Science
SN - 1347-9032
IS - 11
ER -