Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 1165-1170 |
| Number of pages | 6 |
| Journal | Japanese Journal of Cancer Research |
| Volume | 87 |
| Issue number | 11 |
| Publication status | Published - Nov 1996 |
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Keywords
- Balb/c leukemia RL♂1
- Cytotoxic T lymphocyte
- Natural precursor peptide
- Protease
- Tumor rejection antigen peptide
ASJC Scopus subject areas
- Cancer Research
- Oncology
Cite this
Production of murine leukemia RL♂1 rejection antigen peptide pRL1a by proteolysis of natural precursor pRL1b. / Ono, Toshiro; Uenaka, Akiko; Nakayama, Eiichi.
In: Japanese Journal of Cancer Research, Vol. 87, No. 11, 11.1996, p. 1165-1170.Research output: Contribution to journal › Article
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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
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
UR - http://www.scopus.com/inward/record.url?scp=0029959721&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029959721&partnerID=8YFLogxK
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 -