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Japanese Journal of Cancer Research : Gann logoLink to Japanese Journal of Cancer Research : Gann
. 1996 Nov;87(11):1165–1170. doi: 10.1111/j.1349-7006.1996.tb03127.x

Production of Murine Leukemia RL♂1 Rejection Antigen Peptide pRL1a by Proteolysis of Natural Precursor pRL1b

Toshiro Ono 1, Akiko Uenaka 1, Eiichi Nakayama 1,
PMCID: PMC5921005  PMID: 9045946

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♂1‐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 serumcontaining 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‐pRL1a‐2,3D 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 Ld molecules and pRL1b (SI‐pRL1a) peptide is its natural precursor, which generates pRL1a via proteolysis.

Keywords: BALB/c leukemia RL♂l, Cytotoxic T lymphocyte, Tumor rejection antigen peptide, Natural precursor peptide, Protease

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