Development of highly stable galectins: truncation of the linker peptide confers protease-resistance on tandem-repeat type galectins.
Galectin-9 and galectin-8, members of beta-galactoside-binding animal lectin family, are promising agents for the treatment of immune-related and neoplastic diseases. The proteins consist of two carbohydrate recognition domains joined by a linker peptide, which is highly susceptible to proteolysis. To increase protease resistance, we prepared mutant proteins by serial truncation of the linker peptide. As a result, mutant forms lacking the entire linker peptide were found to be highly stable against proteolysis and retained their biological activities. These mutant proteins might be useful tools for analyzing the biological functions and evaluating the therapeutic potential of galectin-9 and galectin-8.
Nishi
Nozomu
N
Department of Endocrinology, Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan. nnishi@med.kagawa-u.ac.jp
Itoh
Aiko
A
Fujiyama
Aimi
A
Yoshida
Naoko
N
Araya
Shin-ichi
S
Hirashima
Mitsuomi
M
Shoji
Hiroki
H
Nakamura
Takanori
T
D001483:Base Sequence; D018076:DNA, Complementary; D037161:Galectins / Q000235:genetics / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D020080:Tandem Repeat Sequences
D018076:DNA, Complementary; D037161:Galectins; D010447:Peptide Hydrolases