RRC ID 28667
Author Nishi N, Itoh A, Fujiyama A, Yoshida N, Araya S, Hirashima M, Shoji H, Nakamura T.
Title Development of highly stable galectins: truncation of the linker peptide confers protease-resistance on tandem-repeat type galectins.
Journal FEBS Lett
Abstract 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.
Volume 579(10)
Pages 2058-64
Published 2005-4-11
DOI 10.1016/j.febslet.2005.02.054
PII S0014-5793(05)00287-5
PMID 15811318
MeSH Base Sequence DNA, Complementary Galectins / genetics Galectins / metabolism* Peptide Hydrolases / metabolism* Tandem Repeat Sequences*
IF 3.057
Times Cited 102
DNA material pET-G9Null-11a (RDB08451) pET-G9Null R65D-2a (RDB08452) pET-G9Null R212D-3a (RDB08453) pGEX-G8Null-1a (RDB08454) pET-G8Null-5a (RDB08455)