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Molecular Characterization and Mitogenic Activity of a Lectin from Purse Crab Philyra Pisum
Author(s) -
Jong Cheon Na,
Byung Tae Park,
Woo Hyuk Chung,
Ha Hyung Kim
Publication year - 2011
Publication title -
korean journal of physiology and pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.514
H-Index - 29
eISSN - 2093-3827
pISSN - 1226-4512
DOI - 10.4196/kjpp.2011.15.4.241
Subject(s) - concanavalin a , splenocyte , lectin , pisum , microbiology and biotechnology , biology , stimulation , hemolymph , biochemistry , amino acid , chemistry , endocrinology , in vitro
A lectin from the hemolymph of purse crab, Philyra pisum, was found to have anti-proliferative activity on human lung cancer cells by our laboratory. In this study, P. pisum lectin (PPL) was molecularly characterized including molecular mass, amino acid sequences, amino acid composition, and the effects of metal ions, temperature, and pH on the activity. We found that PPL showed mitogenic activity on human lymphocytes and BALB/c mouse splenocytes. The mitogenic activity (maximum stimulation index, SI=9.57±0.59) of PPL on human lymphocytes was higher than that of a standard well-known plant mitogen, concanavalin A (maximum SI=8.80±0.59). The mitogenic activity mediated by PPL is required for optimum dosing, and higher or lower concentrations caused decreases in mitogenic response. PPL also induced mitogenic activity on mouse splenocytes, however, the maximum SI (1.77±0.09) on mouse splenocytes of PPL was lower than that (2.14±0.15) of concanavalin A. In conclusion, PPL is a metal ion-dependent monomer lectin with mitogenic activity, and could be used as a lymphocyte or splenocyte stimulator.

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