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Catalytic lectin (leczyme) from bullfrog (Rana catesbeiana) eggs.

K Nitta¹, K Ozaki, Y Tsukamoto

¹UNIV WASHINGTON, SEATTLE, WA 98119 USA. BIOMEMBRANE INST, SEATTLE, WA 98119 USA.

International Journal of Oncology

|May 5, 2011

Summary

Catalytic egg lectins (leczymes) degrade RNA in tumor cells, inhibiting proliferation. These frog egg enzymes bind to cell surfaces, enter cells, and trigger signaling pathways, but are detoxified by cellular mechanisms.

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Area of Science:

Biochemistry
Molecular Biology
Cancer Research

Background:

Catalytic lectins (leczymes) from frog eggs possess sialic acid-binding and RNase activities.
These enzymes inhibit tumor cell proliferation, but their cytotoxic mechanism is not fully understood.
RNase A lacks tumoricidal activity, suggesting a unique mechanism for leczymes.

Purpose of the Study:

To investigate the cytotoxic mechanism of cSBL, a frog egg leczyme.
To elucidate the role of RNA degradation and signal transduction in cSBL-induced cell death.
To identify cellular mechanisms involved in cSBL resistance and detoxification.

Main Methods:

Established a cSBL-resistant cell line (RC-150) from mouse leukemia P388 cells.
Assessed RNA degradation in cSBL-treated sensitive (P388) and resistant (RC-150) cells.

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Monitored intracellular Ca2+ levels, protein kinase activities (PKA, PKG), glutathione levels, and glutathione-S-transferase (GST) activity.

Main Results:

cSBL induced extensive RNA degradation in P388 cells within 1 hour, but not in RC-150 cells.
cSBL treatment altered signal transduction, decreasing Ca2+ and PKA activity while increasing PKG activity in P388 cells.
cSBL decreased glutathione levels and enhanced GST activity in P388 cells, with no effect on RC-150 cells.

Conclusions:

cSBL induces tumor cell death through specific RNA degradation and modulation of intracellular signaling pathways.
Internalized cSBL is detoxified by cellular mechanisms, potentially involving GST or thioltransferase, leading to resistance.
These findings support a bifunctional model of leczymes as adhesive proteins and RNase enzymes in cytotoxicity.