Cancer Grows on SOD1

A report in the Proceedings of the National Academy of Sciences shows how superoxide dismutase 1 acts as a master regulatory switch for kinase phosphorylation in angiogenesis and cell proliferation, making it a potential target to treat a variety of cancers.1 Although some mechanistic details remain to be elucidated, superoxide dismutase 1 inhibition could be used in combination with other cancer treatments and might have utility in some degenerative diseases as well.

Superoxide dismutase 1 (SOD1) is one of three SOD enzymes that catalyze the conversion of intracellular superoxide to hydrogen peroxide. Intracellular superoxide is produced when a growth factor binds to its receptor on the cell surface and induces receptor phosphorylation (see Figure 1, "Superoxide dismutase 1 in cancer").

Recently, SOD1 was identified as the target of tetrathiomolybdate (TTM),2 a compound that has antiangiogenic and antitumor activity in mice,3-5but whose mechanism of action remained unclear.

In the PNASpaper, short interfering RNA and ATN-224, a second-generation TTM from Attenuon LLC, were used to study SOD1 inhibition in human umbilical vein endothelial cells (HUVECs) and multiple myeloma (MM) tumor cells.

The research team was led by Fernando Doate while he was associate director of biology at Attenuon and included scientists from Cold Spring Harbor

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