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PGM3 (phosphoglucomutase 3; phosphoacetylglucosamine mutase)
is an enzyme of the hexosamine biosynthetic pathway that catalyzes the
interconversion of N-acetylglucosamine-6-phosphate and
N-acetylglucosamine-1-phosphate, thereby supporting production of
UDP-N-acetylglucosamine (UDP-GlcNAc). UDP-GlcNAc is required
for protein N-glycosylation, O-GlcNAcylation and other glycosylation reactions
that regulate cell signalling, metabolism and protein stability. PGM3 is
upregulated in several cancers and can promote tumour-cell proliferation,
migration, metabolic reprogramming and survival. In colorectal cancer, increased
PGM3 supports O-GlcNAcylation and maintains β-catenin signalling, whereas PGM3
knockdown reduces proliferation and migration. In bladder cancer, elevated PGM3
promotes both glycolysis and oxidative phosphorylation and is associated with
tumour growth, metastasis and poorer prognosis. The typical cancer-associated
direction is therefore generally up, while the desired
anticancer modulation is down or enzyme inhibition.
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