Glycolytic enzyme activities in breast cancer metastases.
The activities of hexokinase, phosphofructokinase, aldolase, enolase and pyruvate kinase were studied in breast cancer metastases occurring at various sites and compared with the enzyme activities in a series of primary breast cancers. The activities of all enzymes studied were significantly higher in the metastases compared to the primary tumors (p less than or equal to 0.05). However, no changes in the isoenzyme patterns of enolase and pyruvate kinase were observed when the metastases were compared with primary breast cancers. Differences in location of the metastases did not lead to differences in enzyme activities. Our data suggest an association of an increasing rate of glycolysis with tumor progression.
Hennipman
A
A
Surgical Department, University Hospital, The Netherlands.
van Oirschot
B A
BA
Smits
J
J
Rijksen
G
G
Staal
G E
GE
D000368:Aged; D001943:Breast Neoplasms / Q000201:enzymology* / Q000473:pathology; D005260:Female; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D006019:Glycolysis; D006593:Hexokinase / Q000378:metabolism; D006801:Humans; D008875:Middle Aged; D009362:Neoplasm Metastasis / Q000201:enzymology*; D010732:Phosphofructokinase-1 / Q000378:metabolism; D010751:Phosphopyruvate Hydratase / Q000378:metabolism; D011770:Pyruvate Kinase / Q000378:metabolism
D006593:Hexokinase; D010732:Phosphofructokinase-1; D011770:Pyruvate Kinase; D005634:Fructose-Bisphosphate Aldolase; D010751:Phosphopyruvate Hydratase