Phosphoglycerate mutase, 2,3 bisphosphoglycerate phosphatase, creatine kinase and enolase activity and isoenzymes in breast carcinoma

We have compared the levels of phosphoglycerate mutase (EC 5.4.2.1), 2,3-bi sphosphoglycerate phosphatase (EC 3.1.3.13), creatine kinase (EC 2.7.3.2) a nd enolase (EC 4.2.1.11) activities and the distribution of their isoenzyme s in normal breast tissue and in breast carcinoma. Tumour tissue had higher phosphoglycerate mutase and enolase activity than normal tissue. Creatine kinase activity was higher in seven out of 12 tumours. In contrast 2,3-bisp hosphoglycerate phosphatase activity was lower. Phosphoglycerate mutase, en olase and 2,3-bisphosphoglycerate phosphatase presented greater changes in the oestrogen receptor-negative/progesterone receptor-negative breast carci nomas than in the steroid receptor-positive tumours. Determined by electrop horesis, type BE phosphoglycerate mutase, type BE creatine kinase and alpha alpha-enolase were the major isoenzymes detected in normal breast tissue. Types alpha gamma and gamma gamma enolase, types MB and MM phosphoglycerate mutase were detected in much lower proportions. In tumours a decrease of p hosphoglycerate mutase isoenzymes possessing gamma-type subunit and some in crease of enolase isoenzymes possessing gamma-type subunit was observed. No delectable change was observed in the creatine kinase phenotype. (C) 2000 Cancer Research Campaign.