Application of a microchemical technique to the elucidation of enzyme activity profiles within single human mammary tumors.
An ultramicrochemical technique has been adapted to the evolution of enzyme profiles within individual human mammary tumors. Tandem observation of adjacent stained and lyophilized sections permitted dissection of microgram quantities of freeze-dried material within confirmed regions of malignancy. Enzymes frequently monitored to examine glycolytic, respiratory, and metastatic capacity were microanalyzed successfully: lactic dehydrogenase (LDH), phosphoglucose isomerase (PGI), malate dehydrogenase (MDH), acid phosphatase (AP), aldolase (ALD), glucose-6-phosphate dehydrogenase (G6PDH), pyruvate kinase (PK), alpha-glycerophosphate dehydrogenase (alpha-GOPDH), hexokinase (HK), and phosphofructokinase (PRK). All enzyme activities were higher in infiltrating ductal carcinomas than in fibroadenomas. Extracts of tumor cells mixed in varying proportions with brain or muscle extracts of rat evidenced no modification of expected activity. The technical adaptation described provided a sensitive methodology to resolve problems of relication, profile analysis, sample quantity, and selectivity within heterogeneous tissues.
D000135:Acid Phosphatase / Q000378:metabolism; D000232:Adenofibroma / Q000201:enzymology*; D000429:Alcohol Oxidoreductases / Q000378:metabolism; D001943:Breast Neoplasms / Q000201:enzymology*; D002285:Carcinoma, Intraductal, Noninfiltrating / Q000201:enzymology*; D005260:Female; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005956:Glucose-6-Phosphate Isomerase / Q000378:metabolism; D006801:Humans; D008832:Microchemistry; D010770:Phosphotransferases / Q000378:metabolism
D000429:Alcohol Oxidoreductases; D010770:Phosphotransferases; D000135:Acid Phosphatase; D005634:Fructose-Bisphosphate Aldolase; D005956:Glucose-6-Phosphate Isomerase