Transformation linked decrease of pyruvate dehydrogenase complex in human epidermis.
Epidermis exhibits glycolytic features peculiar to cancer cells. The activity of pyruvate dehydrogenase complex, both active (PDHa) and total (PDHt) forms, has been investigated and compared in epidermis and epidermal carcinomas from human source. Low or undetectable PDHa is found in either normal and neoplastic tissue. PDHt is unchanged in human epidermis between the second and seventh decades of life but is dramatically decreased following neoplastic transformation (0.107 and 0.026 units/g fresh tissue for epidermis and epidermal carcinoma, respectively). As PDH plays a key role in mitochondrial carbohydrate metabolism, the decrease of total enzymic capacity found in tumors suggest that different mechanisms regulate PDH expression and, in turn, glycolytic mechanisms of epidermis and cancer cells.
Eboli
M L
ML
Institute of General Pathology, Catholic University, Rome, Italy.
Pasquini
A
A
D000328:Adult; D000368:Aged; D002280:Basal Cell Carcinoma / Q000201:enzymology*; D002294:Carcinoma, Squamous Cell / Q000201:enzymology*; D004817:Epidermis / Q000201:enzymology*; D005260:Female; D006801:Humans; D008297:Male; D008875:Middle Aged; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism*; D012878:Skin Neoplasms / Q000201:enzymology*
D011768:Pyruvate Dehydrogenase Complex