This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by MacDonald, M. J. Articles by Mertz, R. J. Search for Related Content PubMed PubMed Citation Articles by MacDonald, M. J. Articles by Mertz, R. J.

High Activity of Mitochondrial Glycerol Phosphate Dehydrogenase in Insulinomas and Carcinoid and Other Tumors of the Amine Precursor Uptake Decarboxylation System¹

Departments of Pediatrics [M. J. M., R. J. M.] and Surgical Pathology [T. F. W.], University of Wisconsin Medical School, Madison, Wisconsin 53706

The activity of the mitochondrial glycerol phosphate dehydrogenase (EC 1.1.99.5), the enzyme unique to the glycerol phosphate hydrogen shuttle, was measured in normal human tissues and tumors and compared with the activity of succinate dehydrogenase, another enzyme that transfers electrons to ubiquinone at site II of the electron transport chain. Six of 7 insulinomas and 10 of 12 carcinoid tumors showed high glycerol phosphate dehydrogenase activity. The activity was also increased in 3 of 4 gastrinomas, 2 paraganglionomas, 1 of 4 thyroid nodules, and 1 parathyroid tumor. These tissues belong to the amine precursor uptake decarboxylation system. The activity of glycerol phosphate dehydrogenase was generally unremarkable in non-amine precursor uptake decarboxylation system tumors and in normal tissues studied. However, 1 of 2 breast carcinomas, 1 submandibular tumor, and 2 of 3 melanomas were enriched in glycerol phosphate dehydrogenase activity. In general, succinate dehydrogenase activity exceeded that of glycerol phosphate dehydrogenase in all tissues except some of the tissues in which glycerol phosphate dehydrogenase activity was high. Normal tissues, such as the pancreatic ß-cell, which aerobically metabolize glucose rapidly utilize the glycerol phosphate shuttle to oxidize the large amount of NADH formed from glucose metabolism in the cytosol. Whether this is the reason for the enriched activity of the glycerol phosphate dehydrogenase in certain amine precursor uptake decarboxylation system tumors is unknown.

¹ This work was supported by NIH Grant DK28348.

² To whom requests for reprints should be addressed, at University of Wisconsin Medical School, 1300 University Avenue, Room 3459, Madison, WI 53706.

Received 4/27/90. Accepted 8/ 9/90.

This article has been cited by other articles:

				P. Chieco, A. P. Venturini, M. Barbanti, and E. Romagnoli A Quantitative Cytochemical Study on the Pathogenesis of Streptozotocin-Induced Epithelial Tumors in Rat Kidney Toxicol Pathol, June 1, 1993; 21(4): 402 - 408. [Abstract] [PDF]

				Q. Gong, L. J. Brown, and M. J. MacDonald Functional Analysis of Two Promoters for the Human Mitochondrial Glycerol Phosphate Dehydrogenase Gene J. Biol. Chem., November 22, 2000; 275(48): 38012 - 38021. [Abstract] [Full Text] [PDF]