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Diabetes, Vol 34, Issue 3 246-250, Copyright © 1985 by American Diabetes Association
Do pancreatic islets contain significant amounts of phosphoenolpyruvate carboxykinase or ferroactivator activity?
MJ MacDonald and CM Chang
Phosphoenolpyruvate carboxykinase activity was measured in rat pancreatic
islet cytosol and mitochondria. No carboxykinase activity was detected
under a variety of conditions, including those that increase
phosphoenolpyruvate carboxykinase activity in nonislet tissues, such as
starving animals or incubating the islet extracts with Fe2+ or Mn2+ before
assaying for enzyme activity. The amounts of islet cytosol protein used
exceeded those of liver in companion assays used as controls. It was
calculated that if islet phosphoenolpyruvate carboxykinase activity was
0.005 that of liver, or 1 X 10(-5) as high as pyruvate kinase activity in
islets, it should have been detected in the assays used. Ferroactivator is
a protein that permits Fe2+ to activate phosphoenolpyruvate carboxykinase
and it is ubiquitous to many tissues that do and even do not contain the
carboxykinase. Ferroactivator activity was not detectable in pancreatic
islets. Pyruvate kinase, an enzyme that catalyzes a reaction that is
essentially the opposite of that catalyzed by phosphoenolpyruvate
carboxykinase (i.e., phosphoenolpyruvate formation), is plentiful in islet
cytosol. Therefore, even if phosphoenolpyruvate carboxykinase activity is
present in pancreatic islets, it is so low that it is unlikely that
phosphoenolpyruvate formation would be favored and the contribution of the
carboxykinase to intracellular carbohydrate metabolism must be
quantitatively unimportant.

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Copyright © 1985 by the American Diabetes Association.
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