The glycogen concentration in liver is altered in various pathophysiologic states. In fasted rats, it is higher in diabetic, and lower in adrenalectomized rats compared to control animals. In fed rats, it is lower in diabetic, and little changed in adrenalectomized animals compared to controls. We were interested in determining whether the activity of glycogenin, a self-glycosylating protein that initiates the synthesis of new glycogen molecules, could explain these differences in liver glycogen concentration. Glycogenin activity was measured by the incorporation of 14C-glucose from UDP-U-14C-glucose into an acid-precipitable product before and after amylase treatment of liver extracts. The glycogenin activity was similar in normal, diabetic and adrenalectomized fasted animals, regardless of the hepatic glycogen concentration. In fasted rats, glycogenin was present predominantly as the free-form of the enzyme, i.e., not attached to an amylase-digestible glycan, presumably glycogen. In contrast, in fed rats, the majority, if not all of the glycogenin was incorporated into a glycogen-like (proteoglycan) molecule. Proteoglycan synthase activity, previously identified in normal fed rats, also was present in diabetic and adrenalectomized fed rats, and the activity was similar. Thus, the altered ability to store hepatic glycogen in diabetic fed and fasted and adrenalectomized fasted rats cannot be explained by decreases in glycogenin or proteoglycan synthase activities, at least as measured using the present assays.
|Original language||English (US)|
|Number of pages||7|
|Journal||Cellular and molecular biology (Noisy-le-Grand, France)|
|State||Published - Sep 1998|