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J Biol Chem, Vol. 274, Issue 1, 117-122, January 1, 1999

Conformational Change of the Catalytic Subunit of Glucose-6-phosphatase in Rat Liver during the Fetal-to-Neonatal Transition

Ferenc Puskás^§, Paola Marcolongo, Sharlene L. Watkins, József Mandl^§, Bernard B. Allan^¶, Pamela Houston^¶, Ann Burchell^¶, Angelo Benedetti, and Gábor Bánhegyi

From the  Istituto di Patologia Generale, Università di Siena, 53100 Siena, Italy, the ^§ Department of Medical Chemistry, Semmelweis University of Medicine, 1444 Budapest, Hungary, and the ^¶ Department of Obstetrics and Gynaecology, Ninewells Hospital and Medical School, Dundee DD1 9SY, United Kingdom

The glucose-6-phosphatase system was investigated in fetal rat liver microsomal vesicles. Several observations indicate that the orientation of the catalytic subunit is different in the fetal liver in comparison with the adult form: (i) the phosphohydrolase activity was not latent using glucose-6-phosphate as substrate, and in the case of other phosphoesters it was less latent; (ii) the intravesicular accumulation of glucose upon glucose-6-phosphate hydrolysis was lower; (iii) the size of the intravesicular glucose-6-phosphate pool was independent of the glucose-6-phosphatase activities; (iv) antibody against the loop containing the proposed catalytic site of the enzyme inhibited the phosphohydrolase activity in fetal but not in adult rat liver microsomes. Glucose-6-phosphate, phosphate, and glucose uptake could be detected by both light scattering and/or rapid filtration method in fetal liver microsomes; however, the intravesicular glucose-6-phosphate and glucose accessible spaces were proportionally smaller than in adult rat liver microsomes. These data demonstrate that the components of the glucose-6-phosphatase system are already present, although to a lower extent, in fetal liver, but they are functionally uncoupled by the extravesicular orientation of the catalytic subunit.

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