Analysis of glucose-6-phosphate translocase and hexose-6-phosphate phosphohydrolase, the two obligatory components of microsomal glucose-6-phosphatase system, in rat liver.

Hata, Keiko; Kikuchi, Kunimi; Tada, Keiya; Tsuiki, Shigeru

doi:10.1620/tjem.155.173

Cited by 3 publications

(1 citation statement)

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“…Activins are homodimers or heterodimers of the βA or βB subunits of inhibin linked to one another by a single disulfide bond (Hata et al, 1988). Dimerization of these β-subunits gives rise to three forms of activin referred to as activin-A (βAβA), activin-AB (βAβB) and activin-B (βBβB) (Ying, 1988).…”

Section: Introductionmentioning

confidence: 99%

In vitro developmental competence of prepubertal goat oocytes cultured with recombinant activin-A

Hammami

Izquierdo

Catalá

et al. 2014

Animal

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The present study was designed to evaluate the effect of activin-A during the in vitro oocyte maturation (IVM) and in vitro embryo culture (IVC) on nuclear maturation, blastocyst yield and blastocyst quality of prepubertal goat oocytes. In Experiment 1, three groups of oocytes were used during the IVM of prepubertal goat oocytes to determine the optimal concentration of recombinant human activin-A added to the maturation medium. Cumulus-oocyte complexes were matured in an IVM medium containing 0, 10 and 100 ng/ml (groups A0, A10 and A100), fertilized and in vitro cultured using standard procedures. In Experiment 2, the addition of 10 ng/ml activin-A at IVM (A10A0), IVC (A0A10) or IVM + IVC (A10A10) was studied and compared with the control group (A0A0). Results of the first experiment demonstrated that the addition of activin-A yielded similar percentages of maturation (⩽71.0%) and blastocyst formation rates (⩽24.9%) than the control group (A0). Experiment 2 showed that exposure of prepubertal goat oocytes to an IVC medium containing 10 ng/ml activin-A (A0A10) significantly increased the rates of development to the blastocyst stage, as compared with the control group (A0A0) (19.5 ± 2.21% v. 13.1 ± 2.37%, respectively; P < 0.05). With regard to the blastocyst quality, total number of cells, inner cell mass (ICM) and trophectoderm of prepubertal goat embryos produced in the presence of activin-A did not differ significantly among experimental groups. In summary, these results indicate that supplementation of the IVC medium with activin-A enhances embryo development of prepubertal goat oocytes.

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Section: Introductionmentioning

confidence: 99%

In vitro developmental competence of prepubertal goat oocytes cultured with recombinant activin-A

Hammami

Izquierdo

Catalá

et al. 2014

Animal

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Changes in the glucose-6-phosphatase complex in hepatomas

et al. 1993

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Hepatomas tend to have a decreased glucose-6-phosphatase activity. We have observed phenotypic stability for this change in Morris hepatomas transplanted in rats. To determine if this decrease is selective for translocase functions or the hydrolase activity associated with glucose-6-phosphatase, we have compared activities in liver and hepatomas with glucose-6-phosphate or mannose-6-phosphate as substrates and with intact or histone-disrupted microsomes. In five out of seven subcutaneously transplanted rat hepatoma lines, the microsomal mannose-6-phosphatase activity was lower than in preparations from liver of normal or tumor-bearing rats. With liver microsomes and with most hepatoma microsomes, preincubation with calf thymus histones caused a greater increase in mannose-6-phosphatase than in glucose-6-phosphatase activity. In studies with liver and hepatoma microsomes there were similar increases in mannose-6-phosphatase activity with total calf thymus histones and arginine-rich histones. A smaller increase was seen with lysine-rich histones. The effect of polylysine was similar to the action of lysine-rich histones. There was only a small effect with protamine at the same concentration (1 mg/ml). Rat liver or hepatoma H1 histones gave only about half the activation seen with core nucleosomal histones. Our data suggested that microsomes of rat hepatomas tend to have decreased translocase and hydrolase functions of glucose-6-phosphatase relative to activities in untransformed liver.

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