scholarly journals GPI expression in female germ cells of the mouse

1981 ◽  
Vol 37 (3) ◽  
pp. 303-309 ◽  
Author(s):  
Anne McLaren ◽  
Mia Buehr

SUMMARYThe genetically determined oocyte-specific expression of glucose-phosphate isomerase activity in the mouse is first apparent at 6 to 7 days after birth, and occurs in XO as well as in XX oocytes. The regulator locus that controls oocyte-specific expression shows the same linkage relations as the structural gene, suggesting that both form part of a Gpi-1 gene complex.

1984 ◽  
Vol 44 (2) ◽  
pp. 169-181 ◽  
Author(s):  
John D. West ◽  
Graham Fisher

The dimeric enzyme glucose phosphate isomerase (GPI-1) is regulated in oocytes by a cis-acting temporal gene (Gpi-1t) that maps close to the structural gene (Gpi-1s). Quantitative cellulose acetate electrophoresis of GPI-1 allozymes from unfertilized eggs produced by various Gpi-1sa / Gpi-1sb heterozygous females revealed a new Gpi-1t allele that we have designated Gpi-1tc. This allele is present in 101/H mice and a partially congenie stock that carries the Gpi-lsa gene derived from the AKR strain. We have confirmed that Gpi-1tc is closely linked to Gpi-1s and that it is cis-acting. It produces higher levels of GPI-1 in unfertilized eggs than the other two Gpi-lt alleles that are known (Gpi-1ta and Gpi-1tb) but has no effect on GPI-1 in somatic tissues or spermatozoa. This new Gpi-1t allele represents a third developmental programme for GPI-1 expression in oocytes.


1989 ◽  
Vol 4 (1) ◽  
pp. 82-85 ◽  
Author(s):  
John D. West ◽  
Jean H. Flockhart ◽  
Roslyn R. Angell ◽  
Stephen G. Hillier ◽  
Samuel S. Thatcher ◽  
...  

1977 ◽  
Vol 11 (11) ◽  
pp. 1123-1129 ◽  
Author(s):  
A Kahn ◽  
J P M Van Biervliet ◽  
J L Vives-Corrons ◽  
D Cottreau ◽  
G E J Staal

Development ◽  
1995 ◽  
Vol 121 (3) ◽  
pp. 779-783 ◽  
Author(s):  
Y. Kato ◽  
Y. Tsunoda

Chimeric embryos between fertilized eggs from F1 (C57BL × CBA) and 15.5-16.5 days post coitum (dpc) male fetal germ cells (FGCs) from CD-1 strain (glucose phosphate isomerase, Gpi-1a/a) mice were produced by nuclear transfer. Briefly, a single FGC was fused with enucleated oocytes and activated, and the reconstituted oocytes were cultured to the 2-cell stage. The nucleus from the reconstituted 2-cell embryos was then transferred into an enucleated blastomere of the same stage embryos derived from F1 mice to produce chimeric embryos. The reconstituted 2-cell embryos, which synchronously divided to the 4-cell stage after treatment with nocodazole, were further cultured in vitro. Compacted morula and blastocysts were transferred to the uteri of pseudopregnant female mice. Some recipients were allowed to develop to term and the others were killed at mid gestation to analyze the contribution of donor FGC-derived cells. Survival to term was low with no chimeric animals. Glucose phosphate isomerase (GPI) analysis at midgestation revealed that some conceptuses had chimerism in the fetuses, trophoblast and yolk sac at day 10.5 of pregnancy. The contribution of donor cells was 37–47%, 19–65% and 12–63%, respectively. It was concluded that the nucleus from 15.5-16.5 dpc male fetal germ cells had the potency to develop into fetus, trophoblast and yolk sac after serial nuclear transfer with oocytes and fertilized embryos. The reason for the low viability of chimeric embryos is discussed.


Gerontology ◽  
1985 ◽  
Vol 31 (5) ◽  
pp. 315-320 ◽  
Author(s):  
Carol M. Warner ◽  
Carol J. Briggs ◽  
Doris Balinsky ◽  
Terry E. Meyer

Development ◽  
1989 ◽  
Vol 107 (3) ◽  
pp. 465-472
Author(s):  
J.D. West ◽  
J.H. Flockhart

We have compared mouse embryos of three heterozygous, congenic genotypes (with high, medium and low levels of oocyte-coded glucose phosphate isomerase (GPI-1) activity respectively) to test whether 1) the survival time of oocyte-coded GPI-1 activity in the early embryo is affected by its activity level in the oocyte and 2) whether embryo-coded GPI-1 is detected earlier in embryos that inherit low levels of oocyte-coded GPI-1. The oocyte-coded GPI-1 was entirely GPI-1A allozyme in the high and medium groups but was the less stable GPI-1C allozyme in the low group. We determined total GPI-1 activity and the ratio of different GPI-1 allozymes in early embryos and calculated the activity of oocyte-coded and embryo-coded GPI-1. In all three groups, the oocyte-coded enzyme activity remained at a more or less constant level for the first 21 1/2 days. Some oocyte-coded GPI-1 remained in 4 1/2 day embryos from the high and medium groups but was gone by 5 1/2 days. Very little remained in 4 1/2 day embryos that inherited low levels of a less stable form of the enzyme (GPI-1C allozyme). Despite a 4- to 5-fold difference in initial oocyte-coded GPI-1 activity, no differences were seen among the three genotypically distinct groups of embryos in the time of activation of the embryonic Gpi-1s genes. The embryo-coded GPI-1 was first detectable in 3 1/2 day compacted morulae in all three groups. The level of oocyte-coded GPI-1, in the high group, when embryo-coded GPI-1 was first detected was higher than the level in the low group at any stage prior to detection of embryo-coded GPI-1.(ABSTRACT TRUNCATED AT 250 WORDS)


1989 ◽  
Vol 54 (1) ◽  
pp. 27-36 ◽  
Author(s):  
John D. West ◽  
Jean H. Flockhart

SummaryThe activity of blood glucose phosphate isomerase (GPI-1) in mice heterozygous for various alleles at the Gpi-1s structural locus (heterozygotes a/b, a/c and b/c) was significantly higher than expected, on the basis of additive inheritance, from the levels in parental homozygotes. Moreover, the GPI-1 activity was higher in a/b heterozygotes than in either parent (heterosis). Studies of heat stability with kidney homogenates revealed that the relative stabilities of GPI-1 dimers was AA > AB > BB > AC ≥ BC > CC. Differences in dimer stabilities in vivo would affect the total GPI-1 levels in heterozygotes and could account for non-additive inheritance but would be insufficient to explain heterosis for GPI-1 activity. Other possible contributing factors include unequal production or stability of monomers, or higher catalytic activity of heterodimers. Monomers could also associate non-randomly but this would not be sufficient to explain heterosis. It is clear that non-additive inheritance patterns may be produced by variants of either structural or regulatory genes.


Biology Open ◽  
2016 ◽  
Vol 5 (5) ◽  
pp. 596-610 ◽  
Author(s):  
Margaret A. Keighren ◽  
Jean H. Flockhart ◽  
John D. West

Genetics ◽  
1983 ◽  
Vol 103 (4) ◽  
pp. 675-689
Author(s):  
Jeffrey R Powell ◽  
Marko Andjelković

ABSTRACT Two polymorphic systems impinging on α-amylase in Drosophila pseudoobscura have been studied in laboratory populations maintained on medium in which the only carbohydrate source was starch (the substrate of amylase) and replicas maintained on medium in which the only carbohydrate source was maltose (the product of amylase). The two polymorphic systems were alleles at the structural gene (Amy) coding for the enzyme (allozymes) and variation in the tissue-specific expression along the adult midgut controlled by several genes. In the seven populations on maltose medium little consistent change was noted in either system. In the seven populations on starch medium, both polymorphisms exhibited selective changes. A midgut pattern of very limited expression of amylase rose in frequency in all starch populations, as did the frequency of the "fast" (1.00) Amy allele. The overall specific amylase activity did not differ between starch-adapted and maltose-adapted flies.—The results, along with previous studies, indicate that when a gene-enzyme system is specifically stressed in laboratory populations, allozymes often exhibit selective differences. Such results make the selectionist hypothesis at least tenable. Furthermore, the fact that both types of polymorphisms responded to selection indicates the role of structural gene vs. gene regulation changes in adaptive evolution is not an either/or question but one of relative roles and interactions.


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