Parental glucose phosphate isomerase activity in three-day mouse embryos

1973 ◽  
Vol 9 (2) ◽  
pp. 187-191 ◽  
Author(s):  
R. L. Brinster
Keyword(s):  
Mouse Embryos ◽  
Glucose Phosphate Isomerase ◽  
Isomerase Activity ◽  
Glucose Phosphate

Genetic differences in glucose phosphate isomerase activity among mouse embryos

Development ◽  
1989 ◽  
Vol 107 (3) ◽  
pp. 465-472
Author(s):  
J.D. West ◽  
J.H. Flockhart
Keyword(s):  
Early Embryo ◽  
Mouse Embryos ◽  
Activity Level ◽  
Stable Form ◽  
Glucose Phosphate Isomerase ◽  
High Group ◽  
Isomerase Activity ◽  
Glucose Phosphate ◽  
Early Embryos ◽  
Low Levels

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)

Glucose phosphate isomerase activity in mouse and human eggs and pre-embryos

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

scholarly journals Genetic and Molecular Mechanisms of the Congenital Defects in Glucose Phosphate Isomerase Activity: Studies of Four Families

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
Keyword(s):  
Molecular Mechanisms ◽  
Congenital Defects ◽  
Glucose Phosphate Isomerase ◽  
Isomerase Activity ◽  
Glucose Phosphate

scholarly journals The transition from oocyte-coded to embryo-coded glucose phosphate isomerase in the early mouse embryo

Development ◽  
1983 ◽  
Vol 78 (1) ◽  
pp. 127-140
Author(s):  
John D. West ◽  
J. F. Green
Keyword(s):  
Cellulose Acetate ◽  
Mouse Embryo ◽  
Mouse Embryos ◽  
Glucose Phosphate Isomerase ◽  
Cellulose Acetate Electrophoresis ◽  
Early Mouse Embryo ◽  
Glucose Phosphate ◽  
Early Mouse

The proportions of glucose phosphate isomerase (GPI-1) allozymes produced by early (Gpi-1sa/Gpi-1sb ♀ × Gpi-1sc/Gpi-1sc ♂)F1 mouse embryos were analysed by quantitative cellulose acetate electrophoresis. Technical controls showed that this system is extremely sensitive, quantitatively reproducible and quite accurate. Genetic controls established that the Gpi-1sa/Gpi-1sb mothers were homozygous for the Gpi-1tb temporal allele, that produces relatively high GPI-1 activity in the oocyte. The oocyte-coded enzyme lasted until about 5½ days post coitum (p.c.) or shortly thereafter. The maternally derived, embryonic Gpi-1s allele was expressed no earlier than the paternally derived allele. This was first expressed between 2½ and 3½ days p.c. In this cross, most of the transition from oocyte-coded to embryo-coded GPI-1 occurred between 2½ and 3½ days p.c.

Glucose Phosphate Isomerase Activity in C57BL/6 and A Mice of Different Ages

Gerontology ◽  
1985 ◽  
Vol 31 (5) ◽  
pp. 315-320 ◽  
Author(s):  
Carol M. Warner ◽  
Carol J. Briggs ◽  
Doris Balinsky ◽  
Terry E. Meyer
Keyword(s):  
Glucose Phosphate Isomerase ◽  
Isomerase Activity ◽  
Glucose Phosphate ◽  
Different Ages

Quantification of the transition from oocyte-coded to embryo-coded glucose phosphate isomerase in mouse embryos

Development ◽  
1986 ◽  
Vol 97 (1) ◽  
pp. 225-237
Author(s):  
John D. West ◽  
Rosemary Leask ◽  
J. F. Green
Keyword(s):  
Gene Expression ◽  
Electrophoretic Analysis ◽  
Mouse Embryos ◽  
Gene Products ◽  
Glucose Phosphate Isomerase ◽  
Electrophoretic Variants ◽  
Glucose Phosphate

A quantitative electrophoretic analysis of glucose phosphate isomerase (GPI-1) allozymes produced by heterozygous Gpi-1sa/Gpi-1sb mouse embryos has enabled us to estimate separately the contributions of GPI-1 enzyme that were (1) oocyte coded, (2) encoded by the embryonic, maternally derived Gpi-1sa allele and (3) encoded by the embryonic, paternally derived Gpi-1sb allele. The oocyte-coded GPI-1 activity is stable until 2½ days and then declines and is exhausted by 5½ to 6½ days post coitum (p.c). The maternally and paternally derived Gpi-1s alleles are probably usually activated synchronously but several possible exceptions were observed. This activation was first detected in 2½-day embryos. Total GPI-1 activity falls to a minimum around 3½ to 4½ days, even though embryonic gene expression has already begun. The profile of oocyte-coded GPI-1 activity is consistent with the suggestion (Harper & Monk, 1983) hat there is a mechanism for the removal of oocyte-coded gene products at around 2½ days p.c. The method of analysis described is applicable to other dimeric enzymes with electrophoretic variants.

scholarly journals Non-additive inheritance of glucose phosphate isomerase activity in mice heterozygous at the Gpi-1s structural locus

1989 ◽  
Vol 54 (1) ◽  
pp. 27-36 ◽  
Author(s):  
John D. West ◽  
Jean H. Flockhart
Keyword(s):  
Catalytic Activity ◽  
Heat Stability ◽  
Glucose Phosphate Isomerase ◽  
Contributing Factors ◽  
Structural Locus ◽  
Relative Stabilities ◽  
Isomerase Activity ◽  
Glucose Phosphate ◽  
Additive Inheritance

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.

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