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.

Investigation of the determinative state of the mouse inner cell mass

Development ◽  
1975 ◽  
Vol 33 (4) ◽  
pp. 979-990
Author(s):  
J. Rossant
Keyword(s):  
Inner Cell Mass ◽  
Cell Mass ◽  
In Utero ◽  
Glucose Phosphate Isomerase ◽  
Trophoblast Cells ◽  
Electrophoretic Variants ◽  
Glucose Phosphate

Inner cell masses (ICMs) were dissected from 3½- and 4½-day blastocysts and cultured in contact with 2½-day morulae. Blastocysts and morulae were homozygous for different electrophoretic variants of the enzyme glucose phosphate isomerase (GPI). Aggregation of ICMs and morulae was observed, and such aggregates were able to form blastocysts in vitro and morphologically normal foetuses in utero. GPI analysis of these conceptuses revealed that most were chimaeric. However, donor ICM-type isozyme was only detected in the embryonic and extra-embryonic fractions of the chimaeras and never in the trophoblastic fraction. Thus, ICM cells appear unable to form trophoblast derivatives even when exposed to ‘outside’ conditions as experienced by developing trophoblast cells. This is evidence that ICM cells, although not overtly differentiated, are determined by 3½ days.

Polymorphism in morels: isozyme electrophoretic analysis

1996 ◽  
Vol 42 (8) ◽  
pp. 819-827 ◽  
Author(s):  
Daniel Wipf ◽  
Jean-Philippe Bedell ◽  
Bernard Botton ◽  
Jean Charles Munch ◽  
François Buscot
Keyword(s):  
Superoxide Dismutase ◽  
Glutamine Synthetase ◽  
Glutamate Dehydrogenase ◽  
Phylogenetic Relationships ◽  
Aspartate Aminotransferase ◽  
Electrophoretic Analysis ◽  
Glucose Phosphate Isomerase ◽  
Glucose Phosphate ◽  
Morchella Esculenta ◽  
Isozyme Polymorphism

The aim of this study was to assess whether isozyme polymorphism in different members of the Morchellaceae could be used to improve the systematics in this fungal group and to characterize intraspecific crossings between monosporal strains in Morchella esculenta. For this purpose, isozyme electrophoretic analysis of the following enzymes was performed: glutamine synthetase, NAD–glutamate dehydrogenase, NADP–glutamate dehydrogenase, aspartate aminotransferase, malate dehydrogenase, NAD–glyceraldehyde phosphate dehydrogenase, glucose phosphate isomerase, and superoxide dismutase. The analyses allowed discrimination at the inter- or intra-specific levels and could help to establish a method of identification for strains in the Morchellaceae. To a certain extent they appeared to be suitable to analyze interactions of monosporal strains of Morchella esculenta in pairing experiments. The polymorphism shown in this study was consistent with the phylogenetic relationships between the investigated strains only at the genus level.Key words: isozyme analysis, electrophoresis, Morchella sp., polymorphism.

scholarly journals Origin of the ectoplacental cone and secondary giant cells in mouse blastocysts reconstituted from isolated trophoblast and inner cell mass

Development ◽  
1973 ◽  
Vol 30 (3) ◽  
pp. 561-572
Author(s):  
R. L. Gardner ◽  
V. E. Papaioannou ◽  
S. C. Barton
Keyword(s):  
Cell Transformation ◽  
Inner Cell Mass ◽  
Cell Mass ◽  
Giant Cells ◽  
Glucose Phosphate Isomerase ◽  
Electrophoretic Variants ◽  
Decidual Tissue ◽  
Glucose Phosphate ◽  
Donor Type ◽  
Ectoplacental Cone

1. Inner cell mass (ICM) and trophoblast tissue were isolated from 3½-day post-coitum mouse blastocysts that were homozygous for different electrophoretic variants of the enzyme glucose phosphate isomerase (GPI). Blastocysts were reconstituted from these tissues, transferred to pseudo-pregnant recipients and allowed to develop to the early somite stage. 2. The embryo plus membranes and trophoblast were dissected and typed separately for GPI. 3. Contamination of trophoblast with maternal decidual tissue was quantified. 4. The trophoblast of the implanted embryos was almost exclusively of the trophoblastdonor GPI type. The embryos plus membranes were mainly of the ICM-donor type but most also showed a substantial proportion of trophoblast-donor type. 5. It is argued that the ICM controls trophoblast proliferation by inhibiting giant cell transformation of adjacent trophoblast cells rather than through making a significant cellular contribution.

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.

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)

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