INHERITANCE OF SERUM ESTERASES HAVING DIFFERENT ELECTROPHORETIC PATTERNS: Among Inbred Strains of Mice

Popp, Raymond A.; Popp, Diana M.

doi:10.1093/oxfordjournals.jhered.a107140

Cited by 100 publications

(19 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2 illustrates that these expectations are realized. Intermediate hybrid bands are not seen with F isozyme, in agreeirient with observations with Es-1 (15,16).…”

Section: Methodssupporting

confidence: 90%

Detection of Maternal Esterase in Mouse Embryonic Tissues

Sherman¹,

Chew²

1972

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

A genetic variant of esterase in mice is used to demonstrate for the first time that an enzyme of maternal origin is taken up intracellularly by two mid-gestation tissues derived from the embryo: trophoblast and yolk sac (visceral endoderm). Although other alternatives are still possible, it is likely that the esterase is transported from the mother to the trophoblast via the serum. If so, the phenomenon is selective, since at least one other prominent serum esterase is not found in trophoblast or yolk sac cells. The enzyme has not been detected in the embryo proper, even at very. late stages of pregnancy.Trophoblast cellsrdeveloping from blastocysts implanted under the kidney capsule of a male mouse also appear to have the ability to take up host esterase. Efforts to demonstrate uptake of the enzyme by trophoblast cells in blastocyst cultures have been unsuccessful.A mammalian embryo develops in the reproductive tract, and as such is constantly exposed to, and protected by, the maternal environment. Preimplantation embryos removed from the reproductive tract and placed in ectopic sites can implant in the foreign tissue and proceed to develop normally for several days (1-4). Blastocysts maintained in culture medium are able to give rise to some cell types that are at least partially differentiated: trophoblast (5-7), yolk sac (7, 8), and part of the embryo proper (8). It would thus appear that signals for early differentiation need not come from the mother. There is, however, a great advantage to be gained from development in the reproductive tract, namely the selective passage of molecules and macromolecules from mother to fetus. By this phenomenon, for example, the fetus is provided with maternal antibodies that protect it after birth until its own immune system is functional (9). Studies on the passage in mice of injected serum proteins from the maternal bloodstream into embryonic tissues late in pregnancy have revealed that some fractions (e.g., human IgG) can cross the placental barrier more easily than others (e.g., human albumin) (10, 11). The studies described here are the first to illustrate that an enzyme naturally present in the maternal blood penetrates the embryonic tissues of the placenta in the first half of gestation. METHODS AND MATERIALSThe following strains of mice were used in this study: Swiss PO, C57BI/6, SWR/J, SJL/J, C57B1/6J, and C57B1/6J x DBA/2J hybrids. The latter four strains were obtained from the Jackson Laboratory, Bar Harbor, Me. Mice were randommated when postimplantation embryos were required. Preimplantation blastocysts were collected from females superovulated (12) before mating. The day on which vaginal plugs, indicating successful matings, were detected is referred to as the first day of pregnancy. The following tissues were dissected (6) on the 10th or 11th days of gestation: the outer or trophoblast layer of the fetal placenta, containing mainly trophoblast cells, but also Reichert's membrane, parietal endoderm, and, at later stages, part of the allantois; the vis...

show abstract

“…2 illustrates that these expectations are realized. Intermediate hybrid bands are not seen with F isozyme, in agreeirient with observations with Es-1 (15,16).…”

Section: Methodssupporting

confidence: 90%

Detection of Maternal Esterase in Mouse Embryonic Tissues

Sherman¹,

Chew²

1972

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…For instance, using plasma samples at pH 6.4, we usually observed 3 esterase components descending from the Es-l zone. These bands were not detectable simultaneously with the Es-I variation described by Popp & Popp (1962). The CPB-Ft strain showed slightly slower migrating bands, while the CPB-V strains possessed a 4th (slowest) band.…”

Section: Discussionmentioning

confidence: 79%

Identification and genetic monitoring of mouse inbred strains using biochemical polymorphisms

Groen

1977

Lab Anim

View full text Add to dashboard Cite

53 inbred strains and substrains of mice from 3 institutes in The Netherlands were examined at 12 chromosome loci coding body protein-polymorphism (Es-1, Es-2, Es-3, Es-S, Gpi-1, Hbb, Id-1, Ldr-1, Mpi-1, Mup-1, pgm-1, Trf). The allelic variation at 7 loci could be detected simultaneously. Within each institute most strains showed a unique combination of alleles at the 12 loci involved. Some nominally similar (sub)strains showed allelic divergence. One strain showed allelic variation at 4 loci. These findings emphasize the possibility and the necessity of monitoring the genetic purity of inbred strains of mice. A routine monitoring scheme using body protein-polymorphisms is proposed.

show abstract

“…Up to 1977, five genetic variants of mouse hemoglobin a chains were known from studies of hemoglobin solubility and polypeptide sequence analyses (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20) …”

Section: Glymentioning

confidence: 99%

“…We have shown previously (1) that isoelectric focusing-a method for the separation of proteins based upon differences in their isoelectric points-can resolve at least some proteins that differ from one another only by neutral amino acid substitutions. That demonstration relied upon the availability of a variety of mouse hemoglobins (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14) of known amino acid sequence (15)(16)(17)(18)(19)(20) [and nowknown gene sequence (21,22)] that differ from one another only by one to four substitutions of neutral amino acids (valine, isoleucine, serine, threonine, asparagine, glycine, and alanine), Although several additional a-globin genotypes have been discovered since then (23)(24)(25)(26), all of the naturally occurring variant chains subsequently characterized by protein sequence analysis also have differed in neutral amino acids only (Table 1). That no charge variation among mouse a-globins has been found in nature is consistent with the deleterious effect that charged amino acid substitutions generally have in human hemoglobin a chains.…”

mentioning

confidence: 99%

Detection of neutral amino acid substitutions in proteins.

Whitney¹,

Cobb²,

Popp³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The field of biochemical genetics relies heavily upon the detection by electrophoresis of genetically determined variants of proteins. Most of these variants differ by substitutions that involve charged amino acids. Genetic variants of another large class, ones that involve substitutions among neutral amino acids, are not easily detected and are often ignored. Ampholyte isoelectric focusing in some cases can separate proteins indistinguishable by standard electrophoresis, including genetic variants of mouse hemoglobins that differ only by neutral amino acid substitutions. A revolutionary variation of isoelectric focusing, in which gradients covering a small pH range are fixed into place in a polyacrylamide gel, provides greater resolution of these nearly identical proteins. Mouse hemoglobin tetramers that differ only by the substitution of alanine for glycine in the a-globin chains are resolved by several millimeters with the new technique; by comparison, these tetramers are imperfectly resolved on a standard pH 7-9 isoelectric focusing gel. This improved technique of isoelectric focusing was used to identify a variety of previously unreported genetic variants of mouse hemoglobin ar chains. Immobilized gradients tailored to the requirements of the proteins being analyzed will extend greatly the ranges of protein variations that can be easily recognized for diverse applications, including genetic quality-control analyses and in studies of genetics, mutagenesis, and evolution.Standard electrophoretic techniques are often suitable for differentiating among proteins that differ from one another by the substitution of charged amino acids but generally are not capable of separating proteins that differ only by neutral amino acid substitutions. We have shown previously (1) that isoelectric focusing-a method for the separation of proteins based upon differences in their isoelectric points-can resolve at least some proteins that differ from one another only by neutral amino acid substitutions. That demonstration relied upon the availability of a variety of mouse hemoglobins (2-14) of known amino acid sequence (15)(16)(17)(18)(19)(20) [and nowknown gene sequence (21,22)] that differ from one another only by one to four substitutions of neutral amino acids (valine, isoleucine, serine, threonine, asparagine, glycine, and alanine), Although several additional a-globin genotypes have been discovered since then (23)(24)(25)(26)

show abstract

INHERITANCE OF SERUM ESTERASES HAVING DIFFERENT ELECTROPHORETIC PATTERNS: Among Inbred Strains of Mice

Cited by 100 publications

References 3 publications

Detection of Maternal Esterase in Mouse Embryonic Tissues

Detection of Maternal Esterase in Mouse Embryonic Tissues

Identification and genetic monitoring of mouse inbred strains using biochemical polymorphisms

Detection of neutral amino acid substitutions in proteins.

Contact Info

Product

Resources

About