References of "Balling, Rudi 50000566"
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See detailA family of octamer-specific proteins present during mouse embryogenesis: evidence for germline-specific expression of an Oct factor.
Scholer, H. R.; Hatzopoulos, A. K.; Balling, Rudi UL et al

in EMBO Journal (1989), 8(9), 2543-50

We have analysed various adult organs and different developmental stages of mouse embryos for the presence of octamer-binding proteins. A variety of new octamer-binding proteins were identified in ... [more ▼]

We have analysed various adult organs and different developmental stages of mouse embryos for the presence of octamer-binding proteins. A variety of new octamer-binding proteins were identified in addition to the previously described Oct1 and Oct2. Oct1 is ubiquitously present in murine tissues, in agreement with cell culture data. Although Oct2 has been described as a B-cell-specific protein, similar complexes were also found with extracts from brain, kidney, embryo and sperm. In embryo and brain at least two other proteins, Oct3 and Oct7, are present. A new microextraction procedure allowed the detection of two maternally expressed octamer-binding proteins, Oct4 and Oct5. Both proteins are present in unfertilized oocytes and embryonic stem cells, the latter containing an additional protein, Oct6. Whereas Oct4 was not found in sperm or testis, it is expressed in male and female primordial germ cells. Therefore Oct4 expression is specific for the female germline at later stages of germ cell development. Our results indicate that a family of octamer-binding proteins is present during mouse development and is differentially expressed during early embryogenesis. Protease clipping experiments of Oct4 and Oct1 suggest that both proteins contain similar DNA-binding domains. [less ▲]

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See detailCraniofacial abnormalities induced by ectopic expression of the homeobox gene Hox-1.1 in transgenic mice.
Balling, Rudi UL; Mutter, G.; Gruss, P. et al

in Cell (1989), 58(2), 337-47

Hox-1.1 is a murine homeobox-containing gene expressed in a time- and cell-specific manner during embryogenesis. We have generated transgenic mice that ectopically express Hox-1.1 from the chicken beta ... [more ▼]

Hox-1.1 is a murine homeobox-containing gene expressed in a time- and cell-specific manner during embryogenesis. We have generated transgenic mice that ectopically express Hox-1.1 from the chicken beta-actin promoter. In these mice Hox-1.1 expression was changed to an almost ubiquitous pattern. Ectopic expression of Hox-1.1 leads to death of the transgenic animals shortly after birth and is associated with multiple craniofacial anomalies, such as cleft palate, open eyes at birth, and nonfused pinnae. This phenotype is similar to the effects seen after systemic administration of retinoic acid during gestation. This suggests that retinoic acid embryopathy and the specific developmental defects caused by ectopic expression of a potential developmental control gene share a common pathogenic mechanism. [less ▲]

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See detailTranscriptional activity of the octamer motif in embryonic stem cells and preimplantation embryos
Schöler, H. R.; Balling, Rudi UL; Hatzopoulos, A. K. et al

in Hormones and Cell Regulation (1989), 198(14), 91-95

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See detailOctamer binding proteins confer transcriptional activity in early mouse embryogenesis.
Scholer, H. R.; Balling, Rudi UL; Hatzopoulos, A. K. et al

in EMBO Journal (1989), 8(9), 2551-7

Oct4 and Oct5 are two mouse maternally expressed proteins binding to the octamer motif. Both are found in unfertilized oocytes and embryonic stem cells, whereas Oct4 is also found in primordial germ cells ... [more ▼]

Oct4 and Oct5 are two mouse maternally expressed proteins binding to the octamer motif. Both are found in unfertilized oocytes and embryonic stem cells, whereas Oct4 is also found in primordial germ cells. In this study, the activity of the octamer motif was analysed in two embryonic stem cell lines containing Oct4 and Oct5, the teratocarcinoma-derived cell line F9 and the blastocyst-derived cell line D3. It is known that oligomerization of the octamer motif creates a powerful B-cell specific enhancer. As shown here, this oligomerized transcriptional element is also a very strong enhancer in F9 and D3 embryonic stem cells. After differentiation of the stem cells, both enhancer activity and the amount of the octamer binding proteins decrease. An intact octamer stimulates heterologous promoters in embryonic stem cells, whereas mutations in the octamer motif abolish transcriptional stimulation and binding of the octamer factors. The use of transgenic embryos demonstrates transcriptional activation in the inner cell mass but not in the trophoblast of blastocysts. The results indicate that Oct4 and Oct5 are active early in mouse development. [less ▲]

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See detailStructure, expression and chromosomal localization of Zfp-1, a murine zinc finger protein gene.
Chowdhury, K.; Dietrich, S.; Balling, Rudi UL et al

in Nucleic Acids Research (1989), 17(24), 10427-38

Zinc finger proteins (Zfp) are encoded by a large family of genes present in many organisms including yeast and human. Some of them are transcriptional activators and bind specifically to DNA by zinc ... [more ▼]

Zinc finger proteins (Zfp) are encoded by a large family of genes present in many organisms including yeast and human. Some of them are transcriptional activators and bind specifically to DNA by zinc mediated folded structures commonly known as zinc fingers. The Drosophila Kruppel (Kr) is a segmentation gene and encodes a zinc finger protein. Using a probe from the finger domain of Kr, we have isolated a structurally related gene Zfp-1 from the mouse. In this paper, we report the complete nucleotide sequence of two cDNA clones and the amino acid sequence deduced from them. The putative Zfp-1 protein contains in addition to 7 zinc fingers, two helix-turn-helix motifs. During murine embryogenesis, the Zfp-1 was found to express at a peak level in day 12 embryos. The ubiquitously expressed Zfp-1 gene is located in the 16q region on mouse chromosome 8, between the uvomorulin and the tyrosine amino transferase genes. [less ▲]

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See detailMurine Genes with homology to Drosophila segmentation genes.
Dressler, G. R.; Deutsch, U; Balling, Rudi UL et al

in Development (1988), 0(104), 181-186

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See detailA mouse gene homologous to the Drosophila gene caudal is expressed in epithelial cells from the embryonic intestine.
Duprey, P.; Chowdhury, K.; Dressler, G. R. et al

in Genes and Development (1988), 2(12A), 1647-54

A mouse gene, Cdx-1, was isolated from an embryonic cDNA library using a Drosophila caudal gene probe. The deduced amino acid sequence of Cdx-1 contains conserved sequence domains along the entire gene ... [more ▼]

A mouse gene, Cdx-1, was isolated from an embryonic cDNA library using a Drosophila caudal gene probe. The deduced amino acid sequence of Cdx-1 contains conserved sequence domains along the entire gene, as well as a highly conserved caudal-type homeo box. A structural comparison suggests a common ancestral origin of mouse Cdx-1 and Drosophila caudal. The expression of Cdx-1 during embryogenesis was analyzed by Northern blotting and in situ hybridization. Cdx-1-specific transcripts are localized in the epithelial lining of the intestines beginning at 14 days' gestation. The expression of Cdx-1 in the intestine continues into adulthood, but cannot be detected in any other tissues. The Cdx-1 gene is the first homeo-box-containing gene expressed in cells derived from the embryonic endoderm. [less ▲]

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See detailundulated, a mutation affecting the development of the mouse skeleton, has a point mutation in the paired box of Pax 1.
Balling, Rudi UL; Deutsch, U.; Gruss, P.

in Cell (1988), 55(3), 531-5

undulated (un) homozygous mice exhibit vertebral malformations along the entire rostro-caudal axis. Pax 1, a murine paired box-containing gene, is expressed in ventral sclerotome cells and later in ... [more ▼]

undulated (un) homozygous mice exhibit vertebral malformations along the entire rostro-caudal axis. Pax 1, a murine paired box-containing gene, is expressed in ventral sclerotome cells and later in intervertebral disks along the entire vertebral column. We localized the Pax 1 gene on chromosome 2 between beta 2-microglobulin and the agouti locus to an area where un maps. DNA analysis of the un mutant revealed a point mutation in a highly conserved part of the paired box of Pax 1, leading to a Gly-Ser replacement. The chromosomal location and the mutation in the paired box of un mice in conjunction with Pax 1 gene expression in wild-type mice implicate a causative role of Pax 1 in generation of the vertebral column. [less ▲]

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See detailDegree of methylation of transgenes is dependent on gamete of origin.
Sapienza, C.; Peterson, A. C.; Rossant, J. et al

in Nature (1987), 328(6127), 251-4

Data derived from both pronuclear transplantation experiments and classical genetic experiments indicate that the maternal and paternal genetic contributions to the mammalian zygote nucleus do not ... [more ▼]

Data derived from both pronuclear transplantation experiments and classical genetic experiments indicate that the maternal and paternal genetic contributions to the mammalian zygote nucleus do not function equivalently during subsequent development. These observations have been interpreted as resulting from differential 'genome imprinting' during male and female gametogenesis. The molecular mechanism responsible for genome imprinting is unknown, but data gathered to date require that the mechanism fulfill at least four criteria: (1) the imprint must be physically linked to the pronucleus; (2) the imprint must persist through DNA replication and cell division; (3) the mechanism must be capable of affecting gene expression; and (4) the mechanism must be capable of switching the identity of the imprint from one sex to the other in successive generations. One molecular mechanism which could satisfy the first three criteria is differential DNA methylation during gametogenesis itself, or before formation of the zygote nucleus during embryogenesis. We present data indicating that the methylation patterns of exogenous DNA sequences in transgenic mice can be changed by switching their gamete of origin in successive generations. These data suggest that DNA methylation can also satisfy the fourth criterion for an imprinting mechanism. [less ▲]

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See detailDirect effects of nicotine on rabbit preimplantation embryos.
Balling, Rudi UL; Beier, H. M.

in Toxicology (1985), 34(4), 309-13

The effects of various concentrations of nicotine on the in vitro development of 1-cell rabbit preimplantation embryos and on the DNA-synthesis of 4-day-old rabbit blastocysts are investigated. Exposure ... [more ▼]

The effects of various concentrations of nicotine on the in vitro development of 1-cell rabbit preimplantation embryos and on the DNA-synthesis of 4-day-old rabbit blastocysts are investigated. Exposure of rabbit preimplantation embryos to concentrations of nicotine higher than 1 X 10(-3) M results in a marked decrease in the in vitro development and in DNA-synthesis. Concentrations of nicotine below 1 X 10(-3) M have no effect on these early embryos. It can be concluded that the concentrations of nicotine which exert a direct embryotoxic effect are higher than the concentrations that may be expected in the blood circulation of humans considered to be "normal smokers". [less ▲]

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See detailOxidative and conjugative metabolism of diethylstilbestrol by rabbit preimplantation embryos.
Balling, Rudi UL; Haaf, H.; Maydl, R. et al

in Developmental Biology (1985), 109(2), 370-4

Five- and six-day-old rabbit preimplantation embryos were found to be capable of metabolizing [3H]diethylstilbestrol (DES) in vitro. Based on the analysis of the metabolites formed during a 24-hr ... [more ▼]

Five- and six-day-old rabbit preimplantation embryos were found to be capable of metabolizing [3H]diethylstilbestrol (DES) in vitro. Based on the analysis of the metabolites formed during a 24-hr incubation period we conclude that these early stage embryos do have active monooxygenase and conjugative activity. The monooxygenase seems to be specific to this early stage of embryonic development. [less ▲]

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See detailInsertion of a bacterial gene into the mouse germ line using an infectious retrovirus vector.
Huszar, D.; Balling, Rudi UL; Kothary, R. et al

in Proceedings of the National Academy of Sciences of the United States of America (1985), 82(24), 8587-91

Using a Moloney leukemia virus vector containing the bacterial neo gene, we demonstrate that retrovirus vectors can be used to introduce genes into the mouse germ line. Infection of preimplantation ... [more ▼]

Using a Moloney leukemia virus vector containing the bacterial neo gene, we demonstrate that retrovirus vectors can be used to introduce genes into the mouse germ line. Infection of preimplantation embryos with the vector MLV-NEO.1 resulted in integration of neo sequences in approximately equal to 10% of the progeny mice. One of these animals, mouse F.2, contained approximately six MLV-NEO.1 proviruses at independent integration sites, each present at less than a single copy per cell. This mosaic mouse transmitted one of these proviruses to her offspring, producing a line of transgenic mice carrying a full-length, unrearranged MLV.NEO.1 provirus at a single chromosomal integration site. Mice homozygous at this MLV-NEO.1 locus have also been produced. No expression of the neo gene has been detected in the transgenic mice, either by screening of primary bone marrow or lung cells for resistance to G418 or by RNA transfer blot analysis of RNA from several tissues. In addition, the neo gene was found to be extensively methylated in the transgenic mice; however, treatment of primary cells with 5-azacytidine did not induce G418 resistance. The inactivity of the MLV-NEO.1 provirus in transgenic mice and potential means of eliciting neo expression under these conditions are discussed. [less ▲]

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See detailAsparagine and glutamine metabolism in chicks.
Coon, C.; Balling, Rudi UL

in Poultry Science (1984), 63(4), 717-29

In a series of four experiments, asparaginase and glutaminase activity was measured in liver and kidney tissue of 7- to 19-day-old male broiler chicks. In Experiment 1, chicks were fed purified amino acid ... [more ▼]

In a series of four experiments, asparaginase and glutaminase activity was measured in liver and kidney tissue of 7- to 19-day-old male broiler chicks. In Experiment 1, chicks were fed purified amino acid diets with 14.8 and 44.6% protein equivalents (PE) with 1, 3, or 5% added sodium bicarbonate. In Experiments 2, 3, and 4 the chicks were fed a 23% protein basal control diet, basal diet containing 5% ammonium chloride, and basal diet containing 5% ammonium chloride with 5 or 10% sodium bicarbonate, asparagine, or glutamine. In Experiments 2 and 4 the chicks were also fed 25, 50, or 75% protein-isolated soy-purified diets. The 44.6% PE diet increased liver and kidney asparaginase activity in chicks as compared to chicks fed a 14.8% PE diet. The addition of sodium bicarbonate to the 44.6% PE amino acid diet decreased the kidney asparaginase activity equivalent to kidney asparaginase activity of chicks fed the 14.8% PE diet. Asparaginase activity increased 4-fold in the kidneys of chicks fed the 23% protein basal diet containing 5% ammonium chloride and the pH of the urine from the chicks was 4.9. Chicks fed basal diets with 5% ammonium chloride plus 10% sodium bicarbonate or asparagine had the same kidney asparaginase activity and urine pH as chicks fed the 23% protein basal control diet. Glutamine added to chick diets containing 5% ammonium chloride did not decrease the kidney asparaginase activity or the urine acidity. Liver asparaginase activity was not increased in acidotic chicks fed diets with 5% ammonium chloride. The asparaginase activity of liver and kidney tissue were both significantly increased in chicks fed 75% protein-isolated soy purified diets and the pH of their urine was 5.6. The increase in liver asparaginase of chicks fed 75% protein or 44.5% PE diets was probably due to an endocrine gluconeogenic response producing increased catabolism of the majority of amino acids. The increase in kidney asparaginase of chicks fed 75% protein, 44.5% PE diets, and 23% protein basal diets with 5% ammonium chloride was primarily related to metabolic acidosis. Phosphate-dependent glutaminase (PDG) activity was localized in chick kidney mitochondria and was heat sensitive (55 C for 30 sec). The phosphate-independent glutaminase (PIG) activity was primarily localized in chick kidney mitochondria but was stable to a temperature of 55 C for 30 sec.(ABSTRACT TRUNCATED AT 400 WORDS) [less ▲]

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See detailEffect Of Dietary Asparagine And Protein-Equivalents In Crystalline Amino-Acid Diets On Asparagine Metabolism In Chicks
Balling, Rudi UL; Coon, C.

in Journal of Nutrition (1981), 111(10), 1749-1756

The effect of dietary asparagine and protein-equivalents from crystalline amino acid mixtures upon asparagine metabolism in chicks were studied. Liver and kidney asparaginase activities were significantly ... [more ▼]

The effect of dietary asparagine and protein-equivalents from crystalline amino acid mixtures upon asparagine metabolism in chicks were studied. Liver and kidney asparaginase activities were significantly increased in chicks fed 44.6% protein-equivalents compared to chicks fed the Illinois chick standard amino acid mixture containing 14.8% protein-equivalents. The asparagine synthetase activity in chick liver and kidney was not significantly changed by protein-equivalents or dietary asparagine. Liver and kidney asparaginase activities in chicks fed 14.8% protein-equivalent standard diets were decreased with increasing levels of dietary asparagine (0,2 and 6%). Kidney asparaginase activities in chicks fed 44.6% protein-equivalents also were decreased with increasing levels of asparagine but liver asparaginase in these chicks was not changed with dietary asparagine. The plasma asparagine concentration was dependent on the amount of dietary asparagine and protein-equivalents. Dietary asparagine increased plasma asparagine in chicks fed 14.8 and 44.6% protein-equivalent diets but plasma asparagine in chicks fed the 14.8% protein-equivalent diet plus 6% asparagine was 3.5 times higher than plasma asparagine in chicks fed the diet containing 44.6% protein-equivalent plus 6% dietary asparagine. Plasma asparagine in chicks fed the 44.6% protein-equivalent diet with 6% asparagine was reduced due to increased asparaginase activity. [less ▲]

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