19 results on '"Engelkamp, D."'
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2. A ROLE FOR PAX6 IN RHOMBIC LIP DERIVED NEURONS
- Author
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Engelkamp, D., Rashbass, P., Seawright, A., and van Heyningen, V.
- Published
- 1999
3. Role of Pax6 in development of the cerebellar system
- Author
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Engelkamp, D., primary, Rashbass, P., additional, Seawright, A., additional, and van Heyningen, V., additional
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- 1999
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4. Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E.
- Author
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Engelkamp, D, primary, Schäfer, B W, additional, Mattei, M G, additional, Erne, P, additional, and Heizmann, C W, additional
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- 1993
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5. Frequenin—A novel calcium-binding protein that modulates synaptic efficacy in the drosophila nervous system
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Pongs, O., primary, Lindemeier, J., additional, Zhu, X.R., additional, Theil, T., additional, Engelkamp, D., additional, Krah-Jentgens, I., additional, Lambrecht, H.-., additional, Koch, K.W., additional, Schwemer, J., additional, Rivosecchi, R., additional, Mallart, A., additional, Galceran, J., additional, Canal, I., additional, Barbas, J.A., additional, and Ferrús, A., additional
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- 1993
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6. Purification and cation binding properties of the recombinant human S100 calcium-binding protein A3, an EF-hand motif protein with high affinity for zinc.
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Föhr, U G, Heizmann, C W, Engelkamp, D, Schäfer, B W, and Cox, J A
- Abstract
The calcium-binding protein S100A3 is an unusual member of the S100 family, characterized by its very high content of Cys. In order to study the biochemical, cation-binding, and conformational properties, we produced and purified the recombinant human protein in Escherichia coli. The recombinant protein forms noncovalent homodimers, tetramers, and polymers in vitro with a subunit molecular weight of 11,712. The Zn(2+)-binding parameters of S100A3 were studied by equilibrium gel filtration and yielded a stoichiometry of four Zn2+ per monomer with a [Zn2+]0.5 of 11 microM and a Hill coefficient of 1.4 at physiological ionic strength. The affinity for Ca2+ is too low to be determined by direct methods (KCa > 10 mM). Ca(2+)- and Zn(2+)-binding can be followed by optical methods: the Trp-45 fluorescence is high in the metal-free form and addition of Zn2+ and Ca2+, but not of Mg2+, leads to a 4-fold quenching. Ca2+ and Zn2+ promote also quite similar conformational changes in the Tyr and Trp environment as monitored by difference spectrophotometry. Fluorescence titrations with Zn2+ confirmed that there is one set of high affinity binding sites with a [Zn2+]0.5 of 8 microM and a Hill coefficient of 1.3. Binding of Zn2+ to a second set of low affinity sites induces protein precipitation. Fluorescence titrations with Ca2+ confirmed the very low affinity of S100A3 for this ion with a [Ca2+]0.5 of 30 mM and slight negative cooperativity. Mg2+ has no effect on this binding curve. Of the 10 Cys residues in S100A3, 5 only are free thiols, and accessible to 5,5'-dithiobis(2-nitro-benzoic acid); they display a high reactivity in the metal-free and Ca2+ form, but a 20-fold lowered reactivity in the Zn2+ form of S100A3. Ca(2+)-binding promotes the formation of a solvent-accessible hydrophobic surface as monitored by the 60-fold fluorescence increase of 2-p-toluidinylnaphthalene-6-sulfonate, whereas Zn2+ has no noticeable influence. Our data indicate that Ca2+ and Zn2+ do not bind to the same sites and that under physiological conditions S100A3 is a Zn(2+)-binding rather than a Ca(2+)-binding protein; nevertheless, very specific conformational changes are introduced by either Ca2+ or Zn2+. Since no Zn(2+)-binding motif of known structure was identified in the primary sequence of S100A3, the results are suggestive for a novel Zn(2+)-binding motif.
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- 1995
7. Transcription factors in disease
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Engelkamp, D
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- 1996
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8. Nuclear envelope localization of LEMD2 is developmentally dynamic and lamin A/C dependent yet insufficient for heterochromatin tethering.
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Thanisch K, Song C, Engelkamp D, Koch J, Wang A, Hallberg E, Foisner R, Leonhardt H, Stewart CL, Joffe B, and Solovei I
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- Animals, Cell Differentiation genetics, Cell Nucleus metabolism, Heterochromatin genetics, Heterochromatin metabolism, Lamin Type A metabolism, Membrane Proteins metabolism, Mice, Nuclear Envelope metabolism, Nuclear Proteins metabolism, Transgenes, Cell Nucleus genetics, Lamin Type A genetics, Membrane Proteins genetics, Nuclear Envelope genetics, Nuclear Proteins genetics
- Abstract
Peripheral heterochromatin in mammalian nuclei is tethered to the nuclear envelope by at least two mechanisms here referred to as the A- and B-tethers. The A-tether includes lamins A/C and additional unknown components presumably INM protein(s) interacting with both lamins A/C and chromatin. The B-tether includes the inner nuclear membrane (INM) protein Lamin B-receptor, which binds B-type lamins and chromatin. Generally, at least one of the tethers is always present in the nuclear envelope of mammalian cells. Deletion of both causes the loss of peripheral heterochromatin and consequently inversion of the entire nuclear architecture, with this occurring naturally in rod photoreceptors of nocturnal mammals. The tethers are differentially utilized during development, regulate gene expression in opposite manners, and play an important role during cell differentiation. Here we aimed to identify the unknown chromatin binding component(s) of the A-tether. We analyzed 10 mouse tissues by immunostaining with antibodies against 7 INM proteins and found that every cell type has specific, although differentially and developmentally regulated, sets of these proteins. In particular, we found that INM protein LEMD2 is concomitantly expressed with A-type lamins in various cell types but is lacking in inverted nuclei of rod cells. Truncation or deletion of Lmna resulted in the downregulation and mislocalization of LEMD2, suggesting that the two proteins interact and pointing at LEMD2 as a potential chromatin binding mediator of the A-tether. Using nuclei of mouse rods as an experimental model lacking peripheral heterochromatin, we expressed a LEMD2 transgene alone or in combination with lamin C in these cells and observed no restoration of peripheral heterochromatin in either case. We conclude that in contrary to the B-tether, the A-tether has a more intricate composition and consists of multiple components that presumably vary, at differing degrees of redundancy, between cell types and differentiation stages., (Copyright © 2016 International Society of Differentiation. Published by Elsevier B.V. All rights reserved.)
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- 2017
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9. LBR and lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation.
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Solovei I, Wang AS, Thanisch K, Schmidt CS, Krebs S, Zwerger M, Cohen TV, Devys D, Foisner R, Peichl L, Herrmann H, Blum H, Engelkamp D, Stewart CL, Leonhardt H, and Joffe B
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- Animals, Gene Expression Profiling, Mice, Myoblasts cytology, Nuclear Envelope metabolism, Lamin B Receptor, Heterochromatin metabolism, Lamin Type A metabolism, Muscle Development, Myoblasts metabolism, Receptors, Cytoplasmic and Nuclear metabolism
- Abstract
Eukaryotic cells have a layer of heterochromatin at the nuclear periphery. To investigate mechanisms regulating chromatin distribution, we analyzed heterochromatin organization in different tissues and species, including mice with mutations in the lamin B receptor (Lbr) and lamin A (Lmna) genes that encode nuclear envelope (NE) proteins. We identified LBR- and lamin-A/C-dependent mechanisms tethering heterochromatin to the NE. The two tethers are sequentially used during cellular differentiation and development: first the LBR- and then the lamin-A/C-dependent tether. The absence of both LBR and lamin A/C leads to loss of peripheral heterochromatin and an inverted architecture with heterochromatin localizing to the nuclear interior. Myoblast transcriptome analyses indicated that selective disruption of the LBR- or lamin-A-dependent heterochromatin tethers have opposite effects on muscle gene expression, either increasing or decreasing, respectively. These results show how changes in NE composition contribute to regulating heterochromatin positioning, gene expression, and cellular differentiation during development., (Copyright © 2013 Elsevier Inc. All rights reserved.)
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- 2013
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10. Offspring after embryo-preserving biopsy of the embryoblast with standard ICSI equipment in mouse blastocysts.
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Dittrich R, Lotz L, Würfel W, Engelkamp D, Döhler M, Maltaris T, Hoffmann I, Mueller A, Beckmann MW, and Oppelt PG
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- Animals, Biopsy, Culture Media, Female, Male, Mice, Mice, Inbred C57BL, Blastocyst cytology, Embryo, Mammalian, Sperm Injections, Intracytoplasmic instrumentation
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Background/aim: Obtaining human embryonic stem cell lines has so far involved destroying the embryos. This has given rise to ethical concerns and is not permitted in most countries. This investigation tested whether removing multiple cells from blastocysts might allow continued embryonic development., Materials and Methods: A total of 40 blastocysts from a black mouse strain were biopsied. The mouse blastocysts were fixed with a holding pipette. The zona pellucida and trophectoderm layer were penetrated with an injection pipette, and cells from the inner cell mass (ICM) were aspirated. The pipette was removed and the ICM cells were transferred into a medium., Results: The blastocysts collapsed after pipette removal and were allowed to regenerate for 6 h. Twenty-four blastocysts recovered, expanded and were implanted into four white surrogate mothers. One surrogate mother gave birth to two black pups., Conclusion: This experiment demonstrates that nondestructive blastocyst biopsy from the ICM is possible in mice.
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- 2011
11. A novel approach to selectively target neuronal subpopulations reveals genetic pathways that regulate tangential migration in the vertebrate hindbrain.
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Benzing K, Flunkert S, Schedl A, and Engelkamp D
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- Animals, Axons metabolism, Cell Movement genetics, Cells, Cultured, Eye Proteins genetics, Eye Proteins metabolism, Gene Expression Regulation, Homeodomain Proteins genetics, Homeodomain Proteins metabolism, Mice, Mice, Transgenic, Models, Animal, PAX6 Transcription Factor, Paired Box Transcription Factors genetics, Paired Box Transcription Factors metabolism, Phenotype, Repressor Proteins genetics, Repressor Proteins metabolism, Signal Transduction genetics, Transcription Factor Brn-3B genetics, Transcription Factor Brn-3B metabolism, Neurons cytology, Rhombencephalon cytology, Rhombencephalon embryology, Vertebrates embryology, Vertebrates genetics
- Abstract
Vertebrate genes often play functionally distinct roles in different subsets of cells; however, tools to study the cell-specific function of gene products are poorly developed. Therefore, we have established a novel mouse model that enables the visualization and manipulation of defined subpopulations of neurons. To demonstrate the power of our system, we dissected genetic cascades in which Pax6 is central to control tangentially migrating neurons of the mouse brainstem. Several Pax6 downstream genes were identified and their function was analyzed by over-expression and knock-down experiments. One of these, Pou4f2, induces a prolonged midline arrest of growth cones to influence the proportion of ipsilaterally versus contralaterally settling neurons. These results demonstrate that our approach serves as a versatile tool to study the function of genes involved in cell migration, axonal pathfinding, and patterning processes. Our model will also serve as a general tool to specifically over-express any gene in a defined subpopulation of neurons and should easily be adapted to a wide range of applications., Competing Interests: The authors have declared that no competing interests exist.
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- 2011
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12. Evidence for an evolutionary conserved role of homothorax/Meis1/2 during vertebrate retina development.
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Heine P, Dohle E, Bumsted-O'Brien K, Engelkamp D, and Schulte D
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- Animals, Cell Death, Cell Division, Chick Embryo physiology, Embryo, Mammalian physiology, In Situ Hybridization, Mice, Myeloid Ecotropic Viral Integration Site 1 Protein, Reverse Transcriptase Polymerase Chain Reaction, Stem Cells cytology, Gene Expression Regulation, Developmental, Homeodomain Proteins genetics, Neoplasm Proteins genetics, Retina embryology
- Abstract
During eye development in D. melanogaster, the TALE-homeodomain protein Homothorax (Hth) is expressed by progenitor cells ahead of the neurogenic wave front, promotes rapid proliferation of these cells and is downregulated before cells exit the cell cycle and differentiate. Here, we present evidence that hth function is partially conserved in vertebrates. Retinal progenitor cells (RPCs) in chicks and mice express two Hth-related proteins, Meis1 and Meis2 (Mrg1), in species-specific temporal sequences. Meis1 marks RPCs throughout the period of neurogenesis in the retina, whereas Meis2 is specific for RPCs prior to the onset of retinal differentiation. Transfection of Meis-inactivating constructs impaired RPC proliferation and led to microphthalmia. RNA-interference-mediated knock-down of expression indicated that progenitor cells expressing Meis1 together with Meis2 proliferate more rapidly than cells expressing Meis1 alone. Transfection of Meis-inactivating constructs reduced the expression of cyclin D1 (Ccnd1) in the eye primordium and co-transfection of cyclin D1 partially rescued RPC proliferation. Collectively, these results suggest that (1) Meis1 and Meis2, similar to hth, maintain retinal progenitor cells in a rapidly proliferating state; (2) they control the expression of some ocular-determination genes and components of the cell cycle machinery; and (3) together with the species-specific differences in Meis1/Meis2 expression, combinatorial expression of Meis family proteins might be a candidate mechanism for the differential regulation of eye growth among vertebrate species.
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- 2008
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13. Isolation and expression pattern of three mouse homologues of chick Rgm.
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Schmidtmer J and Engelkamp D
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- Amino Acid Sequence, Animals, Cell Adhesion Molecules, Neuronal, Central Nervous System embryology, Central Nervous System metabolism, Chickens, DNA, Complementary chemistry, DNA, Complementary genetics, DNA, Complementary isolation & purification, GPI-Linked Proteins, Gene Expression Regulation, Developmental, In Situ Hybridization, Mesencephalon embryology, Mesencephalon metabolism, Mice embryology, Molecular Sequence Data, Phylogeny, Prosencephalon embryology, Prosencephalon metabolism, Rhombencephalon embryology, Rhombencephalon metabolism, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Gene Expression Profiling, Mice genetics, Muscle Proteins genetics, Nerve Tissue Proteins genetics
- Abstract
Growth cones of developing neurons are guided to their targets by attractive and repulsive cues. We have isolated three mouse homologues of the chick 'repulsive guidance molecule', Rgm [Nature 419 (2002) 392], and characterized their expression patterns. RgmA and RgmB are predominantly expressed in the developing and adult central nervous system in distinct patterns with little overlap. The third member of the Rgm gene family, RgmC, shows exclusive expression in the muscle cell lineage. From sequence and expression data, we suggest RgmA to be the mouse orthologue of chick Rgm.
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- 2004
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14. Cloning of three mouse Unc5 genes and their expression patterns at mid-gestation.
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Engelkamp D
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- Amino Acid Sequence, Animals, Caenorhabditis elegans, Cloning, Molecular, Extremities embryology, Eye embryology, In Situ Hybridization, Mice, Molecular Sequence Data, Phylogeny, Protein Structure, Tertiary, RNA, Messenger metabolism, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Tissue Distribution, Caenorhabditis elegans Proteins biosynthesis, Caenorhabditis elegans Proteins genetics, Gene Expression Regulation, Developmental, Receptors, Cell Surface biosynthesis, Receptors, Cell Surface genetics
- Abstract
The Caenorhabditis elegans gene unc-5 and it's vertebrate homologues are Netrin receptors. In this study, I report the cloning of three mouse Unc5 family members, namely, Unc5h1, Unc5h2 and Unc5h4. Furthermore, a comparative expression analysis is presented with Unc5h3, deleted in colorectal cancer and Netrin-1. Transcript distribution is studied during early eye development, mammary bud formation, vascularisation, and limb development. The most widely expressed Unc5 family member is Unc5h2 and it's mRNA is observed during early blood vessel formation, in the semicircular canal and in a dorsal to ventral gradient in the retina. Unc5h1 expression is restricted to the central nervous system, whereas, sites of Unc5h4 expression are in the developing limb and mammary gland.
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- 2002
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15. Defect of tyrosine hydroxylase-immunoreactive neurons in the brains of mice lacking the transcription factor Pax6.
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Vitalis T, Cases O, Engelkamp D, Verney C, and Price DJ
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- Animals, Brain cytology, Catecholamines physiology, Cell Division, DNA-Binding Proteins deficiency, DNA-Binding Proteins genetics, Eye Proteins, Hypothalamus physiology, Mice, Mice, Knockout, Neurons cytology, Organ Specificity, PAX6 Transcription Factor, Paired Box Transcription Factors, Repressor Proteins, Substantia Nigra physiology, Telencephalon physiology, Thalamus physiology, Transcription Factors deficiency, Transcription Factors genetics, Brain abnormalities, Brain embryology, DNA-Binding Proteins metabolism, Embryonic and Fetal Development, Homeodomain Proteins, Neurons physiology, Transcription Factors metabolism, Tyrosine 3-Monooxygenase metabolism
- Abstract
In the CNS, the lack of the transcription factor Pax6 has been associated with early defects in cell proliferation, cell specification, and axonal pathfinding of discrete neuronal populations. In this study, we show that Pax6 is expressed in discrete catecholaminergic neuronal populations of the developing ventral thalamus, hypothalamus, and telencephalon. In mice lacking Pax6, these catecholaminergic populations develop abnormally: those in the telencephalon are reduced in cell number or absent, whereas those in the ventral thalamus and hypothalamus are greatly displaced and densely packed. Catecholaminergic neurons of the substantia nigra (SN) and the ventral tegmental area (VTA) do not express Pax6 protein. Nevertheless, mice lacking Pax6 display an altered pathfinding of SN-VTA projections: instead of following the route of the medial forebrain bundle ventrally, most of the SN-VTA projections are deflected dorsorostrally at the pretectal-dorsal thalamic transition zone and in the dorsal thalamic alar plate. Moreover, some catecholaminergic neurons are displaced dorsally to an ectopic location at the pretectal-dorsal thalamic transition zone. Interestingly, from the pretectal-dorsal thalamic to the dorsal thalamic-ventral thalamic transition zones, mice lacking Pax6 display an ectopic ventral to dorsal expansion of the chemorepellant/chemoattractive molecule, Netrin-1. This may be responsible for both the altered pathway of catecholaminergic fibers and the ectopic location of catecholaminergic neurons in this region.
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- 2000
16. Influence of PAX6 gene dosage on development: overexpression causes severe eye abnormalities.
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Schedl A, Ross A, Lee M, Engelkamp D, Rashbass P, van Heyningen V, and Hastie ND
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- Animals, Base Sequence, Eye Proteins, Gene Expression Regulation, Developmental genetics, Genetic Complementation Test, Humans, In Situ Hybridization, Fluorescence, Mice, Mice, Inbred C57BL, Mice, Inbred CBA, Mice, Transgenic, Molecular Sequence Data, PAX6 Transcription Factor, Paired Box Transcription Factors, Phenotype, Repressor Proteins, Transgenes physiology, DNA-Binding Proteins genetics, Eye Abnormalities genetics, Gene Dosage, Homeodomain Proteins
- Abstract
Aniridia in man and Small eye in mice are semidominant developmental disorders caused by mutations within the paired box gene PAX6. Whereas heterozygotes suffer from iris hypoplasia, homozygous mice lack eyes and nasal cavities and exhibit brain abnormalities. To investigate the role of gene dosage in more detail, we have generated yeast artificial chromosome transgenic mice carrying the human PAX6 locus. When crossed onto the Small eye background, the transgene rescues the mutant phenotype. Strikingly, mice carrying multiple copies on a wild-type background show specific developmental abnormalities of the eye, but not of other tissues expressing the gene. Thus, at least five different eye phenotypes are associated with changes in PAX6 expression. We provide evidence that not only reduced, but also increased levels of transcriptional regulators can cause developmental defects.
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- 1996
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17. Subnuclear localization of WT1 in splicing or transcription factor domains is regulated by alternative splicing.
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Larsson SH, Charlieu JP, Miyagawa K, Engelkamp D, Rassoulzadegan M, Ross A, Cuzin F, van Heyningen V, and Hastie ND
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- Animals, Antibody Specificity, Autoantigens isolation & purification, Base Sequence, Cell Line, Cell Nucleus drug effects, Cell Nucleus ultrastructure, DNA-Binding Proteins genetics, DNA-Binding Proteins immunology, Dactinomycin pharmacology, Genes, Tumor Suppressor genetics, Immunohistochemistry, Kidney cytology, Kidney embryology, Male, Mice, Molecular Sequence Data, RNA Precursors metabolism, RNA, Messenger metabolism, Testis cytology, Testis embryology, Transcription Factors genetics, Transcription Factors immunology, Transcription, Genetic, WT1 Proteins, Wilms Tumor etiology, Wilms Tumor genetics, snRNP Core Proteins, Alternative Splicing, Cell Compartmentation, Cell Nucleus chemistry, DNA-Binding Proteins isolation & purification, Ribonucleoproteins, Small Nuclear, Spliceosomes chemistry, Transcription Factors isolation & purification
- Abstract
WT1 is a tumor suppressor gene with a key role in urogenital development and the pathogenesis of Wilms' tumor. Two alternative splice sites in the WT1 transcript allow the gene to encode four proteins. These carry four Krüppel-type zinc fingers and to date have primarily been implicated in transcriptional control of genes involved in growth regulation. However, here we demonstrate colocalization of WT1 with splicing factors in the fetal kidney and testis and in expressing cell lines. Using immunoprecipitation, we show that two WT1 isoforms directly associate with one or a limited number of components in the spliceosomes and coiled bodies. Moreover, COS cell expression studies suggest that alternative splicing within the WT1 zinc finger region determines whether the protein localizes mainly with splicing factors or with DNA in transcription factor domains in the nucleus. We propose that WT1 plays roles in posttranscriptional processing of RNA as well as in transcription.
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- 1995
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18. Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family.
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Schäfer BW, Wicki R, Engelkamp D, Mattei MG, and Heizmann CW
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- Base Sequence, Chromosome Mapping, Chromosomes, Artificial, Yeast, DNA Primers, Humans, Molecular Sequence Data, Chromosomes, Human, Pair 1, Multigene Family, S100 Proteins genetics, Terminology as Topic
- Abstract
S100 proteins are low-molecular-weight calcium-binding proteins of the EF-hand superfamily and appear to be involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. More than 10 members of the S100 protein family have been described from human sources so far. We have now isolated a YAC clone from human chromosome 1q21, on which 9 different genes coding for S100 calcium-binding proteins could be localized. Moreover, we have mapped the gene coding for S100P to human chromosome 4p16 and thereby completed the chromosomal assignments of all known human S100 genes. The clustered organization of S100 genes in the 1q21 region allows us to introduce a new logical nomenclature for these genes, which is based on the physical arrangement on the chromosome. The new nomenclature should facilitate and further the understanding of this protein family and be easily expandable to other species.
- Published
- 1995
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19. S100 alpha, CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart.
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Engelkamp D, Schäfer BW, Erne P, and Heizmann CW
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- Amino Acid Sequence, Animals, Base Sequence, Blotting, Northern, Cattle, Cloning, Molecular, Gene Expression, Gene Library, Heart Ventricles, Humans, Molecular Sequence Data, Oligodeoxyribonucleotides, Polymerase Chain Reaction, RNA genetics, RNA isolation & purification, RNA, Messenger genetics, Rats, Restriction Mapping, S100 Calcium Binding Protein A6, S100 Calcium-Binding Protein A4, Sequence Homology, Amino Acid, Calcium-Binding Proteins genetics, Cell Cycle Proteins, Myocardium metabolism, S100 Proteins
- Abstract
Elevated levels of intracellular calcium are a major cause of myocardial dysfunction. To find possible mediators of the deregulated calcium we searched for EF-hand calcium-binding proteins of the S100 family. By PCR technology we identified three members of the S100 protein family (S100 alpha, CACY, and CAPL) in the human heart. We cloned the corresponding cDNAs and examined their expression levels in various human tissues by Northern blot analysis. All three proteins are expressed at high levels in the human heart. Whereas CACY and CAPL mRNAs are expressed ubiquitously, S100 alpha mRNA is restricted to heart, skeletal muscle, and brain. Interestingly, the expression pattern of S100 alpha, CACY, and CAPL in human tissues differs significantly from that in rodent tissues.
- Published
- 1992
- Full Text
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