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  • 1
    Electronic Resource
    Electronic Resource
    Mammary gland-specific hypomethylation ofHpa II sites flanking the bovine αS1-casein gene (1996)
    Springer
    Transgenic research 5 (1996), S. 421-431 
    Details
    ISSN: 1573-9368
    Keywords: bovine αS1-casein gene ; DNA methylation ; transgenic mice ; mammary gland
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the lactating cow, mammary gland-specific hypomethylation occurs at twoHpa II sites in the 5′-flanking region of the αS1-casein gene, and one in the 3′-region. These sites, A, B. and C, are at nucleotide position −1388, −774 and +18034, respectively, relative to the major transcription start site. Site B was hypomethylated when the αS1-casein gene was expressed, and methylated when not expressed. In transgenic mice containing the bovine αS1-casein 5′ and 3′ regulatory elements fused to the human lactoferrin (hLF) cDNA, in some cases similar methylation patterns of sites A and B, as compared to the situation in the cow, were observed. In five mouse lines (out of the seven analysed) expressing the transgene in the milk, site B was hypomethylated in the mammary gland, while it was methylated in liver. In the two other mouse lines, no correlation was found between transgene expression and mammary gland-specific hypomethylation of site B. One of the five mouse lines with transgene expression and showing mammary-gland-specific hypomethylation of site B was studied in detail. In this mouse line, induction of transgene expression preceded hypomethylation of site B.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01980207
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  • 2
    Electronic Resource
    Electronic Resource
    Expression of human lactoferrin in milk of transgenic mice (1994)
    Springer
    Transgenic research 3 (1994), S. 99-108 
    Details
    ISSN: 1573-9368
    Keywords: human lactoferrin ; αS1-casein ; transgenic mice ; tissue specificity ; mammary gland
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The expression of human lactoferrin (hLF) in the milk of transgenic mice is described. Regulatory sequences derived from the bovine αS1-casein gene were fused to the coding sequence of the hLF cDNA and several lines of transgenic mice were generated. Human LF RNA was detected exclusively in the mammary gland of lactating females and only after the onset of lactation. No aberrant RNA products could be detected using northern blotting and primer extension analysis. The hLF concentrations in the milk ranged from less than 0.1 to 36 μg ml−1. Human LF thus expressed did not differ from human milk derived LF, with respect to molecular mass and immunoreactivity with monoclonal and polyclonal antibodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01974087
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  • 3
    Electronic Resource
    Electronic Resource
    Generation of Transgenic Mice and Germline Transmission of a Mammalian Artificial Chromosome Introduced into Embryos by Pronuclear Microinjection (2000)
    Springer
    Chromosome research 8 (2000), S. 183-191 
    Details
    ISSN: 1573-6849
    Keywords: artificial chromosomes (mammalian) ; bovine embryos ; microinjection ; murine embryos ; transgenic animals
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have generated transgenic mice by pronuclear microinjection of a murine satellite DNA-based artificial chromosome (SATAC). As 50% of the founder progeny were SATAC-positive, this demonstrates that SATAC transmission through the germline had occurred. FISH analyses of metaphase chromosomes from mitogen-activated peripheral blood lymphocytes from both the founder and progeny revealed that the SATAC was maintained as a discrete chromosome and that it had not integrated into an endogenous chromosome. To our knowledge, this is the first report of the germline transmission of a genetically engineered mammalian artificial chromosome within transgenic animals generated through pronuclear microinjection. We have also shown that murine SATACs can be similarly introduced into bovine embryos. The use of embryo microinjection to generate transgenic mammals carrying genetically engineered chromosomes provides a novel method by which the unique advantages of chromosome-based gene delivery systems can be exploited.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009206926548
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  • 4
    Electronic Resource
    Electronic Resource
    High-level expression of bovine αs1-casein in milk of transgenic mice (1998)
    Springer
    Transgenic research 7 (1998), S. 5-14 
    Details
    ISSN: 1573-9368
    Keywords: transgenic ; mammary gland ; casein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The bovine αs1-casein gene, isolated from a cosmid library, was introduced into the murine germline. Transgene expression occurred in all transgenic mice, and was confined to the lactating mammary gland. Half of the mouse lines (five out of ten) expressed at relatively high expression levels (〉1 mg ml−1). The highest levels of expression were obtained with a transgene containing 14.2 kb of 5′ flanking sequence, in two cases expression levels comparable to (10 mg ml−1) or well above (20 mg ml−1) αs1-casein levels in bovine milk were obtained. Transcription initiation occurred at the same site in the bovine αs1-casein gene in transgenic mouse as in the cow. A marked induction of expression occurred at parturition rather than at mid-pregnancy, and thus resembled the bovine rather than the murine developmental expression pattern. Bovine αs1-casein specific immunoblotting and RIA were developed for characterization and quantificatio n of the recombinant protein. Using these assays, the properties of the recombinant protein could not be distinguished from those of the natural bovine protein. In spite of the high-level tissue-specific and correctly regulated developmental expression of the transgene, expression levels were integration-site dependent. This may indicate that not all cis-acting regulatory elements involved in bovine αs1-casein expression were included in the transgene
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008892720466
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  • 5
    Electronic Resource
    Electronic Resource
    Production of recombinant human type I procollagen homotrimer in the mammary gland of transgenic mice (1999)
    Springer
    Transgenic research 8 (1999), S. 415-427 
    Details
    ISSN: 1573-9368
    Keywords: collagen ; transgenic mice ; expression ; mammary gland ; biomaterial
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The large scale production of recombinant collagen for use in biomaterials requires an efficient expression system capable of processing a large (〉400 Kd) multisubunit protein requiring post-translational modifications. To investigate whether the mammary gland of transgenic animals fulfills these requirements, transgenic mice were generated containing the αS1-casein mammary gland-specific promoter operatively linked to 37 Kb of the human α1(I) procollagen structural gene and 3′ flanking region. The frequency of transgenic lines established was 12%. High levels of soluble triple helical homotrimeric [(α1)3] type I procollagen were detected (up to 8 mg/ml) exclusively in the milk of six out of 9 lines of lactating transgenic mice. The transgene-derived human procollagen chains underwent efficient assembly into a triple helical structure. Although proline or lysine hydroxylation has never been described for any milk protein, procollagen was detected with these post-translational modifications. The procollagen was stable in mil; minimal degradation was observed. These results show that the mammary gland is capable of expressing a large procollagen gene construct, efficiently assembling the individual polypeptide chains into a stable triple helix, and secreting the intact molecule into the milk.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008959924856
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