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  • 1
    Electronic Resource
    Electronic Resource
    The human vigilin gene: identification, chromosomal localization and expression pattern (1994)
    Springer
    Human genetics 〈Berlin〉 93 (1994), S. 575-582 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Chick vigilin cRNA clones were used to isolate the cognate human gene, by screening a pWE15 genomic library. Three independent cosmid clones were isolated and characterized by restriction mapping. The gene was identified by sequencing an internal EcoRI fragment containing two exons homologous to exon 24 and 25 of the chicken vigilin gene and corresponding to nucleotides 1973–2104 of the human HBP-cDNA. The homology between the chicken and human sequences was 77% and 82% at the cDNA level, and 91% and 100% at the amino acid level. In addition, the analyzed intron/exon boundaries were invariantly conserved. The 5′ and 3′ regions of the human gene were mapped by Southern analysis of the respective clones with synthetic oligonucleotides. The entire vigilin gene spans a region of about 50 kb and has been assigned to chromosome 2q36–q37.2 (FL-pter value of 0.96 ± 0.03) by fluorescence in situ hybridization to metaphase spreads from normal peripheral blood lymphocytes. The vigilin gene is localized in a chromosomal region comprising a cluster of collagen genes (COLIVA3, COLVIA3) and the locus of the Waardenburg syndrome I. Only one mRNA species of 4.4 kb is transcribed from the human vigilin gene. In accordance with previous observations on chicken mRNA, the expression of the human vigilin mRNA depends on the stage of cytodifferentiation both in vitro and in situ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00202827
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  • 2
    Electronic Resource
    Electronic Resource
    Comparative study on the thermostability of collagen I of skin and bone: Influence of posttranslational hydroxylation of prolyl and lysyl residues (1992)
    Springer
    The protein journal 11 (1992), S. 635-643 
    Details
    ISSN: 1573-4943
    Keywords: Collagen stability ; denaturation ; circular dichroism ; fibril melting ; hydroxyproline ; hydroxylysine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Pepsin-solubilized collagen I from skin and bone was analyzed with regard to its thermal stability as a triple helical molecule in solution and afterin vitro fibril formation. Collagen I from human control bone was compared with samples showing deficiencies or surplus in the degree of hydroxylation of lysine. The helix to coil transitions were studied by circulardichroism measurements and limited trypsin digestion. Melting of fibrils from standardizedin vitro self-assembly was investigated turbidimetrically. Human control bone collagen I has a maximum transition rate (T m ) at 43.3°C in 0.05% acetic acid. This is 1.9°C above control skin (T m =41.4°C), most likely, due to a higher degree of prolyl hydroxylation—0.48 in bone vs. 0.41 in skin collagen I. Lysyl overhydroxylation of human and mouse bone collagen I appears to reduce theT m slightly (∼1°C). Underhydroxylated bone collagen has aT m which is 2°C below control. Melting temperatures ofin vitro formed fibrils are an indication for higher thermostability in parallel with an increase of lysyl hydroxylation. Accordingly, the melting temperature of such fibrils from human control skin, 49.3°C, exceeds control bone by 1.4°C. The degree of lysyl hydroxylation in these samples is 0.14 and 0.10, respectively. Further underhydroxylation (0.06) reduced it down to 45.4°C, while extensive overhydroxylation did not continue to increase the thermal stability of fibrils.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024964
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  • 3
    Electronic Resource
    Electronic Resource
    Some aspects of the modulation and regulation of collagen synthesis in vitro (1981)
    Springer
    Molecular and cellular biochemistry 34 (1981), S. 73-85 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary We reviewed here a number of publications containing data on the quantitative aspects of collagen synthesis in vitro. In one section we discussed the factors which modulate the amount of collagen synthesized in various culture systems and in another section we presented experimental evidence for regulatory mechanisms operating in collagen synthesis on the transcriptional and/or translational levels. We believe that growing knowledge of the mechanisms controlling collagen synthesis will help us to understand and deal with fibrotic processes better.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02354861
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  • 4
    Electronic Resource
    Electronic Resource
    A method to select cell populations with enhanced chemotatic activity (1984)
    Springer
    Bioscience reports 4 (1984), S. 311-318 
    Details
    ISSN: 1573-4935
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Virus-transformed and tumor ceils often show a higher chemotactic activity in comparison to normal cells. Here we show that the blind-well chamber assay is an easy and rapid procedure to select cell populations with enhanced chemotactic activity. Collagen-type-specific antibodies have been applied to analyze the efficiency of cell sorting by the chemotaxis assay.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01140494
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  • 5
    Electronic Resource
    Electronic Resource
    Microgravity and hypergravity effects on collagen biosynthesis of human dermal fibroblasts (1995)
    Springer
    Cell & tissue research 282 (1995), S. 513-517 
    Details
    ISSN: 1432-0878
    Keywords: Microgravity ; Collagen ; Bone ; Dermal fibroblasts ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Astronauts experiencing long periods of space flight suffer from severe loss of bone tissue, particularly in those bones that carry the body weight under normal gravity. It is assumed that the lack of mechanical load decreases connective tissue biosynthesis in bone-forming cells. To test this assumption, quantitative and qualitative aspects of collagen synthesis under microgravity, normal gravity, and hypergravity conditions were investigated by incubating human fibroblast cultures with [3H]-proline for 4, 7, 10, and 20 h during the Spacelab D2-mission in 1993. Quantitative analysis revealed an increase of collagen synthesis under microgravity conditions, being up to 143% higher than in 1 g controls. In contrast, hypergravity samples showed a decrease in collagen synthesis with increasing g, being at the 13% level at 10 g. The relative proportion of collagen in total synthesized protein showed a slight decrease with increasing g. The secretion of collagen by the cells, proline hydroxylation of individual collagen α-chains, and the relative proportions of synthesized collagens I, III, and V were not affected under any of the applied conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318883
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  • 6
    Electronic Resource
    Electronic Resource
    Microgravity and hypergravity effects on collagen biosynthesis of human dermal fibroblasts (1995)
    Springer
    Cell & tissue research 282 (1995), S. 513-517 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Microgravity ; Collagen ; Bone ; Dermal fibroblasts ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Astronauts experiencing long periods of space flight suffer from severe loss of bone tissue, particularly in those bones that carry the body weight under normal gravity. It is assumed that the lack of mechanical load decreases connective tissue biosynthesis in bone-forming cells. To test this assumption, quantitative and qualitative aspects of collagen synthesis under microgravity, normal gravity, and hypergravity conditions were investigated by incubating human fibroblast cultures with [3H]-proline for 4, 7, 10, and 20 h during the Spacelab D2-mission in 1993. Quantitative analysis revealed an increase of collagen synthesis under microgravity conditions, being up to 143% higher than in 1 g controls. In contrast, hypergravity samples showed a decrease in collagen synthesis with increasing g, being at the 13% level at 10 g. The relative proportion of collagen in total synthesized protein showed a slight decrease with increasing g. The secretion of collagen by the cells, proline hydroxylation of individual collagen α-chains, and the relative proportions of synthesized collagens I, III, and V were not affected under any of the applied conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050502
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  • 7
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    Some aspects of the modulation and regulation of collagen synthesis in vitro (1981)
    Springer
    Details
    Publication Date: 1981-01-01
    Print ISSN: 0300-8177
    Electronic ISSN: 1573-4919
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Published by Springer
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