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  • 1
    Electronic Resource
    Electronic Resource
    Expression of the fibroblast growth factor receptor 1–4 genes in glomeruli in anti-Thy1.1 mesangial proliferative glomerulonephritis (1999)
    Springer
    Virchows Archiv 435 (1999), S. 501-508 
    Details
    ISSN: 1432-2307
    Keywords: Key words Growth factor ; Experimental mesangial proliferative glomerulonephritis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Basic fibroblast growth factor (FGF2) is generally known to induce proliferation of cultured mesangial cells and is expressed in proliferative mesangial cells in anti-Thy1.1 mesangial proliferative glomerulonephritis (anti-Thy1.1 GN). The distribution of the FGF receptor (FGFR) has not been studied in anti-Thy1.1 GN, so we used in situ hybridization to determine whether cells expressing FGFR1–4 mRNAs could be detected. In normal rats, all glomeruli were negative for FGFR1–4 mRNA, but those of the mesangial proliferative phase expressed FGFR1–4 mRNA in proliferative mesangial cells. Proliferation of mesangial cells has not been observed in normal rats injected with FGF2but it has been noted in anti-Thy1.1 rats injected with FGF2. These data and our results demonstrate that mesangial cells produce and release FGF2after injury and that during the proliferative phase these cells upregulate FGFR in vivo. This study is the first to demonstrate expression of FGFR1–4 mRNAs in pathological glomeruli of anti-Thy1.1 GN. The FGF2 and FGFR1–4 genes were expressed in the proliferative mesangial cells. Upregulation of FGFR is necessary for mesangial proliferation by FGF2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004280050434
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  • 2
    Electronic Resource
    Electronic Resource
    Retinoic acid induces polarizing activity but is unlikely to be a morphogen in the chick limb bud (1991)
    [s.l.] : Nature Publishing Group
    Nature 350 (1991), S. 83-86 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE nucleotide and deduced amino-acid sequence of a chick retinoic acid receptor (RAR) complementary DNA are shown in Fig. 1. The amino-acid sequence is 95% homologous to the sequences of the mouse10 and human11 RAR/3 proteins, but ≪ 75% homologous to those of the mouse RARa and y protein10. ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/350083a0
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning and complete nucleotide sequence of the Escherichia coli glutamine permease operon (glnHPQ) (1986)
    Springer
    Molecular genetics and genomics 205 (1986), S. 260-269 
    Details
    ISSN: 1617-4623
    Keywords: Glutamine permease ; Glutamine-binding protein ; glnHPQ operon ; Escherichia coli ; DNA sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The glutamine permease operon encoding the high-affinity transport system of glutamine in Escherichia coli could be cloned in one of the mini F plasmids, but not in pBR322 or pACYC184, by selection for restoration of the Gln+ phenotype, the ability to utilize glutamine as a sole carbon source. We determined the nucleotide sequence of the glutamine permease operon, which contains the structural gene of the periplasmic glutamine-binding protein (glnH), an indispensable component of the permease activity. The N-terminal amino acid sequence and the overall amino acid composition of the purified glutamine-binding protein were in good agreement with those predicted from the nucleotide sequence, if the N-terminal 22 amino acid residues were discounted. The latter comprised two Lys residues (nos. 2 and 6) followed by 16 hydrophobic amino acid residues and was assumed to be a signal peptide for transport into the periplasmic space. There were two additional reading frames (glnP and glnQ) downstream of glnH sharing a common promoter. It was concluded that the glnP and glnQ proteins as well as the glnH protein are essential for glutamine permease activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00430437
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  • 4
    Electronic Resource
    Electronic Resource
    Expression of the hepatocyte growth factor gene during chick limb development (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Developmental Dynamics 202 (1995), S. 80-90 
    Details
    ISSN: 1058-8388
    Keywords: Hepatocyte growth factor ; c-met ; Gene expression ; Limb development ; In situ hybridization ; Chick embryo ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: It has been shown that mirrorimage duplications of the zeugopodia and digits are formed when MRC-5 fibroblasts producing hepatocyte growth factor (HGF) are applied to the anterior region of the chick limb bud (Yonei et al. [1993] Dev. Biol. 160:246-253). To evaluate the role of HGF in limb development, we observed the expression pattern of the HGF gene using in situ hybridization. The HGF gene was expressed in the mesoderm of the limb bud and in the central core region of mandibular arch and maxillary processes at stages 17 to 24. When both wing and leg buds begin to extend distally, the HGF gene is expressed in the mesenchymal cells, but not in the ectodermal cells and somites. Concomitant with establishment of the apical ectodermal ridge, distal mesenchymal cells of the limb bud express the HGF gene intensely with a gradient higher in the distal region. The HGF expression is later confined to the ventral and subapical mesenchyme of the limb bud, although no signal is detectable in the apical and non-ridge ectoderm. However, signal for the c-met proto-oncogene encoding the HGF receptor is not detectable in the limb bud at stages 17 to 24. These results suggest that HGF produced in the limb mesoderm may be involved in initial induction and maintenance of the apical ectoderm during limb development. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1002020108
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