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  • 1
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: It has been suggested that fibroblast growth factor (FGF)-1 serves as a physiological satiety factor in the hypothalamus, although the molecular mechanism underlying such a function is poorly understood. To gain additional insight into this issue, we used a Sendai virus (SeV) gene expression system in rats to explore genes differentially expressed subsequent to expression of FGF-1. Using cDNA arrays, we determined that infusion of FGF-1/SeV into one lateral ventricle induced selective expression of heat shock protein (HSP) 27 in the hypothalamus. Whereas FGF-1 expression was restricted to the ependymal cell layer of the cerebral ventricles, HSP27 was more widely expressed in astrocytes residing in the surrounding periventricular region. Similarly, infusion of FGF-1 polypeptide into a lateral ventricle induced dose-dependent HSP27 expression in periventricular astrocytes surrounding the third ventricle, with maximum mRNA levels being attained 6 h after infusion. This induction of HSP27 was accompanied by a significant suppression of feeding behaviour. Interestingly, suppression of feeding caused by intracerebro ventricular infusion of ciliary neurotrophic factor was also accompanied by induction of HSP27 in periventricular astrocytes, but suppression of feeding caused by infusion of leptin was not. It therefore appears that suppression of feeding by FGF-1 is accompanied by selective induction of HSP27 expression in hypothalamic astrocytes surrounding the third ventricle, and that this response may be a key component of the mechanism by which appetite is regulated by FGF-1.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature America Inc.
    Nature medicine 5 (1999), S. 2-2 
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] In your November issue, you carried a news story ("Japan renews gene therapy efforts") regarding progress on gene therapy in Japan. We think that your discussion of DNAVEC Research was misleading, and we would like to clarify a few points. We disagree with your suggestion that DNAVEC has failed ...
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Clinical studies of gene therapy for cystic fibrosis (CF) suggest that the key problem is the efficiency of gene transfer to the airway epithelium. The availability of relevant vector receptors, the transient contact time between vector and epithelium, and the barrier function of airway mucus ...
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract Mouse monoclonal antibody (mAb) Pgf-II specific for a 72-kDa major cell-surface protein (72K-CSP) derived from Porphyromonas gingivalis OMZ 409 was prepared. Immunoblotting analysis revealed that mAb Pgf-II reacted with 72K-CSP but not with 41-kDa fimbrial subunit protein (41K-fimbrilin) derived from P. gingivalis 381. Electron microscopic observation revealed that P. gingivalis OMZ 409 possessed peritrichous, thin fimbriae on their surface. Immunogold electron microscopy also demonstrated that mAb Pgf-II bound to the 72K-CSP examined with the gold particles arranged along the fibril array originating from the cell surface of the bacteria. These findings suggested that P. gingivalis 72K-CSP was identifiable as another fimbriae (termed Pg-II fimbriae) different from the fimbriae (termed Pg-I fimbriae) composed of a 41K-fimbrilin. Using multipin peptide synthesis technology, 102 sequential overlapping peptides covering the entire 514 amino-acid stretch of Pg-II fimbriae were synthesised. Seven immunodominant regions within Pg-II fimbrial protein molecule, which definitely reacted with the serum of patients with periodontal diseases, were detected.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A 72-kDa major cell-surface protein (72K-CSP) was purified from the wash fluid of Porphyromonas gingivalis OMZ409. Using the synthetic oligonucleotide probes corresponding to the determined amino-terminal amino acid sequence of 72K-CSP, recombinant plasmid clones carrying approx. 3.4-kb KpnI-XhoI fragments in XL1-Blue libraries of P. gingivalis OMZ409 and 381 were obtained. The premature form proteins of 558 and 563 amino acids led by putative signal sequences were thought to be processed to form the mature proteins of a predicted size of 55 655 Da for strain OMZ409 and of 55 654 for strain 381. Both proteins had unusual proline-rich regions in their carboxyl-terminal regions. No homologous sequences could be found in protein databases. Examination of antigen-specific antibody responses in the serum of patients with adult periodontitis by ELISA revealed that 72K-CSP had a different immunoreactivity from that of P. gingivalis 381 fimbriae.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of anesthesia 7 (1993), S. 385-387 
    ISSN: 1438-8359
    Keywords: Postintubation ; Subglottic granuloma ; Dyspnea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0851
    Keywords: Ganglioside ; Melanoma ; Chimeric antibody
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Ganglioside GD3, which is one of the major gangliosides expressed on the cell surface of human tumors of neuroectodermal origin has been focused on as a target molecule for passive immunotherapy. We have cloned the cDNA encoding the immunoglobulin light and heavy chains of an anti-GD3 monoclonal antibody KM641 (murine IgG3, κ), and constructed the chimeric genes by linking the cDNA fragments of the murine light and heavy variable regions to cDNA fragments of the human κ and γ1 constant regions, respectively. The transfer of these cDNA constructs into SP2/0 mouse myeloma cells resulted in the production of the chimeric antibody, designated KM871, that retained specific binding activity to GD3. Indirect immunofluorescence revealed the same staining pattern for chimeric KM871 and the mouse counterpart KM641 on GD3-expressing melanoma cells. When human serum and human peripheral blood mononuclear cells were used as effectors in complement-mediated cytotoxicity and antibody-dependent cell-mediated cytotoxicity respectively, the chimeric KM871 was more effective in killing GD3-expressing tumor cells than was the mouse counterpart KM641. Intravenous injection of chimeric KM871 markedly suppressed tumor growth in nude mice. The chimeric KM871, having enhanced antitumor activities and less immunogenicity than the mouse counterpart, would be a useful agent for passive immunotherapy of human cancer.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We constructed a cDNA library derived from cultured bovine adrenal zona glomerulosa (BAG) cells which had abundant binding sites for angiotensin II, using the mammalian expression vector pCDMS (ref. 7). A whole library was transfected into COS-7 cells, which had no detectable receptor. The ...
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-0878
    Keywords: Key words: In situ hybridization ; Intracellular Ca2+ ; IP3 (inositol 1 ; 4 ; 5-trisphosphate) ; IP3 receptor ; Mouse (ICR)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The inositol 1,4,5-trisphosphate receptor (IP3R) is an intracellular Ca2+ release channel responsible for mobilizing stored Ca2+. Three different receptor types have been molecularly cloned, and their genes have been classified into a family. The gene for the type 1 receptor (IP3R1) is predominantly expressed in cerebellar Purkinje neurons, but its gene product is localized widely in a variety of tissues; however, there is little information on what types of cells express the other two receptor types, type 2 and type 3 (IP3R2 and IP3R3, respectively). We studied the expression of the IP3R gene family in various mouse tissues by in situ hybridization histochemistry. Compared with IP3R1, the levels of expression of IP3R2 and IP3R3 mRNAs were low in all of the tissues tested. IP3R2 mRNA was localized in the intralobular duct cells of the submandibular gland, the urinary tubule cells of the kidney, the epithelial cells of epididymal ducts and the follicular granulosa cells of the ovary, while the IP3R3 mRNA was distributed in gastric cells, salivary and pancreatic acinar cells and the epithelium of the small intestine. All of these cells which express either IP3R2 or IP3R3 mRNA are known to have a secretory function in which IP3/Ca2+ signalling has been shown to be involved, and thus either IP3R2 or IP3R3 may be a prerequisite to secretion in these cells.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-0878
    Keywords: In situ hybridization ; Intracellular Ca2+ ; IP3 (inositol 1,4,5-trisphosphate) ; IP3 receptor ; Mouse (ICR)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The inositol 1,4,5-trisphosphate receptor (IP3R) is an intracellular Ca2+ release channel responsible for mobilizing stored Ca2+. Three different receptor types have been molecularly cloned, and their genes have been classified into a family. The gene for the type 1 receptor (IP3R1) is predominantly expressed in cerebellar Purkinje neurons, but its gene product is localized widely in a variety of tissues; however, there is little information on what types of cells express the other two receptor types, type 2 and type 3 (IP3R2 and IP3R3, respectively). We studied the expression of the IP3R gene family in various mouse tissues by in situ hybridization histochemistry. Compared with IP3R1, the levels of expression of IP3R2 and IP3R3 mRNAs were low in all of the tissues tested. IP3R2 mRNA was localized in the intralobular duct cells of the submandibular gland, the urinary tubule cells of the kidney, the epithelial cells of epididymal ducts and the follicular granulosa cells of the ovary, while the IP3R3 mRNA was distributed in gastric cells, salivary and pancreatic acinar cells and the epithelium of the small intestine. All of these cells which express either IP3R2 or IP3R3 mRNA are known to have a secretory function in which IP3/Ca2+ signalling has been shown to be involved, and thus either IP3R2 or IP3R3 may be a prerequisite to secretion in these cells.
    Type of Medium: Electronic Resource
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