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  • 1
    ISSN: 1432-0428
    Keywords: Insulin release ; pancreatic islets ; phospho-oligosaccharide ; insulin messenger
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The phospho-oligosaccharide extracted from rat liver and supposed to act as the insulin second messenger inhibits glucose-stimulated insulin release. In the present study, this phospho-oligosaccharide was found not to affect D-[U-14C]glucose oxidation and 45Ca net uptake, but to inhibit insulin release evoked by either D-glucose or 2-ketoisocaproate in isolated rat islets. The relative extent of the latter inhibition was unaffected by either the concentration of D-glucose or the presence of dibutyryl-cyclic AMP, forskolin or glucagon in the incubation medium. At variance with the inhibitory effect of clonidine, that of the phospho-oligosaccharide was resistant to both blockade of α2-adrenergic receptors or pre-treatment with the toxin of Bordetella pertussis. It is speculated, therefore, that such a phospho-oligosaccharide might interfere with a distal event in the insulin secretory sequence.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We have previously reported that there are differences in the number of predominant amoebic antigens recognized by serum and small intestinal antibodies induced after local and systemic immunization with glutarldehyde-fixed Entamoeba histolytica trophozoites (GFT) in BALB/c mice, by an immunoblot analysis. Moreover, by enzyme-linked immunosorbent assay (ELISA) analysis, we found differences in the antiamoebic antibody isotype patterns elicited at the large and small intestines. To further characterize the antiamoebic immune response induced in BALB/c mice, after local (oral and rectal) and systemic (intraperitoneal and intramuscular) immunization with GFT, we performed an immunoblot analysis of the amoebic proteins predominantly recognized by immunoglobulins (Ig)G, IgA and IgM in the serum and in the small and large intestines. The present work shows differences between the large and small intestine in the IgG- and IgA-antibody recognition pattern of amoebic proteins, thus confirming and extending our previous findings supporting the compartmentalization of the intestinal immune response. Furthermore, our reported observation that there are differences in the amoebic proteins predominantly recognized by antibodies of different isotypes was extended to the intestines, as some proteins with relative molecular weights of 24–25, 66, 140 kDa are strongly recognized by IgG but not by other antibody isotypes.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0303-7207
    Keywords: Insulin-producing tumoral cell ; l-Arginine ; l-Ornithine
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Cell Research 1013 (1989), S. 133-143 
    ISSN: 0167-4889
    Keywords: (Rat) ; Pancreatic islet ; Polyamine ; l-Arginine ; l-Ornithine
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Regulatory regions controlling p53 gene transcription in Syrian hamster embryo cells were characterized by use of chloramphenicol acetyl-transferase (CAT) constructs encompassing various subfragments of its 5′-flanking sequences. This analysis identified a 961 bp PstI-SacI (PS) fragment upstream from the p53 P1 promoter, which exhibited promoter activity only in the reverse orientation relative to the p53 gene. Northern hybridization of mRNA from hamster embryo cells with genomic probes containing the PS fragment detected a 2.1-kb transcript expressed at much lower levels than the p53 mRNA. Steady-state levels of the 2.1-kb mRNA were threefold higher in actively growing cells than in cells from confluent cultures. Library screenings with PS-containing probes resulted in the isolation from exponentially growing cells of a cDNA, the nucleotide sequence of which showed no significant homology to genes previously described. This novel gene, named Gnb5, for guanine nucleotide-binding protein, beta 5, codes for a protein of 538 amino acids with a highly acidic amino terminus containing a proline-rich domain, followed by a neutral domain with five repeat units of the β-transducin (WD-40) motif. The homology with β subunits of G proteins and with other WD-40 repeat-containing proteins was restricted to the repeats. The Gnb5 gene is well conserved in rodents and primates, as the hamster Gnb5 cDNA recognized, under high stringency conditions, the human and mouse counterparts in Southern and Northern hybridizations. Expression of Gnb5 in adult tissues was detected preferentially in testes, in both hamsters and humans.
    Type of Medium: Electronic Resource
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