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  • 1
    Electronic Resource
    Electronic Resource
    Calcium oxalate crystallizing properties of polyanions elaborated by cultured renal proximal tubular cells (1995)
    Springer
    Urological research 23 (1995), S. 103-110 
    Details
    ISSN: 1434-0879
    Keywords: Calcium oxalate ; Crystallization ; Glycosaminoglycans ; Renal polyanions ; Renal cell culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To study the influence of renal polyanions on crystallization of urinary calcium oxalate, we recovered polyanionic macromolecules from media conditioned by primary cultures of renal proximal tubular epithelial cells of rats in serum-free, hormonally defined medium. Cells cultured on microporous supports showed a higher degree of morphological and functional proximal differentiation into a polarized monolayer than those on plastic impervious substrata. Papainization of the polyanions yielded the glycosaminoglycans chondroitin/dermatan sulphate and heparan sulphate. These accounted respectively for 60% and 80% of the crystal nucleation-promoting activities of polyanions recovered from the apical and basal media conditioned by polarized cultures on microporous supports. Similar relative activities were observed among the urinary glycosaminoglycans and polyanions similarly tested. Primary cultures of polarized proximal tubular epithelial cells are useful then as an in vitro model to study the crystallizing activities of polyanionic macromolecules produced by renal cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307940
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular cloning of a maltose transport gene from Bacillus stearothermophilus and its expression in Escherichia coli K-12 (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 343-352 
    Details
    ISSN: 1617-4623
    Keywords: LacY ; MalG ; mal genes ; CscB
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Genes responsible for maltose utilization from Bacillus stearothermophilus ATCC7953 were cloned in the plasmid vector pBR325 and functionally expressed in Escherichia coli. The 4.2 kb Bacillus DNA insert in clone pAM1750 suppressed the growth defects on maltose caused by mutations in E. coli maltose transport genes (malE, malK or complete malB deletion) but not mutations in genes affecting intracellular maltose metabolism (malA region). Transport studies in E. coli and B. stearothermophilus suggested that pAM1750 codes for a high affinity transport system, probably one of two maltose uptake systems found in B. stearothermophilus ATCC7953. Nucleotide sequence analysis of a 3.6 kb fragment of pAM 1750 revealed three open reading frames (ORFs). One of the ORFs, malA, encoded a putative hydrophobic protein with 12 potential transmembrane segments. MalA showed amino acid sequence similarity to proteins in the superfamily containing LacY lactose permease and also some similarity to MaIG protein, a member of a binding protein-dependent transport system in E. coli. The products of two other ORFs were not hydrophobic, did not show similarity to other known sequences and were found not to be essential for maltose utilization in transport-defective E. coli mutants. Hence MalA protein was the only protein necessary for maltose transport, but despite giving a detectable but low level of transport function in E. coli, the protein was very poorly expressed and could not be identified.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00301070
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Increases in mRNA levels of glucose transporters types 1 and 3 in Ehrlich ascites tumor cells during tumor development (1997)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 67 (1997), S. 131-135 
    Details
    ISSN: 0730-2312
    Keywords: Ehrlich ascites tumor ; glucose transporter ; mRNA ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: A common feature of many tumors is an increase in glucose catabolism during tumor growth. We studied the mechanism of this phenomenon by using Ehrlich ascites tumor bearing mice as the animal model. We found that Ehrlich ascites tumor cells possess only glucose transporter 1 (GLUT1) and GLUT3 but no GLUT2, GLUT4, or GLUT5. The mRNA levels of GLUT1 and GLUT3 increased progressively in the tumour during development; however, there were no changes observable in mRNA levels of glucose transporters of all types in brain, liver, and heart of the host mice. These findings suggest that Ehrlich ascites tumor augments its glucose transport mechanism relative to other tissues in response to its unique growth needs. J. Cell. Biochem. 67:131-135, 1997. © 1997 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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