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  • 1
    Electronic Resource
    Electronic Resource
    Voltage-gated K + channels in human T lymphocytes: a role in mitogenesis? (1984)
    [s.l.] : Nature Publishing Group
    Nature 307 (1984), S. 465-468 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Figure 1 shows outward potassium currents recorded from a human T lymphocyte in the whole cell conformation. Depolarizing voltage steps up to ?40 mV given from a holding potential of -80 mV produce very small leakage currents, representing an input resistance of greater than 20 GO for this cell. At ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/307465a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Involvement of signal transduction pathways in Salmonella typhimurium porin activated gut macrophages (1999)
    Springer
    Molecular and cellular biochemistry 194 (1999), S. 235-243 
    Details
    ISSN: 1573-4919
    Keywords: S. typhimurium ; porins ; macrophages ; protein kinase C ; nitric acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Many membrane proteins are implicated in the regulation of cell functions by triggering specific signaling pathways. Porins are known potential modulators of cell proliferation and differentiation. We explored the possible involvement of this protein in signal transduction pathways in mouse gut macrophages. In the present work we have shown that porins can trigger signal transduction in mouse macrophages infected with S. typhimurium. Activation of macrophages by porins results in an increase in inositol trisphosphate and intracellular Ca2+ mobilization. There is a translocation of protein kinase C to the membrane which is accompanied by nitric oxide release within the macrophages. This effect is the outcome of the expression of nitric oxide synthase, which is dependent on Protein kinase C. Further, we observed that there is an increased binding of the porins on macrophages infected with S. typhimurium which results in activation of macrophages and triggering of specific signaling pathways. These results indicate that porins induce the production of nitric oxide via a protein kinase C dependent pathway. Nitric oxide plays a fundamental role in macrophage effector function where it has both communication and defensive function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006971621653
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  • 3
    Electronic Resource
    Electronic Resource
    Intestinal mucins: the binding sites forsalmonella typhimurium (2000)
    Springer
    Molecular and cellular biochemistry 204 (2000), S. 107-117 
    Details
    ISSN: 1573-4919
    Keywords: salmonelly typhimurium ; binding sites ; intestinal mucins ; Mucus-Rs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Mucus-bacterial interactions in the gastrointestinal tract and their impact on subsequent enteric infections are poorly delineated. In the present study, we have examined the binding ofSalmonella typhimurium to rat intestinal mucus and characterized a mucus protein (Mucus-Rs) which specifically binds to S. typhimurium. Both virulent (1402/84), and avirulent (SF 1835) S. typhimurium were observed to bind to crude mucus, however, the virulent strain showed 6 fold more binding as compared to avirulent strain. Fractionation of crude mucus on sepharose CL-6B resolved it into three major peaks. Maximal bacterial binding was observed with a high mol. wt. glycoprotein corresponding to neutral mucin. SDS-PAGE of purified protein (termed Mucus-Rs) under non reducing conditions showed it to be a homogenous glycoprotein (mol. wt. 250 kDa), while under reducing conditions, three bands corresponding to mol. wt. of 118,75 and 60 kDa were observed. Pretreatment of Mucus-Rs with pronase, trypsin and sodium metaperiodate markedly inhibited bacterial binding. GLC analysis of Mucus-Rs showed it to contain Mannose, Glucose, Galactose, Glucosamine, Galactosamine and Sialic acid as main sugars. Competitive binding in the presence of various sugars and lectins indicated the involvement of mannose in the mucus-bacterial interactions. The Mucus-Rs binding was highly specific for S. typhimurium; no significant binding was seen with E.coliand V. cholerae. Thus, we conclude that S. typhimurium specifically binds to a 250 kDa neutral mucin of intestinal tract. This binding appears to occur via specific adhesin-receptor interactions involving bacterial pili and mannose of neutral mucin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007015312036
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  • 4
    Electronic Resource
    Electronic Resource
    Mechanisms of transmembrane signalling in human T cell activation (1989)
    Springer
    Molecular and cellular biochemistry 91 (1989), S. 45-50 
    Details
    ISSN: 1573-4919
    Keywords: signal transduction ; T-cell growth ; cell surface molecules
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Several monoclonal antibodies directed against a number of T cell surface molecules are used to elucidate the role of these molecules (cell surface molecules) in T cell activation. The activation of T cells via these molecules are both antigen-dependent (CD3/TcR complex) and antigen-independent. Irrespective of their antigen-dependency, these monoclonal antibodies activate T cells by a classical signal transduction pathway, in which the binding of monoclonal antibodies to their cell surface receptors leads to activation of phospholipase C resulting in the the depolarization of plasma membrane, hydrolysis of IP2 and IP3 and DAG, the ‘second messengers’. IP3 leads to mobilization of intracellular calcium to contribute to an increase in [Ca++]i, whereas DAG causes activation and translocation of PKC and an increasing apparent affinity for Ca++. The role of IN in the mobilization of intracellular calcium is emerging. In addition, influx of extracellular calcium also contributes to increase in [Ca−+];. The increase in [Ca++]; following activation via some T cell surface antigen is predominantly due to intracellular mobilization of Ca−+ (e.g. CD3/TcR complex), whereas activation via other T cell surface antigen, the increase in [Ca+−]i is almost entirely due to an influx of extracellular calcium (e.g. CD5 antigen). All these molecules activate autocrine system of T cell growth, namely IL-2 production, IL-2 receptor expression and T cell proliferation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00228078
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