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  • 1
    Electronic Resource
    Electronic Resource
    Enhanced expression of GTP-binding proteins in differentiated U937 monocytic cells: Possible involvement of tyrosine kinase and protein kinase C (1995)
    Springer
    Molecular and cellular biochemistry 152 (1995), S. 113-120 
    Details
    ISSN: 1573-4919
    Keywords: protein tyrosine kinase ; monocytes ; macrophages ; G-proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Monocytic U937 cells were differentiated into mature macrophages in the presence of 100 nM phorbol 12-myristate 13-acetate (PMA) for 24 h at 37°C. We investigated the alterations in the expression of GTP-binding proteins that take place during differentiation of these cells. A 40 KDa α-subunit of the inhibitory G-protein was identified by specific antibodies to Giα-1/2 and Giα-3 on Western blots and also by ADP-ribosylation catalyzed by pertussis toxin. The expression of the 40 KDa Giα subunit was increased 3.4 fold in differentiated cells. The expression of a 43 kDa Gsα subunit identified by Western blotting using specific antibody to Gsα and by ADP-ribosylation in the presence of cholera toxin was increased approximately 2 fold in differentiated cells. A faintly recognizable 46 KDa Gsα subunit was also increased but to a lesser extent (1.3 fold). Small molecular weight GTP-binding proteins identified by [35S]GTPγS binding on nitrocellulose blots were also increased significantly. The PMA-induced expression of Giα-1/2 and Gsα subunits was blocked to control level by both genistein and staurosporine, inhibitors of protein tyrosine kinase and protein kinase C, respectively. However, staurosporine was unable to block the PMA-induced expression of Giα-3; this was blocked only by genistein. These data suggest a role for tyrosine kinase and protein kinase C in the expression of G-proteins during differentiation of U937 cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01076073
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Endothelin-1 induces tyrosine phosphorylation in human blood monocytes (1996)
    Springer
    Molecular and cellular biochemistry 159 (1996), S. 33-38 
    Details
    ISSN: 1573-4919
    Keywords: protein tyrosine kinase ; monocytes ; endothelin-1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Mediators including the neuropeptide endothelin-1 (ET-1), which are released in response to injury, modulate the expression of cell adhesion molecules on leukocytes and endothelial cells. The mechanisms underlying this process are not clear. In this study we investigated the effect of endothelin-1 on the expression of tyrosine phosphorylated proteins in human blood monocytes. Endothelin-1 caused an increase in tyrosine phosphorylated proteins in monocytes in a time-dependent and dose-dependent manner, the Mr 60, 80 and 110 kDa proteins being the most prominent. This effect was blocked by pre-incubating the monocytes with the selective tyrosine kinase inhibitors genistein or herbimycin A. Endothelin-1-induced upregulation of tyrosine phosphorylated proteins appears to be mediated by the ETAreceptor. Unlike our previously reported studies in endothelial cells, immunoprecipitation with anti-src or anti-JAK antibodies followed by immunoblotting with PY20 in human blood monocytes revealed that these proteins of Mr 60, 80 and 110 kDa were not related to src or JAK kinases. These findings suggest that ET-1 exerts its effect on monocytes by a pathway involving tyrosine kinases other than src or JAK kinases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00226060
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    Paper (German National Licenses)
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