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  • Articles  (4)
  • Articles: DFG German National Licenses  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Identification of G-proteins in rat parotid gland plasma membranes and granule membranes: presence of distinct components in granule membranes (1992)
    Springer
    Molecular and cellular biochemistry 115 (1992), S. 155-162 
    Details
    ISSN: 1573-4919
    Keywords: G-proteins ; parotid gland ; exocytosis ; granule membranes ; ADP ribosylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract We have identified by immunoblotting and ADP-ribosylation by cholera toxin and pertussis toxin the presence of Mr 43 and 46 KDa Gsα, and 39 and 41 KDa Giα;.. subunits in rat parotid gland plasma membranes but not in granule membranes. A Mr 28 KDa polypeptide that served as substrate for ADP-ribosylation by both cholera toxin and pertussis toxin was present exclusively in granule membranes. Photoaffinity crosslinking of [α-32P]GTP showed the presence of high molecular weight GTP-binding proteins (Mr 160,100 KDa) in granule membranes. Six low molecular weight GTP-binding proteins (Mr 21–28 KDa) were differentially distributed in both plasma membranes and granule membranes. The present study identifies various GTP-binding proteins in rat parotid gland plasma membranes and granule membranes, and demonstrates the presence of distinct molecular weight GTP-binding proteins in granule membranes. These granule-associated GTP-binding proteins may be involved in secretory processes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00230326
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Identification of guanine nucleotide binding regulatory proteins in bovine tracheal smooth muscle (1996)
    Springer
    Molecular and cellular biochemistry 154 (1996), S. 179-184 
    Details
    ISSN: 1573-4919
    Keywords: G-proteins ; airway smooth muscle ; ADP-ribosylation ; immunoblotting ; photolabeling ; nitrocellulose blot overlay
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The identity of G-proteins in airway smooth muscle is not well elucidated. In the present study, by immunoblotting using AS/7 antibody specific for Giα−1/2, EC/2 antibody specific for Giα−3 and RM/1 antibody specific for GSa, we identified, respectively, Mr 39, 41, 46 and 52 KDa, Mr 41 and 43 KDa, and Mr 43 and 46 KDa polypeptides of conventional (heterotrimeric) G-proteins in purified membranes of bovine tracheal smooth muscle. The identity of the Mr 41, 43 and 52 KDa Giα, and the Mr 43 and 46 Gsα was also confirmed by ADP-ribosylation with pertussis and cholera toxins, respectively. In addition, the common antibody (AG/1) for both Giα and Gsα revealed the presence of all the above polypeptides, except the Mr 52 KDa band. By nitrocellulose blot overlay with [35S]GTPγS, we also detected seven low molecular weight GTP-binding proteins of Mr 18–30 KDa in the bovine tracheal smooth muscle. Photoaffinity crosslinking of [α-32P]GTP demonstrated the presence of high molecular GTP-binding proteins of Mr 55, 75 and 110 KDa. It is concluded that plasma membranes of bovine tracheal smooth muscle contain various types of conventional, low molecular weight and high molecular weight G-proteins. This warrantes further attention to elucidate the functional roles of G-proteins in airway smooth muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00226786
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  • 4
    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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