scholarly journals Chemotactic Peptide Receptor-supported ADP-Ribosylation of a Pertussis Toxin Substrate GTP-binding Protein by Cholera Toxin in Neutrophil-type HL-60 Cells

1989 ◽  
Vol 264 (35) ◽  
pp. 21394-21400
Author(s):  
T Iiri ◽  
M Tohkin ◽  
N Morishima ◽  
Y Ohoka ◽  
M Ui ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Pertussis Toxin ◽  
Binding Protein ◽  
Chemotactic Peptide ◽  
Gtp Binding Protein ◽  
Peptide Receptor ◽  
Adp Ribosylation ◽  
Gtp Binding

Effects of lithium ion on ADP ribosylation of inhibitory GTP-binding protein by pertussis toxin, islet-activating protein

1991 ◽  
Vol 206 (1) ◽  
pp. 33-37 ◽  
Author(s):  
Hideo Kawamoto ◽  
Yasuhiro Watanabe ◽  
Taro Imaizumi ◽  
Tadaaki Iwasaki ◽  
Hiroshi Yoshida
Keyword(s):  
Pertussis Toxin ◽  
Binding Protein ◽  
Lithium Ion ◽  
Gtp Binding Protein ◽  
Adp Ribosylation ◽  
Gtp Binding

scholarly journals Pertussis toxin substrate is a guanosine 5′-[β-thio]diphosphate-, N-ethylmaleimide-, Mg2+- and temperature-sensitive GTP-binding protein

1985 ◽  
Vol 232 (1) ◽  
pp. 191-197 ◽  
Author(s):  
S K Wong ◽  
B R Martin ◽  
A M Tolkovsky
Keyword(s):  
Pertussis Toxin ◽  
Binding Protein ◽  
Alkylating Agents ◽  
Guanine Nucleotides ◽  
Temperature Sensitive ◽  
Gtp Binding Protein ◽  
Adp Ribosylation ◽  
Gtp Binding ◽  
Rat Brain And Liver ◽  
Liver Membranes

We compared the effects of guanine nucleotides and Mg2+ on ADP-ribosylation of rat brain and liver membrane proteins catalysed by Bordetella pertussis toxin (IAP) and cholera toxin (CT). Labelling of proteins in the presence of [alpha-32P]NAD+, ATP and CT required GTP or guanosine 5′-[γ-thio]triphosphate (GTP [S]). In contrast, labelling of one (liver) or two (brain) polypeptides by IAP was enhanced by guanosine 5′-[β-thio]diphosphate (GDP[S]) or GTP, but was blocked by GTP[S] or guanosine 5′-[β, γ-imido]triphosphate (p[NH]ppG). The order of labelling intensity was GDP[S] greater than GTP greater than no addition greater than GTP[S] = p [NH]ppG. Mg2+ increased labelling by CT, but decreased labelling by IAP. In addition, Mg2+ potentiated the effects of the guanine nucleotides, increasing the inhibitory effects of GTP[S] and the activatory effects of GDP[S] or GTP. Preincubating liver membranes at 30 degrees C in the presence of 10 mm-MgCl2 inhibited labelling by IAP irreversibly. Pretreatment of liver membranes with 4.95 mM-N-ethylmaleimide decreased labelling by CT by approximately 15%, but almost completely blocked labelling by IAP. These results suggest that the undissociated, GDP-bound, conformation of Ni, the inhibitory GTP-binding protein of adenylate cyclase, is the preferred substrate for ADP-ribosylation by IAP. This conformation, which is prevalent in native membranes, is sensitive to temperature, Mg2+ ions and alkylating agents such as N-ethylmaleimide. At 30 degrees C, Mg2+ may cause dissociation and denaturation of Ni in native membranes.

scholarly journals The inhibitory GTP-binding protein (Gi) occurs in rat Leydig cells and is differentially modified by lutropin and 12-O-tetradecanoylphorbol 13-acetate

1988 ◽  
Vol 253 (3) ◽  
pp. 895-899 ◽  
Author(s):  
E A Platts ◽  
D Schulster ◽  
B A Cooke
Keyword(s):  
Plasma Membrane ◽  
Luteinizing Hormone ◽  
Cyclic Amp ◽  
Cholera Toxin ◽  
Pertussis Toxin ◽  
Leydig Cells ◽  
Binding Protein ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
Subsequent Response

Luteinizing-hormone (LH)-stimulated cyclic AMP production in rat testis Leydig cells was desensitized by both LH and 12-O-tetradecanoylphorbol 13-acetate (TPA). However, TPA, but not LH, enhanced the subsequent response to cholera toxin. Treatment of the cells with pertussis toxin potentiated cyclic AMP production in both control and LH-desensitized cells, but did not potentiate further the responses obtained by TPA pretreatment. The results implicate the presence of an inhibitory GTP-binding protein (Gi), which may be inhibited by TPA. The presence of a Gi-like protein within the plasma membrane of Leydig cells was demonstrated by pertussis-toxin-catalysed [32P]ADP-ribosylation of a Mr-40000-41000 protein.

scholarly journals Identification of two novel GTP-binding protein alpha-subunits that lack apparent ADP-ribosylation sites for pertussis toxin

1991 ◽  
Vol 266 (19) ◽  
pp. 12676-12681 ◽  
Author(s):  
F. Nakamura ◽  
K. Ogata ◽  
K. Shiozaki ◽  
K. Kameyama ◽  
K. Ohara ◽  
...  
Keyword(s):  
Pertussis Toxin ◽  
Binding Protein ◽  
Gtp Binding Protein ◽  
Adp Ribosylation ◽  
Alpha Subunits ◽  
Gtp Binding
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