Trends in Pharmacological Sciences
Islet-activating protein, pertussis toxin: a probe for functions of the inhibitory guanine nucleotide regulatory component of adenylate cyclase
References (21)
- et al.
J. Biol. Chem.
(1981) - et al.
J. Biol. Chem.
(1982) - et al.
Arch. Biochem. Biophys.
(1982) - et al.
J. Biol. Chem.
(1979) - et al.
J. Biol. Chem.
(1983) - et al.
J. Biol. Chem.
(1981) - et al.
J. Biol. Chem.
(1983) - et al.
Arch. Biochem. Biophys.
(1983) - et al.
J. Biol. Chem.
(1982) - et al.
Arch. Biochem. Biophys.
(1983)
Cited by (477)
Strong G-Protein-Mediated Inhibition of Sodium Channels
2018, Cell ReportsCitation Excerpt :GPCRs can be coupled to a range of different G-protein complexes, the primary families being Gi/o, Gq, Gs, and G12 (Neves et al., 2002). Pertussis toxin (PTx) is a specific inhibitor of Gi/o signaling (Ui, 1984). Preincubation with PTX (200 ng/mL) for either 16–24 hr (n = 8) or 48–72 hr (n = 6) did not alter the cinacalcet-induced inhibition of VGSC currents, indicating that the pathway was mediated by G-proteins other than Gi/o (Figures 4F and 4G).
Rapid membrane responses to dihydrotestosterone are sex dependent in growth plate chondrocytes
2012, Journal of Steroid Biochemistry and Molecular BiologyCitation Excerpt :Chondrocytes from the resting zone of the growth plate were treated with testosterone and DHT, and rapid effects on phospholipase A2 (PLA2) and PKC signaling pathways determined. 5α-Dihydrotestosterone (DHT); testosterone; G-protein inhibitor pertussis toxin (PTX, Gαi inhibitor) [35], cholera toxin (CTX, Gαs activator) [36], and GDPβs (general G-protein inhibitor) [37,38]; and PLA2 inhibitors AACOCF3 [39] and quinacrine [40] were obtained from Sigma Chemical Co. (St. Louis, MO). Thapsigargin, which inhibits a Ca-ATPase pump in the endoplasmic reticulum [41]; verapamil hydrochloride and nifedipine, which are inhibitors of specific L type Ca2+ channels on the cell membrane [42,43]; the transcription inhibitor actinomycin D [44]; the translation inhibitor cycloheximide [45,46]; U73122 (phospholipase C inhibitor) [47] and cyproterone acetate (CPA), which is an inhibitor of the classical androgen receptor (AR) [48] were purchased from Sigma Chemical Co. (St. Louis, MO).
Cell-free synthesis and characterization of a novel cytotoxic pierisin-like protein from the cabbage butterfly Pieris rapae
2011, ToxiconCitation Excerpt :Notably, the primary amino acid sequence of pierisin is highly similar to the bacterial protein toxin MTX (mosquitocidal toxin) from Bacillus sphaericus SSII-1, which is known to be a protein-specific mono-ADP-ribosyltransferase (Thanabalu et al., 1993; Schirmer et al., 2002; Carpusca et al., 2006). Many bacterial ADP-ribosyltransferases specifically modify nucleotide-binding proteins, including heterotrimeric G proteins (e.g., cholera toxin (Cassel and Selinger, 1977) or pertussis toxin (Ui, 1984)), elongation factor 2 (e.g., diphtheria toxin (Collier, 1990) or Pseudomonas exotoxin A (Iglewski et al., 1977)) and low molecular mass GTPases (e.g., Clostridium botulinum C3 toxin (Aktories et al., 1987), Pseudomonas exoenzyme S (Barbieri and Sun, 2004) or Photorhabdus luminescens toxin complex PTC5 (Lang et al., 2010)). Other bacterial protein toxins ADP-ribosylate the ATP-binding protein actin e.g. the family of binary ADP-ribosylating toxins including C. botulinum C2 toxin (Aktories et al., 1986) or P. luminescens toxin complex PTC3 (Lang et al., 2010).
Mechanisms of Kringle Fragment of Urokinase-Induced Vascular Smooth Muscle Cell Migration
2007, Journal of Surgical ResearchCitation Excerpt :Dulbecco’s minimal essential medium (DMEM) and Dulbecco’s PBS (dPBS) were purchased from Cellgro. Pertussis toxin catalyzes the ADP-ribosylation of the α-subunit of Gi and Go specifically, preventing coupling with receptors [12], and was used at a standard inhibitory concentration. Pertussis toxin does not affect Gαq, even when modified at its C-terminus to mimic Gi [13].
Natriuretic peptide receptor-C signaling and regulation
2005, Peptides
- 1
Dr. Michio Ui graduated from the Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, University of Tokyo in 1955 Since 1958 he has been in the Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University as an Instructor until 1965, as an Associate Professor until 1973 and then as a Professor and the Chairman of the department. His principal research interests are metabolic physiology and biochemical pharmacology, currently focusing on the mechanisms of transmembrane signal transduction.