Antisense oligodeoxynucleotides to Gs protein α-subunit sequence accelerate differentiation of fibroblasts to adipocytes

Nature ◽  
1992 ◽  
Vol 358 (6384) ◽  
pp. 334-337 ◽  
Author(s):  
Hsien-yu Wang ◽  
David C. Watkins ◽  
Craig C. Malbon
Keyword(s):  
Antisense Oligodeoxynucleotides ◽  
Α Subunit ◽  
Gs Protein ◽  
Subunit Sequence

Analysis of mutations in the Gs protein α subunit gene in human leukaemia

1992 ◽  
Vol 16 (5) ◽  
pp. 485-489 ◽  
Author(s):  
Bartrum W. Baker ◽  
John D. Norton
Keyword(s):  
Subunit Gene ◽  
Α Subunit ◽  
Gs Protein ◽  
Human Leukaemia

Antisense oligodeoxynucleotides to G-protein α-subunit subclasses identify a transductional requirement for the modulation of normal feeding dependent on GαOA subunit

1995 ◽  
Vol 33 (1) ◽  
pp. 72-78 ◽  
Author(s):  
Carlos R. Plata-Salamán ◽  
Charlie D. Wilson ◽  
Gayatri Sonti ◽  
Jeffrey P. Borkoski ◽  
Jarlath M.H. ffrench-Mullen
Keyword(s):  
G Protein ◽  
Antisense Oligodeoxynucleotides ◽  
Α Subunit ◽  
Normal Feeding ◽  
G Protein Α Subunit

Synthetic peptides of the α subunit of Gs protein inhibit receptor mediated adenylyl cyclase

2006 ◽  
pp. 587-588
Author(s):  
Paolo Rovero ◽  
Claudia Galoppini ◽  
Simone Taddei ◽  
Laura Giusti ◽  
Maria R. Mazzoni
Keyword(s):  
Adenylyl Cyclase ◽  
Synthetic Peptides ◽  
Α Subunit ◽  
Gs Protein

Conformational studies on three synthetic C-terminal fragments of the α subunit of a Gs protein

2006 ◽  
pp. 523-524
Author(s):  
Stefania Albrizio ◽  
Annamaria D’Ursi ◽  
Giovanni Greco ◽  
Maria R. Mazzoni ◽  
Ettore Novellino ◽  
...  
Keyword(s):  
Α Subunit ◽  
Conformational Studies ◽  
Gs Protein

Gs protein dysfunction in allergen-challenged human isolated passively sensitized bronchi

2000 ◽  
Vol 279 (2) ◽  
pp. L209-L215 ◽  
Author(s):  
Pingfang Song ◽  
Manlio Milanese ◽  
Emanuele Crimi ◽  
Santina Bruzzone ◽  
Elena Zocchi ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Allergen Challenge ◽  
Specific Ige ◽  
Response Curves ◽  
Α Subunit ◽  
Subunit Expression ◽  
Gs Protein ◽  
Relaxation Curves ◽  
The Right ◽  
Protein Dysfunction

We studied the intracellular mechanisms of allergen-induced β2-adrenoceptor dysfunction in human isolated passively sensitized bronchi. Sensitization was obtained by overnight incubation of bronchial rings with serum containing a high specific IgE level to Dermatophagoides but a low total IgE level. Allergen challenge was done by incubation with a Dermatophagoidesmix. The Gs protein stimulant cholera toxin (2 μg/ml) displaced the carbachol (CCh) concentration-response curves of control and sensitized but not of challenged rings to the right. Cholera toxin (10 μg/ml) displaced the concentration-response curves to CCh of control, sensitized, and challenged rings to the right, but this effect was less in challenged rings. The effects of the Gi protein inhibitor pertussis toxin (250 ng/ml or 1 μg/ml) on salbutamol concentration-relaxation curves did not differ significantly between challenged and sensitized rings. The adenylyl cyclase activator forskolin and the Ca2+-activated K+-channel opener NS-1619 relaxed CCh-contracted bronchial rings without significant differences between control, sensitized, and challenged rings. Neither Gi nor Gs α-subunit expression differed between control, sensitized, and challenged tissues. We conclude that Gs protein dysfunction may be a mechanism of allergen-induced β2-adrenoceptor dysfunction in human isolated passively sensitized bronchi.

Oncogenic mutations of α-Gi2 protein are not determinant for human adrenocortical tumourigenesis

1995 ◽  
Vol 133 (2) ◽  
pp. 166-172 ◽  
Author(s):  
Christine Gicquel ◽  
Anne Dib ◽  
Xavier Bertagna ◽  
Serge Amselem ◽  
Yves Le Bouc
Keyword(s):  
Adenylyl Cyclase ◽  
Denaturing Gradient Gel Electrophoresis ◽  
Direct Sequencing ◽  
Α Subunit ◽  
Signal Transducers ◽  
Activating Mutations ◽  
Oncogenic Mutations ◽  
Adrenocortical Tumours ◽  
Gradient Gel Electrophoresis ◽  
Gs Protein

Gicquel C, Dib A, Bertagna X, Amselem S, Le Bouc Y. Oncogenic mutations of α-Gi2 protein are not determinant for human adrenocortical tumourigenesis. Eur J Endocrinol 1995:133:166–72. ISSN 0804–4643 Activating mutations of G proteins, which are membrane signal transducers, have been associated recently with the development of various endocrine neoplasms. Mutations of two highly conserved codons, Arg201 and Gin227, in the α-subunit of the Gs protein, the adenylyl cyclase-stimulating protein, were first described in growth hormone-producing pituitary tumours. They resulted in constitutive activation of the αs-subunit by decreasing intrinsic GTPase activity. A similar mutation, affecting codon Arg179 (exon 5) in the α-subunit of the Gi2 protein, the adenylyl cyclase-inhibiting protein, has been described by a single group in ovarian and adrenocortical tumours. We evaluated the frequency of activating mutations in the α-subunit of the Gi2 protein in 18 human adrenocortical tumours. We screened exons 5 (codon Arg179) and 6 (codon Gln205) for mutations by denaturing gradient gel electrophoresis analysis of leucocyte and tumoural DNA. No abnormal migration pattern was found in either exon. The absence of mutation in exon 5, which includes the Arg179 codon, was confirmed in all tumoural DNA by direct sequencing. In conclusion, we did not find any oncogenic mutations in the GTPase domain of the α-subunit of the Gi2 protein in adrenocortical tumours. Thus, the previously oncogenic gip2 mutations do not appear to be determinant for adrenocortical tumourigenesis. Christine Gicquel, Laboratoire d'Explorations Fonctionnelles Endocriniennes, Hôpital Trousseau, 26 Avenue Arnold Netter, 75012 Paris, France

273: Knock-Down of BCL-2 By Antisense Oligodeoxynucleotides Induces Radiosensitization and Inhibition of Angiogenesis

2007 ◽  
Vol 177 (4S) ◽  
pp. 91-92
Author(s):  
Satoshi Anai ◽  
Yoshihisa Sakai ◽  
Steve Goodison ◽  
Kathleen Shiverick ◽  
Bob Brown ◽  
...  
Keyword(s):  
Antisense Oligodeoxynucleotides ◽  
Knock Down ◽  
Inhibition Of Angiogenesis
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