Title : Transforming growth factor beta 1 treatment of AKR-2B cells is coupled through a pertussis-toxin-sensitive G-protein(s).

Pub. Date : 1989 Aug 1

PMID : 2508623






13 Functional Relationships(s)
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1 In plasma membranes from AKR-2B cells, TGF beta 1 increased binding of the radiolabelled, non-hydrolysable GTP analogue, guanosine 5"-[gamma-[35S]thio]triphosphate (GTP[35S]), in a dose-dependent manner. Guanosine Triphosphate transforming growth factor, beta 1 Mus musculus
2 In plasma membranes from AKR-2B cells, TGF beta 1 increased binding of the radiolabelled, non-hydrolysable GTP analogue, guanosine 5"-[gamma-[35S]thio]triphosphate (GTP[35S]), in a dose-dependent manner. guanosine 5"-[gamma-[35s]thio]triphosphate transforming growth factor, beta 1 Mus musculus
3 In plasma membranes from AKR-2B cells, TGF beta 1 increased binding of the radiolabelled, non-hydrolysable GTP analogue, guanosine 5"-[gamma-[35S]thio]triphosphate (GTP[35S]), in a dose-dependent manner. Guanosine Triphosphate transforming growth factor, beta 1 Mus musculus
4 In plasma membranes from AKR-2B cells, TGF beta 1 increased binding of the radiolabelled, non-hydrolysable GTP analogue, guanosine 5"-[gamma-[35S]thio]triphosphate (GTP[35S]), in a dose-dependent manner. Sulfur-35 transforming growth factor, beta 1 Mus musculus
5 Instead, TGF beta 1 increased the number of available binding sites for GTP[35S] from 16.2 +/- 1.2 to 21.6 +/- 2.1 pmol/mg of protein. Guanosine Triphosphate transforming growth factor, beta 1 Mus musculus
6 Instead, TGF beta 1 increased the number of available binding sites for GTP[35S] from 16.2 +/- 1.2 to 21.6 +/- 2.1 pmol/mg of protein. Sulfur-35 transforming growth factor, beta 1 Mus musculus
7 Only guanine nucleotides were able to compete for binding, and of the growth factors tested (epidermal growth factor, platelet-derived growth factor, insulin, TGF beta 1 and TGF beta 2) only TGF beta 1 affected GTP[35S] binding. Guanosine Triphosphate transforming growth factor, beta 1 Mus musculus
8 Only guanine nucleotides were able to compete for binding, and of the growth factors tested (epidermal growth factor, platelet-derived growth factor, insulin, TGF beta 1 and TGF beta 2) only TGF beta 1 affected GTP[35S] binding. Sulfur-35 transforming growth factor, beta 1 Mus musculus
9 TGF beta 1 increased GTPase activity, as determined by the release of 32PO4(3-) from GTP gamma[32P], from 116 +/- 5.5 to 175 +/- 4.3 pmol/mg of protein following a 15 min incubation. 32po4 transforming growth factor, beta 1 Mus musculus
10 TGF beta 1 increased GTPase activity, as determined by the release of 32PO4(3-) from GTP gamma[32P], from 116 +/- 5.5 to 175 +/- 4.3 pmol/mg of protein following a 15 min incubation. Guanosine Triphosphate transforming growth factor, beta 1 Mus musculus
11 TGF beta 1 increased GTPase activity, as determined by the release of 32PO4(3-) from GTP gamma[32P], from 116 +/- 5.5 to 175 +/- 4.3 pmol/mg of protein following a 15 min incubation. Phosphorus-32 transforming growth factor, beta 1 Mus musculus
12 Pretreatment of the membranes with pertussis toxin inhibited both TGF beta 1-stimulated binding of GTP[35S] as well as TGF beta 1-stimulated GTPase activity. Guanosine Triphosphate transforming growth factor, beta 1 Mus musculus
13 Pretreatment of the membranes with pertussis toxin inhibited both TGF beta 1-stimulated binding of GTP[35S] as well as TGF beta 1-stimulated GTPase activity. Sulfur-35 transforming growth factor, beta 1 Mus musculus