Regulation of exocytosis by the small GTP-binding protein rho in rat basophilic leukemia (RBL-2H3) cells |
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| Affiliation: | 1. Programa de Pós‐Graduação em Ciências Ambientais e Saúde (PPGCAS), Pontifícia Universidade Católica de Goiás (PUC‐Goiás), Goiânia, GO, Brasil;2. Departamento de Medicina, Programa de Pós‐Graduação em Ciências Ambientais e Saúde (PPGCAS), Pontifícia Universidade Católica de Goiás (PUC‐Goiás), Goiânia, GO, Brasil;1. Department of Statistics and Medical Informatics, Medical University of Bialystok, Szpitalna 37, 15-295 Bialystok, Poland;2. Centre for Reproductive Medicine KRIOBANK, Bialystok, Poland;3. Department of Reproduction and Gynecological Endocrinology, Medical University of Bialystok, Poland;4. Department of Gynecology, Medical University of Bialystok, Poland;1. Ronald O. Perelman and Claudia Cohen Center for Reproductive Medicine, New York, New York;2. Caryl and Israel Englander Institute for Precision Medicine, Weill Cornell Medicine, New York, New York |
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| Abstract: | ![]()
- 1.1. We investigated the effect of Clostridium botulinum C3 ADP-ribosyltransferase upon β-hexosaminidase release induced by various stimuli from streptolysin-O (0.5-1 U/ml)-permeabilized rat basophilic leukemia (RBL-2H3) cells.
- 2.2. The C3 transferase inhibited β-hexosaminidase release induced by Ca2+ or by guanosine-5'-(3-thio-triphosphate) (GTPyS) plus Ca2+.
- 3.3. The C3 transferase also inhibited β-hexosaminidase release induced by stimulating high affinity IgE and m3 muscarinic acetylcholine receptors.
- 4.4. The substrate for the C3 transferase was present in cytosol of RBL-2H3 cells, indicating the presence of rho p21. About 60% of the total cellular substrate protein remained within the cells permeabilized by 1 U/ml of streptolysin-O.
- 5.5. The protein rho p21 appears to be regulated by several pathways and it may function as an integration point for exocytosis.
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