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Bombesin receptors interact with Gi and p21ras proteins in plasma membranes from rat pancreatic acinar cells

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Pröfrock,  André
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Zimmermann,  Petra
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Schulz,  Irene
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Pröfrock, A., Zimmermann, P., & Schulz, I. (1992). Bombesin receptors interact with Gi and p21ras proteins in plasma membranes from rat pancreatic acinar cells. American Journal of Physiology-Gastrointestinal and Liver Physiology, 263(2 Pt 1), G240-G247. doi:10.1152/ajpgi.1992.263.2.G240.


Cite as: http://hdl.handle.net/21.11116/0000-0007-EA11-E
Abstract
This study investigates interaction of bombesin receptors with heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins) and monomeric small molecular weight GTP-binding proteins (smg proteins), respectively, in plasma membranes (PM) of rat pancreatic acinar cells. Addition of bombesin to isolated PM stimulated the incorporation of the photoaffinity analogue [alpha-rasP]GTP-gamma-azidoanilide into Gi proteins of 40-41 kDa and reduced the pertussis toxin-induced ADP ribosylation of three 40-41 kDa proteins, which had been previously identified as Gi1, Gi2, and Gi3 (30). In PM isolated from bombesin-prestimulated acinar cells, binding of [alpha-rasP]-GTP to PM proteins of 21-22 kDa and of a monoclonal antibody against p21ras proteins was increased. Two-dimensional separation of PM proteins revealed the presence of 18 or 19 differently charged smg proteins. The p21ras proteins could be separated into two differently charged proteins with isoelectric points of 5.58 and 5.79. In microsomal membranes (MM), [alpha-32P]GTP binding to yet unidentified 21-22 kDa smg proteins was decreased compared with membranes from unstimulated acinar cells. The data suggest that Gi proteins as well as p21ras proteins are involved in bombesin receptor-mediated signal transduction in the PM. Furthermore, 21-22 kDa smg proteins in MM might play a role in bombesin-induced stimulation of intracellular pathways that lead to enzyme secretion from pancreatic acinar cells.