The Role of Small Molecular Weight GTP-Binding Proteins in Stimulus Secretion Coupling of Pancreatic Acinar Cells

1993 ◽  
pp. 353-367
Author(s):  
Irene Schulz ◽  
Stefan Zeuzem ◽  
Petra Zimmermann
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Acinar Cells ◽  
Pancreatic Acinar Cells ◽  
Small Molecular Weight ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Stimulus Secretion Coupling

High- and Small-Molecular-Weight GTP-Binding Proteins in Zymogen Granule Membranes of Rat Pancreatic Acinar Cells

1992 ◽  
Vol 2 (2) ◽  
pp. 77-89 ◽  
Author(s):  
Susanne Schnefel ◽  
Petra Zimmermann ◽  
André Pröfrock ◽  
Reinhard Jahn ◽  
Klaus Aktories ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Acinar Cells ◽  
Pancreatic Acinar Cells ◽  
Zymogen Granule ◽  
Small Molecular Weight ◽  
Gtp Binding Proteins ◽  
Gtp Binding

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

1992 ◽  
Vol 263 (2) ◽  
pp. G240-G247
Author(s):  
A. Profrock ◽  
P. Zimmermann ◽  
I. Schulz
Keyword(s):  
Plasma Membranes ◽  
Binding Proteins ◽  
Acinar Cells ◽  
Pancreatic Acinar Cells ◽  
Small Molecular Weight ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Microsomal Membranes ◽  
Bombesin Receptors ◽  
Gi Proteins

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-32P]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-32P]-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.

Small molecular weight GTP-binding proteins and signal transduction

1989 ◽  
Vol 185 (3) ◽  
pp. 347-355 ◽  
Author(s):  
Katsuhiko Yamamoto ◽  
Tetsuji Tanimoto ◽  
Shigekuni Kim ◽  
Akira Kikuchi ◽  
Yoshimi Takai
Keyword(s):  
Signal Transduction ◽  
Molecular Weight ◽  
Binding Proteins ◽  
Small Molecular Weight ◽  
Gtp Binding Proteins ◽  
Gtp Binding

Purification, Characterization, and Possible Functions of Small Molecular Weight GTP-Binding Proteins

1990 ◽  
Vol 3 (8 Pt 2) ◽  
pp. 220S-223S ◽  
Author(s):  
Y. Takai ◽  
A. Kikuchi ◽  
M. Kawata ◽  
K. Yamamoto ◽  
M. Hoshijima
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Small Molecular Weight ◽  
Gtp Binding Proteins ◽  
Gtp Binding

scholarly journals Small Molecular Weight GTP-binding Proteins in Human Platelet Membranes

1989 ◽  
Vol 264 (3) ◽  
pp. 1877-1881 ◽  
Author(s):  
T Ohmori ◽  
A Kikuchi ◽  
K Yamamoto ◽  
S Kim ◽  
Y Takai
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Human Platelet ◽  
Small Molecular Weight ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Platelet Membranes
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