Effect of a low-molecular weight serine proteinase inhibitor (camostate) on amylase release from isolated pancreatic acini

1989 ◽  
Vol 189 (1) ◽  
pp. 33-38 ◽  
Author(s):  
B. Göke ◽  
J. Leferink ◽  
R. Göke ◽  
G. Adler
Keyword(s):  
Molecular Weight ◽  
Proteinase Inhibitor ◽  
Serine Proteinase ◽  
Low Molecular Weight ◽  
Serine Proteinase Inhibitor ◽  
Amylase Release ◽  
Pancreatic Acini ◽  
Isolated Pancreatic Acini

scholarly journals The Serine Proteinase Inhibitor (Serpin) Plasminogen Activation Inhibitor Type 2 Protects against Viral Cytopathic Effects by Constitutive Interferon α/β Priming

1998 ◽  
Vol 187 (11) ◽  
pp. 1799-1811 ◽  
Author(s):  
Toni M. Antalis ◽  
May La Linn ◽  
Karen Donnan ◽  
Luis Mateo ◽  
Joy Gardner ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Proteinase Inhibitor ◽  
Rapid Development ◽  
Serine Proteinase ◽  
Productive Infection ◽  
Interferon Α ◽  
Serine Proteinase Inhibitor ◽  
Cytopathic Effects ◽  
Inhibitor Type

The serine proteinase inhibitor (serpin) plasminogen activator inhibitor type 2 (PAI-2) is well characterized as an inhibitor of extracellular urokinase-type plasminogen activator. Here we show that intracellular, but not extracellular, PAI-2 protected cells from the rapid cytopathic effects of alphavirus infection. This protection did not appear to be related to an effect on apoptosis but was associated with a PAI-2–mediated induction of constitutive low-level interferon (IFN)-α/β production and IFN-stimulated gene factor 3 (ISGF3) activation, which primed the cells for rapid induction of antiviral genes. This primed phenotype was associated with a rapid development of resistance to infection by the PAI-2 transfected cells and the establishment of a persistent productive infection. PAI-2 was also induced in macrophages in response to viral RNA suggesting that PAI-2 is a virus response gene. These observations, together with the recently demonstrated PAI-2–mediated inhibition of tumor necrosis factor-α induced apoptosis, (a) illustrate that PAI-2 has an additional and distinct function as an intracellular regulator of signal transduction pathway(s) and (b) demonstrate a novel activity for a eukaryotic serpin.

scholarly journals The Axonally Secreted Serine Proteinase Inhibitor, Neuroserpin, Inhibits Plasminogen Activators and Plasmin but Not Thrombin

1998 ◽  
Vol 273 (4) ◽  
pp. 2312-2321 ◽  
Author(s):  
Thomas Osterwalder ◽  
Paolo Cinelli ◽  
Antonio Baici ◽  
Amedea Pennella ◽  
Stefan Robert Krueger ◽  
...  
Keyword(s):  
Proteinase Inhibitor ◽  
Serine Proteinase ◽  
Plasminogen Activators ◽  
Serine Proteinase Inhibitor
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