Can a Viral Serine Proteinase Inhibitor Prevent Postangioplasty Restenosis?

Circulation ◽  
1996 ◽  
Vol 94 (11) ◽  
pp. 2694-2695
Author(s):  
Edgar Haber
Keyword(s):  
Proteinase Inhibitor ◽  
Serine Proteinase ◽  
Serine Proteinase Inhibitor

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

scholarly journals Alpha-1 Antitrypsin and Monocytes

2015 ◽  
Vol 25 (2) ◽  
pp. 32-35
Author(s):  
Danielius Serapinas
Keyword(s):  
Experimental Investigation ◽  
Biological Activity ◽  
Proteinase Inhibitor ◽  
Serine Proteases ◽  
Serine Proteinase ◽  
Serine Proteinase Inhibitor ◽  
Short Term ◽  
Dual Effect ◽  
Soluble Cd14 ◽  
Alpha 1 Antitrypsin

Alpha-1 antitrypsin (AAT) is the main circulating serine proteinase inhibitor. A number of studies suggest that AAT can also exhibit biological activity independent of inhibition of serine proteases. The aim of the study was to make experimental investigation of AAT influence on monocytes stimulated by bacterial endotoxyn . AAT affects monocyte responses to LPS by regulating soluble CD14 release. Here we show that a short-term monocyte exposure to AAT leads to an increase of CD14 levels (p0.05). In parallel, a short-term cell exposure to AAT significantly enhances TNFα release. However, AAT was found to have a dual effect on LPS-induced TNFα release. Probably a rapid increase in AAT concentrations during various inflammatory and infectious conditions may enhance the magnitude of monocyte responses to endotoxin and subsequently accelerate resolution of the inflammatory reaction.

Design of octadecapeptide loop structures by modeling the active-site region of barley serine proteinase inhibitor-2

Peptides ◽  
1994 ◽  
pp. 613-615
Author(s):  
F. Jean ◽  
A. Basak ◽  
H. Dugas ◽  
N. G. Seidah ◽  
M. Chrétien ◽  
...  
Keyword(s):  
Active Site ◽  
Proteinase Inhibitor ◽  
Serine Proteinase ◽  
Serine Proteinase Inhibitor ◽  
Active Site Region
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