A low molecular weight serine proteinase inhibitor from human articular cartilage

1988 ◽  
Vol 23 (1-2) ◽  
pp. 60-62
Author(s):  
H. Burkhardt ◽  
M. Kasten ◽  
S. Rauls
Keyword(s):  
Molecular Weight ◽  
Articular Cartilage ◽  
Proteinase Inhibitor ◽  
Serine Proteinase ◽  
Low Molecular Weight ◽  
Human Articular Cartilage ◽  
Serine Proteinase Inhibitor

scholarly journals Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions

1991 ◽  
Vol 274 (1) ◽  
pp. 269-273 ◽  
Author(s):  
B Böhm ◽  
R Deutzmann ◽  
H Burkhardt
Keyword(s):  
Articular Cartilage ◽  
Proteinase Inhibitor ◽  
Serine Proteinase ◽  
Cathepsin G ◽  
Human Articular Cartilage ◽  
Serine Proteinase Inhibitor ◽  
Inhibitor Molecule ◽  
Leucocyte Elastase ◽  
Sds Page

An inhibitor of the serine proteinases human leucocyte elastase (EC 3.4.21.37), of cathepsin G (EC 3.4.21.20) and of trypsin (EC 3.4.21.4) has been purified from human articular cartilage. The apparent Mr of the cationic (pI greater than 10) protein was determined to 15,000 by SDS/PAGE. It was shown to cross-react in Western blot with a specific antibody to a recombinant-derived serine-proteinase inhibitor of human mucous secretions. Identity of both inhibitors is indicated by the determination of the N-terminal amino acid sequence of the cartilage-derived serine-proteinase inhibitor. In all 24 residues the cartilage inhibitor was shown to be identical with the human secretory leucocyte proteinase inhibitor (‘SLPI’). The inhibitor molecule may play a crucial role in the protection of cartilage matrix proteins against proteolytic attack.

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.

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