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.

Identification of trypsin-inhibitory site and structure determination of human SPINK2 serine proteinase inhibitor

2009 ◽  
Vol 77 (1) ◽  
pp. 209-219 ◽  
Author(s):  
Ting Chen ◽  
Tian-Ren Lee ◽  
Wei-Guang Liang ◽  
Wun-Shaing Wayne Chang ◽  
Ping-Chiang Lyu
Keyword(s):  
Structure Determination ◽  
Proteinase Inhibitor ◽  
Serine Proteinase ◽  
Serine Proteinase Inhibitor ◽  
Inhibitory Site

Formation of Stable Complexes Between Urokinase and a Human Urinary Component

1985 ◽  
Vol 53 (01) ◽  
pp. 036-041 ◽  
Author(s):  
Witold Cieplak ◽  
David A Hart
Keyword(s):  
Complex Formation ◽  
Gel Electrophoresis ◽  
Proteinase Inhibitor ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Serine Proteinase ◽  
Serine Proteinase Inhibitor ◽  
Diisopropyl Fluorophosphate ◽  
Sds Page ◽  
Multiple Species

SummaryHuman urine was found to contain multiple species of urokinase (UK)-like plasminogen activator (PA) activity when subjected to concentration and/or dialysis and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and zymography. Untreated, freshly voided urine contained only Mr = 52,000 and 35,000 UK while dialyzed or undialyzed urine concentrates contained additional PA activity at Mr = 80,000 and 95.000. SDS-PAGE of incubation mixtures of radioiodinated UK (Mr = 52,000 or 35,000) and urine concentrates revealed the presence of radiolabeled complexes with MrS of 80,000 and 95.000. The bond(s) involved in complex formation was also relatively resistant to heat and reduction. Treatment of radioiodinated UK with the serine proteinase inhibitor, p-nitrophenyl guanidinobenzoate, prior to incubation with dialyzed, concentrated urine prevented formation of the complexes. In addition, the enzymatic activity of the Mr = 80,000 and 95,000 species was unaffected by diisopropyl fluorophosphate. These results indicate that UK forms SDS-stable complexes with a urinary component that has a Mr of approximately 40,000. The results further suggest that these complexes express PA activity when analyzed by SDS- PAGE and zymography.

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.

Sign in / Sign up

Export Citation Format

Share Document