Selective oxidation of methionyl residues in the human recombinant secretory leukocyte proteinase inhibitor. Effect on the inhibitor binding properties

1994 ◽  
Vol 7 (1) ◽  
pp. 31-37 ◽  
Author(s):  
Svetlana Tomova ◽  
Francesca Cutruzzolà ◽  
Donatella Barra ◽  
Gino Amiconi ◽  
Paolo Ascenzi ◽  
...  
Keyword(s):  
Selective Oxidation ◽  
Proteinase Inhibitor ◽  
Inhibitor Binding ◽  
Binding Properties ◽  
Secretory Leukocyte Proteinase Inhibitor

Selective oxidation of Met-192 in bovine α-chymotrypsin. Effect on catalytic and inhibitor binding properties

1993 ◽  
Vol 1161 (2-3) ◽  
pp. 201-208 ◽  
Author(s):  
Francesca Cutruzzolá ◽  
Paolo Ascenzi ◽  
Donatella Barra ◽  
Martino Bolognesi ◽  
Enea Menegatti ◽  
...  
Keyword(s):  
Selective Oxidation ◽  
Inhibitor Binding ◽  
Binding Properties

scholarly journals Prothioconazole and Prothioconazole-Desthio Activities against Candida albicans Sterol 14-α-Demethylase

2012 ◽  
Vol 79 (5) ◽  
pp. 1639-1645 ◽  
Author(s):  
Josie E. Parker ◽  
Andrew G. S. Warrilow ◽  
Hans J. Cools ◽  
Bart A. Fraaije ◽  
John A. Lucas ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Type Ii ◽  
Inhibitor Binding ◽  
Binding Properties ◽  
Content Type ◽  
Azole Antifungals ◽  
A Cell ◽  
Antifungal Action ◽  
Binding Spectra

ABSTRACTProthioconazole is a new triazolinthione fungicide used in agriculture. We have usedCandida albicansCYP51 (CaCYP51) to investigate thein vitroactivity of prothioconazole and to consider the use of such compounds in the medical arena. Treatment ofC. albicanscells with prothioconazole, prothioconazole-desthio, and voriconazole resulted in CYP51 inhibition, as evidenced by the accumulation of 14α-methylated sterol substrates (lanosterol and eburicol) and the depletion of ergosterol. We then compared the inhibitor binding properties of prothioconazole, prothioconazole-desthio, and voriconazole with CaCYP51. We observed that prothioconazole-desthio and voriconazole bind noncompetitively to CaCYP51 in the expected manner of azole antifungals (with type II inhibitors binding to heme as the sixth ligand), while prothioconazole binds competitively and does not exhibit classic inhibitor binding spectra. Inhibition of CaCYP51 activity in a cell-free assay demonstrated that prothioconazole-desthio is active, whereas prothioconazole does not inhibit CYP51 activity. Extracts fromC. albicansgrown in the presence of prothioconazole were found to contain prothioconazole-desthio. We conclude that the antifungal action of prothioconazole can be attributed to prothioconazole-desthio.

scholarly journals Streptococcal Inhibitor of Complement Inhibits Two Additional Components of the Mucosal Innate Immune System: Secretory Leukocyte Proteinase Inhibitor and Lysozyme

2002 ◽  
Vol 70 (9) ◽  
pp. 4908-4916 ◽  
Author(s):  
Barbara A. Fernie-King ◽  
David J. Seilly ◽  
Alexandra Davies ◽  
Peter J. Lachmann
Keyword(s):  
Immune System ◽  
Temperature Dependence ◽  
Innate Immune System ◽  
Proteinase Inhibitor ◽  
Biological Activities ◽  
Insertion Site ◽  
Innate Immune ◽  
Strong Temperature Dependence ◽  
Secretory Leukocyte Proteinase Inhibitor

ABSTRACT Streptococcal inhibitor of complement (SIC) is a 31-kDa extracellular protein of a few, very virulent, strains of Streptococcus pyogenes (particularly M1 strains). It is secreted in large quantities (about 5 mg/liter) and inhibits complement lysis by blocking the membrane insertion site on C5b67. We describe investigations into the interaction of SIC with three further major components of the innate immune system found in airway surface liquid, namely, secretory leukocyte proteinase inhibitor (SLPI), lysozyme, and lactoferrin. Enzyme-linked immunosorbent assays showed that SIC binds to SLPI and to both human and hen egg lysozyme (HEL) but not to lactoferrin. Studies using 125I-labeled proteins showed that SIC binds approximately two molecules of SLPI and four molecules of lysozyme. SLPI binding shows little temperature dependence and a small positive enthalpy, suggesting that the binding is largely hydrophobic. By contrast, lysozyme binding shows strong temperature dependence and a substantial negative enthalpy, suggesting that the binding is largely ionic. Lysozyme is precipitated from solution by SIC. Further studies examined the ability of SIC to block the biological activities of SLPI and lysozyme. An M1 strain of group A streptococci was killed by SLPI, and the antibacterial activity of this protein was inhibited by SIC. SIC did not inhibit the antiproteinase activity of SLPI, implying that there is specific inhibition of the antibacterial domain. The antibacterial and enzymatic activities of lysozyme were also inhibited by SIC. SIC is the first biological inhibitor of the antibacterial action of SLPI to be described and may prove to be an important tool for investigating this activity in vivo. Inhibition of the antibacterial actions of SLPI and lysozyme would be advantageous to S. pyogenes in establishing colonization on mucosal surfaces, and we propose that this is the principal function of SIC.

Secretory Leukocyte Proteinase Inhibitor Protects Acute Kidney Injury Through Immune and Non-Immune Pathways

Shock ◽  
2021 ◽  
Vol Publish Ahead of Print ◽  
Author(s):  
Diego Guerrieri ◽  
Nella Gabriela Ambrosi ◽  
Horacio Romeo ◽  
Juan Salaberry ◽  
Fernanda Toniolo ◽  
...  
Keyword(s):  
Acute Kidney Injury ◽  
Proteinase Inhibitor ◽  
Kidney Injury ◽  
Secretory Leukocyte Proteinase Inhibitor ◽  
Immune Pathways
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