scholarly journals IgE-mediated histamine release from nasal mucosa is inhibited by SLPI (secretory leukocyte protease inhibitor) to the level of spontaneous release

1998 ◽  
Vol 7 (3) ◽  
pp. 217-220 ◽  
Author(s):  
U. Westin ◽  
E. Lundberg ◽  
K. Ohlsson
Keyword(s):  
Protease Inhibitor ◽  
Histamine Release ◽  
Nasal Mucosa ◽  
Secretory Leukocyte Protease Inhibitor ◽  
Cathepsin G ◽  
Low Molecular Weight ◽  
Spontaneous Release ◽  
Ige Mediated ◽  
Dose Dependent

The secretory leukocyte protease inhibitor (SLPI) is a low-molecular-weight inhibitor of proteases, such as elastase and cathepsin G which are released from leukocytes during phagocytosis. The purpose of this study was to determine whether or not SLPI is able to inhibit IgE-mediated histamine release. Nasal mucosa from 11 test subjects without atopic disposition was used for thisin vitrostudy. We found that SLPI inhibited histamine release in a dose-dependent way but was without influence on the spontaneous release.

scholarly journals Modulation of HIV Replication in Monocyte-Derived Macrophages (MDM) by Host Antiviral Factors Secretory Leukocyte Protease Inhibitor and Serpin Family C Member 1 Induced by Steroid Hormones

Viruses ◽  
2022 ◽  
Vol 14 (1) ◽  
pp. 95
Author(s):  
Santanu Biswas ◽  
Emily Chen ◽  
Yamei Gao ◽  
Sherwin Lee ◽  
Indira Hewlett ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Steroid Hormones ◽  
Molecular Mechanisms ◽  
Secretory Leukocyte Protease Inhibitor ◽  
Cathepsin G ◽  
Coagulation Cascade ◽  
Coagulation System ◽  
The Impact ◽  
Hiv 1

The impact of steroid hormones estrogen and progesterone on human immunodeficiency virus type 1 (HIV-1) replication is well documented. However, the exact mechanism involved in the regulation of HIV-1 replication by estrogen and progesterone is still unclear. In the present study, we wanted to elucidate the molecular mechanisms underlying the modulation of HIV-1 replication by estrogen and progesterone. To achieve this goal, we used real-time quantitative PCR arrays (PCR arrays) to identify differentially expressed host genes in response to hormone treatments that are involved in antiviral responses. Our in vitro results suggest that treatment with high doses of estrogen and progesterone promotes the expression of host antiviral factors Secretory leukocyte protease inhibitor (SLPI) and Serpin family C member 1 (SERPIN C1) among others produced in response to HIV-1 infection. SLPI is an enzyme that inhibits human leukocyte elastase, human cathepsin G, human trypsin, neutrophil elastase, and mast cell chymase. SERPIN C1 is a plasma protease inhibitor that regulates the blood coagulation cascade by the inhibition of thrombin and other activated serine proteases of the coagulation system. A dose dependent downmodulation of HIV-1 replication was observed in monocyte-derived macrophages (MDMs) pre-treated with the two proteins SLPI and SERPIN C1. Further investigations suggests that the host antiviral factors, SLPI and SERPIN C1 act at the pre-integration stage, inhibiting HIV-1 viral entry and leading to the observed downmodulation of HIV-1 replication. Our studies would help identify molecular mechanisms and pathways involved in HIV-1 pathogenesis.

Effect of Low-Molecular-Weight Heparin (Tinzaparin) and Unfractionated Heparin on Platelet Aggregation

1996 ◽  
Vol 2 (3) ◽  
pp. 209-212 ◽  
Author(s):  
Hanne B. Ravn ◽  
Claus Bregengaard ◽  
Henrik Vissinger ◽  
Per Østergaard ◽  
Jan Holst ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Platelet Aggregation ◽  
Unfractionated Heparin ◽  
Low Molecular Weight Heparin ◽  
Ex Vivo ◽  
Subcutaneous Administration ◽  
Low Molecular Weight ◽  
Pronounced Difference ◽  
Dose Dependent

A low-molecular-weight heparin (LMWH), when anti-IIa activity was compared. In the ex vivo part Tinzaparin, was compared with unfractionated heparin of the study, a significant enhancement of ADP-induced (UFH) for their effects on platelet aggregation in vitro and platelet aggregation was observed after i.v. administra ex vivo. Both heparins showed a dose-dependent proag- tion of both Tinzaparin and UFH with no difference in gregatory effect on ADP- and collagen-induced platelet potency. Subcutaneous administration of Tinzaparin in aggregation in vitro, but LMWH was less potent. The two different doses did not have any effect on platelet differences in potency between Tinzaparin and UFH de- activity. In conclusion, Tinzaparin appears, like other pended on how the compounds were compared. The most LMWHs, to have less proaggregatory effect on platelets pronounced difference was found when molar concentra- than UFH both in vitro and ex vivo.

Characterisation of IgE-mediated histamine release from equine basophils in vitro

1988 ◽  
Vol 20 (5) ◽  
pp. 352-356 ◽  
Author(s):  
A. M. MAGRO ◽  
U. H. RUDOFSKY ◽  
W. P. SCHRADER ◽  
J. PRENDERGAST
Keyword(s):  
Histamine Release ◽  
Ige Mediated

Neutrophil elastase increases secretory leukocyte protease inhibitor transcript levels in airway epithelial cells

1993 ◽  
Vol 265 (3) ◽  
pp. L286-L292 ◽  
Author(s):  
J. M. Abbinante-Nissen ◽  
L. G. Simpson ◽  
G. D. Leikauf
Keyword(s):  
Epithelial Cells ◽  
Protease Inhibitor ◽  
Neutrophil Elastase ◽  
Airway Epithelial Cells ◽  
Secretory Leukocyte Protease Inhibitor ◽  
Cathepsin G ◽  
Dependent Manner ◽  
Airway Epithelial ◽  
Necrosis Factor Alpha ◽  
Transcript Levels

Airway inflammation is often associated with the infiltration of activated neutrophils and subsequent protease release. Although aiding in the digestion and phagocytosis of foreign proteins and microorganisms, neutrophil proteases can indiscriminately damage healthy lung tissue. In the conducting airway, proteases, particularly neutrophil elastase, are counter-balanced by several antiproteases, including secretory leukocyte protease inhibitor (SLPI). SLPI can be produced locally by a number of cells including the airway epithelial cell. To examine the effects of neutrophil granule components on SLPI transcript levels, airway epithelial cells were treated (up to 96 h) with elastase, other proteases, or enzymes isolated from human sputum. We found that neutrophil elastase increased SLPI transcript levels in primary and transformed human airway epithelial cells in a time- and dose-dependent manner. Other neutrophil products, such as cathepsin G, myeloperoxidase, and lysozyme, had little or no effect on SLPI transcript levels. However, two nonneutrophil proteases, trypsin and pancreatic elastase, also increased SLPI transcript levels at higher doses than that required of neutrophil elastase. Two inflammatory cytokines, tumor necrosis factor-alpha and interleukin-8, produced little or no effect on SLPI transcript levels. This study demonstrates one way in which SLPI is regulated, via a protease that it inhibits, neutrophil elastase.

Cleaved SLPI, a novel biomarker of chymase activity

2008 ◽  
Vol 389 (9) ◽  
Author(s):  
Stanley M. Belkowski ◽  
John Masucci ◽  
Andrew Mahan ◽  
Jukka Kervinen ◽  
Matthew Olson ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Disulfide Bonds ◽  
Ex Vivo ◽  
Human Saliva ◽  
Cathepsin G ◽  
Proteinase 3 ◽  
Liquid Chromatography Mass Spectrometry ◽  
Enzymatic Assays ◽  
Reducing Conditions

Abstract Secretory leukocyte protease inhibitor (SLPI) is a protease inhibitor of the whey acidic protein-like family inhibiting chymase, chymotrypsin, elastase, proteinase 3, cathepsin G and tryptase. Performing in vitro enzymatic assays using both Western blotting and liquid chromatography/mass spectrometry techniques we showed that, of the proteases known to interact with SLPI, only chymase could uniquely cleave this protein. The peptides of the cleaved SLPI (cSLPI) remain coupled due to the disulfide bonds in the molecule but under reducing conditions the cleavage can be observed as peptide products. Subsequent ex vivo studies confirmed the presence of SLPI in human saliva and its susceptibility to cleavage by chymase. Furthermore, inhibitors of chymase activity are able to inhibit this cleavage. Human saliva from both normal and allergic individuals was analyzed for levels of cSLPI and a correlation between the level of cSLPI and the extent of allergic symptoms was observed, suggesting the application of cSLPI as a biomarker of chymase activity in humans.

INFLUENCE OF OESTROGEN ADMINISTRATION IN VIVO AND IN VITRO ON THE RELEASE AND SYNTHESIS OF LH AND FSH FROM INCUBATED PITUITARIES

1977 ◽  
Vol 86 (4) ◽  
pp. 704-713 ◽  
Author(s):  
Marta E. Apfelbaum ◽  
S. Taleisnik
Keyword(s):  
Incubation Medium ◽  
Additive Effects ◽  
Spontaneous Release ◽  
Oestrogen Treatment ◽  
Gonadotrophin Secretion ◽  
Oestradiol Benzoate ◽  
Dose Dependent

ABSTRACT The effect of oestrogen on the release and synthesis of LH and FSH was studied in rat adenohypophyses incubated for a period of 4 h in flasks containing 1 ml Eagle's medium. One hemipituitary was used as the experimental gland and the other half served as a control. The spontaneous release of LH and FSH by glands from ovarectomized rats was not affected by oestradiol-17β added to the incubation medium in doses of 55, 166, 500 and 1500 ng/ml. The amount of hormones released by pituitaries from spayed rats injected with oestradiol benzoate (2.5, 5.0 and 10.0 μg/rat) 2 h or 24 h before killing the animals too was not different from that of oil-injected rats. Neither was there any effect of oestrogen when added to the incubation medium of glands from oestrogen-pre-treated rats. However, the concentration of LH and FSH in the gland increased when oestrogen was added to the incubation medium, indicating enhanced synthesis. The effect was dose-dependent up to the dose of 500 ng/ml oestradiol but a dose of 1500 ng/ml was less effective. Increased synthesis of LH but not of FSH was also observed in incubated glands from rats injected with oestrogen 24 h before death, but no changes were seen in those of rats killed 2 h after treatment. Additive effects occurred with the in vivo and in vitro steroid treatment. These results indicate that oestrogen favours synthesis of LH and FSH in cultured pituitaries, without affecting gonadotrophin secretion and that the changes induced in the in situ gland by oestrogen treatment are reflected by their in vitro activity.

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