scholarly journals Regulation of Myostatin in Vivo by Growth and Differentiation Factor-Associated Serum Protein-1: A Novel Protein with Protease Inhibitor and Follistatin Domains

2003 ◽  
Vol 17 (6) ◽  
pp. 1144-1154 ◽  
Author(s):  
Jennifer J. Hill ◽  
Yongchang Qiu ◽  
Rodney M. Hewick ◽  
Neil M. Wolfman
Keyword(s):  
Protease Inhibitor ◽  
Serum Protein ◽  
Differentiation Factor ◽  
Novel Protein

The immunomodulatory activity of SerpinB3 an protease-inhibitor in vivo and in vitro

2017 ◽  
Vol 49 (1) ◽  
pp. e26
Author(s):  
A. Cappon ◽  
G. Villano ◽  
S. Quarta ◽  
A. Biasiolo ◽  
C. Turato ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Immunomodulatory Activity

scholarly journals Nasal commensal, Staphylococcus epidermidis shapes the mucosal environment to prevent influenza virus invasion through Serpine1 induction

2020 ◽  
Author(s):  
Ara Jo ◽  
Jina Won ◽  
Chan Hee Chil ◽  
Jae Young Choi ◽  
Kang-Mu Lee ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Respiratory Tract ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Nasal Mucosa ◽  
Staphylococcus Epidermidis ◽  
Influenza Virus Infection ◽  
Serine Protease Inhibitor ◽  
Cellular Environment

ABSTRACTOur recent study presented evidence that Staphylococcus epidermidis (S. epidermidis) was the most frequently encountered microbiome component in healthy human nasal mucus and that S. epidermidis could induce interferon (IFN)-dependent innate immunity to control acute viral lung infection. The serine protease inhibitor Serpine1 was identified to inhibit influenza A virus (IAV) spread by inhibiting glycoprotein cleavage, and the current study supports an additional mechanism of Serpine1 induction in the nasal mucosa, which can be regulated through S. epidermidis and IFN signaling. The exposure of in vivo mice to human S. epidermidis increased IFN-λ secretion in nasal mucosa and prevented an increase in the burden of IAV in the lung. S. epidermidis-inoculated mice exhibited the significant induction of Serpine1 in vivo in the nasal mucosa, and by targeting airway protease, S. epidermidis-induced Serpine1 inhibited the intracellular invasion of IAV to the nasal epithelium and led to restriction of IAV spreading to the lung. Furthermore, IFN-λ secretion was involved in the regulation of Serpine1 in S. epidermidis-inoculated nasal epithelial cells and in vivo nasal mucosa, and this was biologically relevant for the role of Serpine1 as an interferon-stimulated gene in the upper airway. Together, our findings reveal that human nasal commensal S. epidermidis manipulates the suppression of serine protease in in vivo nasal mucosa through Serpine1 induction and protects the nasal mucosa from IAV invasion through IFN-λ signaling.IMPORTANCEPreviously, we proved that nasal microbiome could enhance IFN-related innate immune responses to protect the respiratory tract against influenza virus infection. The present study shows a great understanding of the intimate association of S. epidermidis-regulated IFN-lambda induction and serine protease inhibitor in nasal mucosa. Our data demonstrate that S. epidermidis-regulated Serpine1 suppresses the invasion of influenza virus through suppression of airway serine protease at the level of nasal mucosa and impedes IAV spread to the respiratory tract. Thus, human nasal commensal S. epidermidis represents a therapeutic potential for treating respiratory viral infections via the change of cellular environment in respiratory tract.

scholarly journals Effect of phenyl vinyl sulphone cysteine protease inhibitor on Schistosoma mansoni: in vitro and in vivo experimental studies

2017 ◽  
Vol 41 (4) ◽  
pp. 1049-1058
Author(s):  
Manal Salah El-Din Mahmoud ◽  
Ayman Nabil Ibrahim ◽  
Abeer Fathy Badawy ◽  
Nourhan Mohamed Abdelmoniem
Keyword(s):  
Protease Inhibitor ◽  
Schistosoma Mansoni ◽  
Cysteine Protease ◽  
Experimental Studies ◽  
Cysteine Protease Inhibitor ◽  
Phenyl Vinyl

Novel peptide prodrugs: Lipid derivatization of protease inhibitor enhances in vivo plasma half life

Peptides ◽  
1994 ◽  
pp. 837-839
Author(s):  
C. Basava ◽  
L. M. Selk ◽  
R. Basava ◽  
M. Gardner ◽  
S. Parker ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Half Life ◽  
Plasma Half Life

scholarly journals ABT-378, a Highly Potent Inhibitor of the Human Immunodeficiency Virus Protease

1998 ◽  
Vol 42 (12) ◽  
pp. 3218-3224 ◽  
Author(s):  
Hing L. Sham ◽  
Dale J. Kempf ◽  
Akhteruzammen Molla ◽  
Kennan C. Marsh ◽  
Gondi N. Kumar ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Protease Inhibitor ◽  
Response To Therapy ◽  
Hiv Protease ◽  
Healthy Human ◽  
Human Volunteers ◽  
Immunodeficiency Virus ◽  
Potent Protease Inhibitor

ABSTRACT The valine at position 82 (Val 82) in the active site of the human immunodeficiency virus (HIV) protease mutates in response to therapy with the protease inhibitor ritonavir. By using the X-ray crystal structure of the complex of HIV protease and ritonavir, the potent protease inhibitor ABT-378, which has a diminished interaction with Val 82, was designed. ABT-378 potently inhibited wild-type and mutant HIV protease (Ki = 1.3 to 3.6 pM), blocked the replication of laboratory and clinical strains of HIV type 1 (50% effective concentration [EC50], 0.006 to 0.017 μM), and maintained high potency against mutant HIV selected by ritonavir in vivo (EC50, ≤0.06 μM). The metabolism of ABT-378 was strongly inhibited by ritonavir in vitro. Consequently, following concomitant oral administration of ABT-378 and ritonavir, the concentrations of ABT-378 in rat, dog, and monkey plasma exceeded the in vitro antiviral EC50 in the presence of human serum by >50-fold after 8 h. In healthy human volunteers, coadministration of a single 400-mg dose of ABT-378 with 50 mg of ritonavir enhanced the area under the concentration curve of ABT-378 in plasma by 77-fold over that observed after dosing with ABT-378 alone, and mean concentrations of ABT-378 exceeded the EC50 for >24 h. These results demonstrate the potential utility of ABT-378 as a therapeutic intervention against AIDS.

THE BINDING OF THYROIDAL HORMONES BY TRITON WR-1339

1963 ◽  
Vol 41 (1) ◽  
pp. 1803-1809
Author(s):  
William V. C. Leahy ◽  
Thomas F. McNickle
Keyword(s):  
Guinea Pig ◽  
Serum Protein ◽  
Filter Paper ◽  
Serum Proteins ◽  
Direct Method ◽  
Triton Wr 1339

The ability of Triton WR-1339 to bind thyroxine was determined by the thyroxine-stabilization technic of Tata. In addition, the effect of Triton treatment on the amount of triiodothyronine bound by guinea pig plasma was measured by the erythrocytic system of Hamolsky et al. and the direct method of Scholer. It was found that Triton was as effective as whole serum protein in its ability to inhibit the drying-induced deiodination of thyroxine occurring on filter paper. Triton treatment resulted in a significantly decreased uptake of triiodothyronine in the erythrocytic system and, conversely, a significantly increased binding of triiodothyronine by plasma. These results are discussed in terms of a possible competition for available thyroxine in vivo between Triton and thyroxine-binding serum proteins.

In vivo administration of a thiol protease inhibitor, E-64-C, to hereditary dystrophic chicken

1982 ◽  
Vol 5 (9) ◽  
pp. 738-744 ◽  
Author(s):  
Hideo Sugita ◽  
Masaaki Kimura ◽  
Yasuo Tarumoto ◽  
Masaharu Tamai ◽  
Kazunori Hanada ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Thiol Protease ◽  
Thiol Protease Inhibitor ◽  
In Vivo Administration ◽  
Dystrophic Chicken
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