scholarly journals The Role of a Second Shell Hydrophobic Interaction in Trypsin‐Fold Serine Protease Function

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Anna Batt ◽  
Hanine Rafidi ◽  
Teaster Baird
Keyword(s):  
Serine Protease ◽  
Hydrophobic Interaction

Correction: Structural modeling and role of HAX-1 as a positive allosteric modulator of human serine protease HtrA2

2020 ◽  
Vol 477 (2) ◽  
pp. 459-459
Author(s):  
Lalith K. Chaganti ◽  
Shubhankar Dutta ◽  
Raja Reddy Kuppili ◽  
Mriganka Mandal ◽  
Kakoli Bose
Keyword(s):  
Serine Protease ◽  
Structural Modeling ◽  
Allosteric Modulator ◽  
Positive Allosteric Modulator

scholarly journals Carbohydrate-controlled serine protease inhibitor (serpin) production in Bifidobacterium longum subsp. longum

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
S. Duboux ◽  
M. Golliard ◽  
J. A. Muller ◽  
G. Bergonzelli ◽  
C. J. Bolten ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Serine Proteases ◽  
Intestinal Tract ◽  
Defense Mechanism ◽  
Inflammatory Diseases ◽  
Bifidobacterium Longum ◽  
Serine Protease Inhibitor ◽  
Innate Defense

AbstractThe Serine Protease Inhibitor (serpin) protein has been suggested to play a key role in the interaction of bifidobacteria with the host. By inhibiting intestinal serine proteases, it might allow bifidobacteria to reside in specific gut niches. In inflammatory diseases where serine proteases contribute to the innate defense mechanism of the host, serpin may dampen the damaging effects of inflammation. In view of the beneficial roles of this protein, it is important to understand how its production is regulated. Here we demonstrate that Bifidobacterium longum NCC 2705 serpin production is tightly regulated by carbohydrates. Galactose and fructose increase the production of this protein while glucose prevents it, suggesting the involvement of catabolite repression. We identified that di- and oligosaccharides containing galactose (GOS) and fructose (FOS) moieties, including the human milk oligosaccharide Lacto-N-tetraose (LNT), are able to activate serpin production. Moreover, we show that the carbohydrate mediated regulation is conserved within B. longum subsp. longum strains but not in other bifidobacterial taxons harboring the serpin coding gene, highlighting that the serpin regulation circuits are not only species- but also subspecies- specific. Our work demonstrates that environmental conditions can modulate expression of an important effector molecule of B. longum, having potential important implications for probiotic manufacturing and supporting the postulated role of serpin in the ability of bifidobacteria to colonize the intestinal tract.

The Role of Hydrophobic Interaction on Hydration Forces in Thin Aqueous Layers

1985 ◽  
pp. 227-234
Author(s):  
Gerhard Peschel ◽  
Mathilde M. Müller ◽  
Manfred M. Müller
Keyword(s):  
Hydrophobic Interaction ◽  
Hydration Forces

scholarly journals Biochemical Aspects of a Serine Protease fromCaesalpinia echinataLam. (Brazilwood) Seeds: A Potential Tool to Access the Mobilization of Seed Storage Proteins

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Priscila Praxedes-Garcia ◽  
Ilana Cruz-Silva ◽  
Andrezza Justino Gozzo ◽  
Viviane Abreu Nunes ◽  
Ricardo José Torquato ◽  
...  
Keyword(s):  
Serine Protease ◽  
Storage Proteins ◽  
Gel Filtration ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Optimum Ph ◽  
Caesalpinia Echinata ◽  
Pepstatin A ◽  
Potential Tool

Several proteins have been isolated from seeds of leguminous, but this is the first report that a protease was obtained from seeds ofCaesalpinia echinataLam., a tree belonging to the Fabaceae family. This enzyme was purified to homogeneity by hydrophobic interaction and anion exchange chromatographies and gel filtration. This 61-kDa serine protease (CeSP) hydrolyses H-D-prolyl-L-phenylalanyl-L-arginine-p-nitroanilide (Km55.7 μM) in an optimum pH of 7.1, and this activity is effectively retained until50∘C. CeSP remained stable in the presence of kosmotropic anions (PO4 3−,SO4 2−, andCH3COO−) or chaotropic cations (K+and Na+). It is strongly inhibited by TLCK, a serine protease inhibitor, but not by E-64, EDTA or pepstatin A. The characteristics of the purified enzyme allowed us to classify it as a serine protease. The role of CeSP in the seeds cannot be assigned yet but is possible to infer that it is involved in the mobilization of seed storage proteins.

scholarly journals A common African polymorphism abolishes tyrosine sulfation of human anionic trypsinogen (PRSS2)

2009 ◽  
Vol 418 (1) ◽  
pp. 155-161 ◽  
Author(s):  
Zsolt Rónai ◽  
Heiko Witt ◽  
Olga Rickards ◽  
Giovanni Destro-Bisol ◽  
Andrew R. M. Bradbury ◽  
...  
Keyword(s):  
Serine Protease ◽  
Healthy Population ◽  
Primary Role ◽  
Tyrosine Sulfation ◽  
Sequence Alignments ◽  
Single Nucleotide ◽  
Cationic Trypsinogen ◽  
Anionic Trypsin ◽  
A Minor

Human pancreatic trypsinogens undergo post-translational sulfation on Tyr154, catalysed by the Golgi-resident enzyme tyrosylprotein sulfotransferase 2. Sequence alignments suggest that the sulfation of Tyr154 is facilitated by a unique sequence context which is characteristically found in primate trypsinogens. In the search for genetic variants that might alter this sulfation motif, we identified a single nucleotide polymorphism (c.457G>C) in the PRSS2 (serine protease 2, human anionic trypsinogen) gene, which changed Asp153 to a histidine residue (p.D153H). The p.D153H variant is common in subjects of African origin, with a minor allele frequency of 9.2%, whereas it is absent in subjects of European descent. We demonstrate that Asp153 is the main determinant of tyrosine sulfation in anionic trypsinogen, as both the natural p.D153H variation and the p.D153N mutation result in a complete loss of trypsinogen sulfation. In contrast, mutation of Asp156 and Glu157 only slightly decrease tyrosine sulfation, whereas mutation of Gly151 and Pro155 has no effect. With respect to the biological relevance of the p.D153H variant, we found that tyrosine sulfation had no significant effect on the activation of anionic trypsinogen or the catalytic activity and inhibitor sensitivity of anionic trypsin. Taken together with previous studies, the observations of the present study suggest that the primary role of trypsinogen sulfation in humans is to stimulate autoactivation of PRSS1 (serine protease 1, human cationic trypsinogen), whereas the sulfation of anionic trypsinogen is unimportant for normal digestive physiology. As a result, the p.D153H polymorphism which eliminates this modification could become widespread in a healthy population.

scholarly journals A Model to Evaluate Toxic Factors Influencing Islets during Collagenase Digestion: The Role of Serine Protease Inhibitor in the Protection of Islets

2012 ◽  
Vol 21 (2-3) ◽  
pp. 473-482 ◽  
Author(s):  
Manabu Tsukada ◽  
Takuro Saito ◽  
Kazuya Ise ◽  
Akira Kenjo ◽  
Takashi Kimura ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Serine Protease Inhibitor ◽  
Factors Influencing ◽  
Collagenase Digestion ◽  
Toxic Factors

Progress in research on the role of Omi/HtrA2 in neurological diseases

2019 ◽  
Vol 30 (3) ◽  
pp. 279-287 ◽  
Author(s):  
Xiao Juan Su ◽  
Lingyi Huang ◽  
Yi Qu ◽  
Dezhi Mu
Keyword(s):  
Cell Death ◽  
Signaling Pathways ◽  
Serine Protease ◽  
Brain Damage ◽  
Therapeutic Target ◽  
Neurological Diseases ◽  
Mitochondrial Matrix ◽  
Ischemic Brain ◽  
External Signals

Abstract Omi/HtrA2 is a serine protease present in the mitochondrial space. When stimulated by external signals, HtrA2 is released into the mitochondrial matrix where it regulates cell death through its interaction with apoptotic and autophagic signaling pathways. Omi/HtrA2 is closely related to the pathogenesis of neurological diseases, such as neurodegeneration and hypoxic ischemic brain damage. Here, we summarize the biological characteristics of Omi/HtrA2 and its role in neurological diseases, which will provide new hints in developing Omi/HtrA2 as a therapeutic target for neurological diseases.

scholarly journals Isolated choanal and gut atresias: pathogenetic role of serine protease inhibitor type 2 (SPINT2) gene mutations unlikely

2018 ◽  
Vol 23 (1) ◽  
Author(s):  
Christian Niederwanger ◽  
Silvia Lechner ◽  
Lisa König ◽  
Andreas R. Janecke ◽  
Claus Pototschnig ◽  
...  
Keyword(s):  
Protease Inhibitor ◽  
Serine Protease ◽  
Gene Mutations ◽  
Serine Protease Inhibitor ◽  
Pathogenetic Role ◽  
Inhibitor Type
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