proteolytic processing
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Léčba kombinací proteolytických enzymů – systémová enzymoterapie (SET) – projevuje při orální aplikaci řadu příznivých účinků na fyziologické i patologické procesy v lidském organismu. K nejvýznamnějším patří podpora obranného zánětu a omezování zánětu opakovaného a chronického. Na slabou a oslabenou imunitu působí SET podnětně, na nadměrnou a patologickou (imunokomplexové a autoimunitní procesy) tlumivě. Novější zkušenosti ukazují, že SET může být hlavně pro svůj protizánětlivý efekt s prospěchem využívána i u atopických jedinců.
Treatment with combination of proteolytic enzymes - the oral enzyme therapy (OET) - reveals a series of favourable effects on physiologic as well as pathologic processes in the human organism. The most important pharmacologic effects involve the support of a physiologic and the depression of a recurrent or chronic inflammation, similarly as the support of an insufficient immunity and the depression of immunopathologic (immunocomplex and autoimmune) processes. Recent experience indicate, that OET may be (especially for its antiinflammatory activity) with advantage utilized even in atopic individuals.
In sturgeon, the acquisition of the potential for motility activation called spermatozoon maturation takes place outside testes. This process can be accomplished in vitro by pre-incubation of immature testicular spermatozoa in seminal fluid collected from fully mature Wolffian duct sperm. Addition of trypsin inhibitor to the pre-incubation medium disrupts spermatozoon maturation. There are no available data for the role of proteolysis regulators in fish spermatozoon maturation, while their role is recognized in mammalian sperm maturation. The present study evaluated the involvement of seminal fluid proteases and anti-proteolytic activity in the sterlet spermatozoon maturation process. Casein and gelatin zymography and quantification of amidase and anti-proteolytic activity were conducted in sturgeon seminal fluid from Wolffian duct sperm and seminal fluid from testicular sperm, along with spermatozoon extracts from Wolffian duct spermatozoa, testicular spermatozoa, and testicular spermatozoa after in vitro maturation. We did not find significant differences in proteolytic profiles of seminal fluids from Wolffian duct sperm and ones from testicular sperm. Zymography revealed differences in spermatozoon extracts: Wolffian duct spermatozoon extracts were characterized by the presence of a broad proteolytic band ranging from 48 to 41 kDa, while testicular spermatozoon extracts did not show such activity until after in vitro maturation. The differences in amidase activity coincided with these results. It may not be the levels of proteolytic and anti-proteolytic activity per se, but the alterations in their interactions triggering a cascade of signaling events, that is crucial to the maturation process.
- MeSH
- amidohydrolasy metabolismus MeSH
- motilita spermií MeSH
- proteolýza MeSH
- ryby fyziologie MeSH
- spermie fyziologie MeSH
- testis cytologie MeSH
- Wolffovy vývody cytologie MeSH
- zrání spermie * MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
Springer laboratory manual
[1st ed.] IX, 366 s. : il.
- MeSH
- fyziologický stres MeSH
- fyziologie buňky MeSH
- nádory MeSH
- patologie MeSH
- proteasy fyziologie MeSH
- replikace viru MeSH
- ubikvitin fyziologie MeSH
- Publikační typ
- přehledy MeSH
Cullin-RING ubiquitin ligases (CRLs) represent the largest family of E3 ubiquitin ligases that control most if not all cellular processes. In CUL3-based CRLs, the substrate specificity is conferred by the interaction with one of around 183 existing BTB proteins, implying a broad spectrum of possible ubiquitylation signals and possible direct ubiquitylation substrates. Indeed, CUL3-based E3-ligases can catalyze various proteolytic and non-proteolytic ubiquitin signals regulating many physiological and pathophysiological states. Here, we discuss the recent studies focusing on the non-proteolytic CUL3-based signaling in mammalian cells, which emerge as important pathways during cell division, embryonic development as well as other biological processes. Mechanistically, non-proteolytic ubiquitin signals generated by CUL3 E3-ligases often regulate substrates' interactions with other downstream factors or their subcellular localization. Existing data also demonstrate an interplay with the proteolytic ubiquitylation catalyzed on the same substrates by different E3-ligases or by the same CUL3-BTB CRL3s on different substrates. In future, a deeper understanding of the upstream spatiotemporal regulatory mechanisms will help to dissect this fascinating CUL3 ubiquitin code.
- MeSH
- kulinové proteiny metabolismus MeSH
- lidé MeSH
- proteolýza MeSH
- ubikvitin metabolismus MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- přehledy MeSH
Celiac disease is triggered by partially digested gluten proteins. Enzyme therapies that complete protein digestion in vivo could support a gluten-free diet, but the barrier to completeness is high. Current options require enzyme amounts on the same order as the protein meal itself. In this study, we evaluated proteolytic components of the carnivorous pitcher plant (Nepenthes spp.) for use in this context. Remarkably low doses enhance gliadin solubilization rates, and degrade gliadin slurries within the pH and temporal constraints of human gastric digestion. Potencies in excess of 1200:1 (substrate-to-enzyme) are achieved. Digestion generates small peptides through nepenthesin and neprosin, the latter a novel enzyme defining a previously-unknown class of prolyl endoprotease. The digests also exhibit reduced TG2 conversion rates in the immunogenic regions of gliadin, providing a twin mechanism for evading T-cell recognition. When sensitized and dosed with enzyme-treated gliadin, NOD/DQ8 mice did not show intestinal inflammation, when compared to mice challenged with only pepsin-treated gliadin. The low enzyme load needed for effective digestion suggests that gluten detoxification can be achieved in a meal setting, using metered dosing based on meal size. We demonstrate this by showing efficient antigen processing at total substrate-to-enzyme ratios exceeding 12,000:1.
- MeSH
- bezlepková dieta * MeSH
- celiakie enzymologie imunologie terapie MeSH
- Drosophila metabolismus MeSH
- enzymoterapie * MeSH
- gliadin metabolismus MeSH
- gluteny metabolismus MeSH
- koncentrace vodíkových iontů MeSH
- lidé MeSH
- myši inbrední NOD MeSH
- myši MeSH
- proteiny vázající GTP metabolismus MeSH
- proteolýza MeSH
- transglutaminasy metabolismus MeSH
- zánět imunologie metabolismus prevence a kontrola MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- mužské pohlaví MeSH
- myši MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Poultry feathers make up for as much as 8.5% of chicken weight and represent a considerable amount of almost pure keratin waste which is not being adequately utilized at the present time. The present study dealt with the processing of poultry feathers through a two-stage alkaline-enzymatic hydrolysis. In the first stage, feathers were mixed with a 0.1 or 0.3% KOH water solution in a 1 : 50 ratio and were incubated at 70°C for 24 h. After adjusting pH to 9, the effects examined in the second processing stage on the amount of degraded feathers were those of proteolytic enzyme additions (1-5%), time (4-8 h) and temperature (50-70°C). Processing feathers in 0.3% KOH and hydrolysing for 8 h in the second stage at 70°C with a 5% dose of enzyme (relative to dry feathers weight) produced approx. 91% degradation. Keratin hydrolysate is distinct for its high nitrogen content and reasonable inorganic solids level. Two-stage technology of alkaline-enzymatic hydrolysing of poultry feathers in an environment of 0.3% KOH achieves high efficiency under quite mild reaction conditions (temperature not exceeding 70°C with pH in a mildly alkaline region), and is feasible from an economic viewpoint. Keratin hydrolysate can find particular application in packaging technology (films, foils and encapsulates).
- MeSH
- drůbež MeSH
- hydrolýza MeSH
- keratiny chemie MeSH
- koncentrace vodíkových iontů MeSH
- odpadky - odstraňování metody MeSH
- peří chemie MeSH
- proteasy chemie MeSH
- průmyslový odpad analýza statistika a číselné údaje MeSH
- teplota MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH