Academic literature on the topic 'Gastrointestinal proteases'
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Journal articles on the topic "Gastrointestinal proteases":
1
Edgington-Mitchell, Laura E. "Pathophysiological roles of proteases in gastrointestinal disease." American Journal of Physiology-Gastrointestinal and Liver Physiology 310, no. 4 (February 15, 2016): G234—G239. http://dx.doi.org/10.1152/ajpgi.00393.2015.
Abstract:
Gastrointestinal diseases, such as irritable bowel syndrome, inflammatory bowel disease, and colorectal cancer, affect a large proportion of the population and are associated with many unpleasant symptoms. Although the causes of these diseases remain largely unknown, there is increasing evidence to suggest that dysregulated protease activity may be a contributing factor. Proteases are enzymes that cleave other proteins, and their activity is normally very tightly regulated. During disease, however, the balance between proteases and their inhibitors is often shifted, leading to altered spatial and temporal control of substrate cleavage. Evaluating protease levels in normal physiology and disease has relied heavily on the use of chemical tools. Although these tools have greatly advanced the field, they are not without caveats. This review provides an introduction to these tools, their application in the gut, and a summary of the current knowledge on the contribution of protease activity to gastrointestinal disease.
2
Kryukov, V. S., S. V. Zinoviev, and R. V. Nekrasov. "Proteases in the diet of monogastric animals." Agrarian science 344, no. 1 (March 13, 2021): 30–38. http://dx.doi.org/10.32634/0869-8155-2021-344-1-30-38.
Abstract:
There are many proteases, and about 2% of the human genome is involved in the regulation of their formation. The share of proteases involved in digestion accounts for only a small part. Despite this, the mechanisms of action of digestive proteases are less studied than carbohydrases and lipases. The incorporation of exogenous proteases into young animal feeds is often accompanied by improved utilization of protein and other nutrients. Exogenous proteases degrade inhibitors of the endogenous protease and lectins in feed. Alkaline proteases are of interest due to their broader substrate specificity and activity throughout the entire gastrointestinal tract. This group includes keratinases, which digest proteins inaccessible for cleavage by proteases and peptidases of animals. Keratinases digest agglutinins, glycinin and b-conglycinin and connective tissue proteins, which are resistant to the action of gastrointestinal enzymes and a number of exogenous proteases. The alleged reasons for the inconsistent results when using feed proteases are described. Their mediated positive effects not associated with proteolysis are indicated. It is advisable to use proteases with keratinolytic activity as fodder proteases.
3
Jones, Jennifer C., Shelly Rustagi, and Peter J. Dempsey. "ADAM Proteases and Gastrointestinal Function." Annual Review of Physiology 78, no. 1 (February 10, 2016): 243–76. http://dx.doi.org/10.1146/annurev-physiol-021014-071720.
4
Herszényi, László, Mario Plebani, Paolo Carraro, Massimo De Paoli, Giovanni Roveroni, Romilda Cardin, Francesca Foschia, Zsolt Tulassay, Remo Naccarato, and Fabio Farinati. "Proteases in gastrointestinal neoplastic diseases." Clinica Chimica Acta 291, no. 2 (February 2000): 171–87. http://dx.doi.org/10.1016/s0009-8981(99)00227-2.
5
González-Páez, Gonzalo E., Emily J. Roncase, and Dennis W. Wolan. "X-ray structure of an inactive zymogen clostripain-like protease from Parabacteroides distasonis." Acta Crystallographica Section D Structural Biology 75, no. 3 (February 28, 2019): 325–32. http://dx.doi.org/10.1107/s2059798319000809.
Abstract:
The clostripain-like (C11) family of cysteine proteases are ubiquitously produced by the vast majority of the bacterial strains that make up the human distal gut microbiome. Recent reports show that some C11 proteases promote host immune responses and bacterial pathogenesis, including the induction of neutrophil phagocytosis and the activation of bacterial pathogenic toxins, respectively. The crystal structure of distapain, the only C11 protease predicted within the genome of the commensal bacterium Parabacteroides distasonis, was determined in the inactive zymogen state to 1.65 Å resolution. This is the first C11 protease structure of a zymogen, and the structure helped to uncover key unique conformations among critical active-site residues that are likely to assist in preserving the inactive protease. His135, a member of the catalytic dyad, is repositioned approximately 5.5 Å from the orientation found in active C11 structures and forms a hydrogen bond to Asp180 and a π-stacking interaction with Trp133. The structure sheds light on the potential importance of Asp180 and Trp133, as these residues are highly conserved across C11 proteases. Structure elucidation of C11 proteases will ultimately help to identify new ways to chemically and/or biologically regulate this family of enzymes, which represent potential drug-discovery targets in microbiome-related gastrointestinal diseases.
6
Lebuan, Urbanus Yustus, Roga Florida Kembaren, Merry Meryam Martgrita, and Cut Rizlani Kholibrina. "Thrombolytic protease characterization from leaves and fruit flesh of the jernang rattan plant (Daemonorops draco)." Indonesian Journal of Biotechnology 28, no. 4 (December 30, 2023): 248. http://dx.doi.org/10.22146/ijbiotech.82390.
Abstract:
Thrombolytic agents are used for thrombolytic therapy to dissolve blood clots that form in a blood vessel. All currently used thrombolytic agents have unfavorable shortcomings, such as gastrointestinal bleeding, allergic reactions, and thrombolytic agent resistance, treatment for some of which can be quite expensive. As a result, the search for thrombolytic agents derived from plants is currently taking place. Some plants have been discovered to contain protease enzymes with thrombolytic activity; pharmaceuticals derived from plants are believed to be safer. Jernang rattan (Daemonorops draco) is a plant of the Arecaceae family and is known to produce resin. Jernang rattan resin is also known to have antioxidant, antiseptic, antitumor, antimicrobial, and cytotoxic activity, but very limited information on proteolytic activity of the protease from this plant. This research aims to isolate proteases from the leaves and fruit flesh of the rattan jernang plant (D. draco) and to investigate the proteolytic activity of the isolated proteases. The protease was isolated from the leaves and the fruit flesh, and then partially purified by ammonium sulfate precipitation. The radial caseinolytic assay showed that protease in a 60% ammonium sulfate fraction gave a clear zone, with diameters of 1.4 cm and 1.8 cm for the protease isolated from leaves and fruit flesh, respectively. A Folin‐Ciocalteau assay showed that the enzymes isolated were able to hydrolyze casein and release L‐tyrosine, with activity of 0.158 U/mL and 0.174 U/mL for the protease from the leaves and fruit flesh, respectively. A fibrinogenolytic assay showed that the protease from the fruit flesh hydrolyzed the A‐α, B‐β and the γ chain of human fibrinogen, while the protease from the leaves hydrolyzed the A‐α and γ chain. Both proteases were inhibited by 56% by phenylmethylsulfonyl fluoride (PMSF), indicating that the enzymes are serine proteases. Based on the assay results obtained, it can be concluded that proteases isolated from the leaves and fruit flesh have potential as thrombolytic proteases.
7
Linz, Bodo, Irshad Sharafutdinov, Nicole Tegtmeyer, and Steffen Backert. "Evolution and Role of Proteases in Campylobacter jejuni Lifestyle and Pathogenesis." Biomolecules 13, no. 2 (February 8, 2023): 323. http://dx.doi.org/10.3390/biom13020323.
Abstract:
Infection with the main human food-borne pathogen Campylobacter jejuni causes campylobacteriosis that accounts for a substantial percentage of gastrointestinal infections. The disease usually manifests as diarrhea that lasts for up to two weeks. C. jejuni possesses an array of peptidases and proteases that are critical for its lifestyle and pathogenesis. These include serine proteases Cj1365c, Cj0511 and HtrA; AAA+ group proteases ClpP, Lon and FtsH; and zinc-dependent protease PqqE, proline aminopeptidase PepP, oligopeptidase PepF and peptidase C26. Here, we review the numerous critical roles of these peptide bond-dissolving enzymes in cellular processes of C. jejuni that include protein quality control; protein transport across the inner and outer membranes into the periplasm, cell surface or extracellular space; acquisition of amino acids and biofilm formation and dispersal. In addition, we highlight their role as virulence factors that inflict intestinal tissue damage by promoting cell invasion and mediating cleavage of crucial host cell factors such as epithelial cell junction proteins. Furthermore, we reconstruct the evolution of these proteases in 34 species of the Campylobacter genus. Finally, we discuss to what extent C. jejuni proteases have initiated the search for inhibitor compounds as prospective novel anti-bacterial therapies.
8
Weiss, Stefanie A. I., Salome R. T. Rehm, Natascha C. Perera, Martin L. Biniossek, Oliver Schilling, and Dieter E. Jenne. "Origin and Expansion of the Serine Protease Repertoire in the Myelomonocyte Lineage." International Journal of Molecular Sciences 22, no. 4 (February 7, 2021): 1658. http://dx.doi.org/10.3390/ijms22041658.
Abstract:
The deepest evolutionary branches of the trypsin/chymotrypsin family of serine proteases are represented by the digestive enzymes of the gastrointestinal tract and the multi-domain proteases of the blood coagulation and complement system. Similar to the very old digestive system, highly diverse cleavage specificities emerged in various cell lineages of the immune defense system during vertebrate evolution. The four neutrophil serine proteases (NSPs) expressed in the myelomonocyte lineage, neutrophil elastase, proteinase 3, cathepsin G, and neutrophil serine protease 4, collectively display a broad repertoire of (S1) specificities. The origin of NSPs can be traced back to a circulating liver-derived trypsin-like protease, the complement factor D ancestor, whose activity is tightly controlled by substrate-induced activation and TNFα-induced locally upregulated protein secretion. However, the present-day descendants are produced and converted to mature enzymes in precursor cells of the bone marrow and are safely sequestered in granules of circulating neutrophils. The potential site and duration of action of these cell-associated serine proteases are tightly controlled by the recruitment and activation of neutrophils, by stimulus-dependent regulated secretion of the granules, and by various soluble inhibitors in plasma, interstitial fluids, and in the inflammatory exudate. An extraordinary dynamic range and acceleration of immediate defense responses have been achieved by exploiting the high structural plasticity of the trypsin fold.
9
Durán-Pérez, Sergio A., José G. Rendón-Maldonado, Lucio de Jesús Hernandez-Diaz, Annete I. Apodaca-Medina, Maribel Jiménez-Edeza, and Julio Montes-Avila. "In Silico Identification and Molecular Characterization of Extracellular Cathepsin L Proteases from Giardia duodenalis." Current Proteomics 17, no. 4 (June 29, 2020): 342–51. http://dx.doi.org/10.2174/1570164617666191016170628.
Abstract:
Background: The protozoan Giardia duodenalis, which causes giardiasis, is an intestinal parasite that commonly affects humans, mainly pre-school children. Although there are asymptomatic cases, the main clinical features are chronic and acute diarrhea, nausea, abdominal pain, and malabsorption syndrome. Little is currently known about the virulence of the parasite, but some cases of chronic gastrointestinal alterations post-infection have been reported even when the infection was asymptomatic, suggesting that the cathepsin L proteases of the parasite may be involved in the damage at the level of the gastrointestinal mucosa. Objective: The aim of this study was the in silico identification and characterization of extracellular cathepsin L proteases in the proteome of G. duodenalis. Methods: The NP_001903 sequence of cathepsin L protease from Homo sapienswas searched against the Giardia duodenalisproteome. The subcellular localization of Giardia duodenaliscathepsin L proteases was performed in the DeepLoc-1.0 server. The construction of a phylogenetic tree of the extracellular proteins was carried out using the Molecular Evolutionary Genetics Analysis software (MEGA X). The Robetta server was used for the construction of the three-dimensional models. The search for possible inhibitors of the extracellular cathepsin L proteases of Giardia duodenaliswas performed by entering the three-dimensional structures in the FINDSITEcomb drug discovery tool. Results: Based on the amino acid sequence of cathepsin L from Homo sapiens, 8 protein sequences were identified that have in their modular structure the Pept_C1A domain characteristic of cathepsins and two of these proteins (XP_001704423 and XP_001704424) are located extracellularly. Threedimensional models were designed for both extracellular proteins and several inhibitory ligands with a score greater than 0.9 were identified. In vitrostudies are required to corroborate if these two extracellular proteins play a role in the virulence of Giardia duodenalisand to discover ligands that may be useful as therapeutic targets that interfere in the mechanism of pathogenesis generated by the parasite. Conclusion: In silicoanalysis identified two proteins in the Giardia duodenalisprotein repertoire whose characteristics allowed them to be classified as cathepsin L proteases, which may be secreted into the extracellular medium to act as virulence factors. Three-dimensional models of both proteins allowed the identification of inhibitory ligands with a high score. The results suggest that administration of those compounds might be used to block the endopeptidase activity of the extracellular cathepsin L proteases, interfering with the mechanisms of pathogenesis of the protozoan parasite Giardia duodenalis.
10
Upadhyay, Ratna, Mihir Gadan, Supriya Raut, and Sneha Badak. "Evaluation of Proprietary MDZenPro Formulation by Zenherb Labs in Mediating Protein Digestion under INFOGEST in-vitro Simulated Gastrointestinal Conditions." International Journal For Multidisciplinary Research 04, no. 04 (2022): 129–38. http://dx.doi.org/10.36948/ijfmr.2022.v04i04.012.
Abstract:
Protein breakdown by endogenous enzymes in the gastrointestinal (GI) tract results in generation of peptides and amino acids that act as building blocks in essential biological functions. Exogenous proteases possess immense potential as digestive enzyme supplements that can assist protein digestion in the GI system. Plant proteases, in addition to their promising activity, are considered to be safe in nature. The present study evaluated the potential application of a plant protease based proprietary formulation - MDZenPro in digesting raw whey protein, whey protein isolate and plant protein under INFOGEST simulated GI conditions. The gastric and GI digested protein products were analyzed for determining the degree of hydrolysis. The protein profiles were evaluated using SDS-PAGE. The results of the degree of hydrolysis study revealed that MDZenPro facilitated gastric and GI digestion of proteins. This increase in degree of hydrolysis was noted to be higher than that observed in proteins that were not treated with MDZenPro. The SDS-PAGE profile further supported these findings wherein, the MDZenPro treated protein samples displayed low molecular weight fragmented peptides in contrast to the profile of undigested proteins. The present study thus highlights the promising application of ‘MDZenPro’ as an effective supplement for protein digestion.
Dissertations / Theses on the topic "Gastrointestinal proteases":
1
Sriwai, Wimolpak. "Signaling By Protease-Activated Receptors in Gastrointestinal Smooth Muscle." Available to VCU users online at:, 2007. http://hdl.handle.net/10156/1315.
2
Segobola, Phokela Jonathan. "Efficacy of exogenous phytase and protease enzymes on performance and gastrointestinal health in broiler chickens." Diss., University of Pretoria, 2016. http://hdl.handle.net/2263/60857.
Abstract:
The efficacy of exogenous phytase and protease, alone and in combination, or in combination with AGP, zinc bacitracin on performance and intestinal morphology in broilers was tested. Broilers were fed a diet containing nutrients at recommended levels (positive control, PC) with no enzyme supplementation or a diet with lower nutrient density than PC, either without enzyme supplementation (negative control, NC) or with enzyme(s) (Treatments, Trt). Nutrient specifications of NC1, 2 and 3 diets were decreased by levels expected to be made available by Ronozyme® HiPhos, Ronozyme® ProAct and a combination of Ronozyme® HiPhos and ProAct, respectively. The NC1, 2 and 3 diets contained the same level of nutrients than the NC counterpart, but with the respective enzymes supplemented to the diets. At 34d of age, body weight (BW), but not feed intake (FI), of NC1 was lower (P<0.05), and feed conversion ratio (FCR) not significantly different than PC. With the addition of 100 mg/kg of a phytase product (Trt1), no difference in performance of broilers was noted compared to PC. Broilers in NC2 and Trt2 groups did not differ in performance from PC, suggesting that nutrients in NC2 were not lowered sufficiently to limit performance. BW and FI, of NC3 was lower and FCR was not significantly different than PC. With the addition of phytase and protease (Trt3), performance of broilers was similar to PC. Addition of zinc bacitracin to Trt3 did not improve any of the performance parameters compared to Trt3. There was no difference in metatarsal bone ash mass, ash concentrations, densities and percentage Ca and P of birds fed PC or NC or diets supplemented with enzymes. While no differences were found for the ileum, phytase supplementation to the diet increased the duodenal villi length: crypt depth from 8.20 (PC) to 10.75 and 10.79 (Trt1 and Trt3, respectively). No differences in this ratio were noted between PC and the NC diets. The addition of phytase, alone and in combination with a protease, increased the available nutrient levels, improved duodenal villi height to crypt depth ratio and subsequently improved broiler production. The study was therefore conducted to determine the efficacy of exogenous phytase and protease, alone and in combination, or in combination with AGP, zinc bacitracin on performance and intestinal morphology in broilers from day old to 35 days of age.Dissertation (MSc (Agric))--University of Pretoria, 2016.
Animal and Wildlife Sciences
MSc (Agric)
Unrestricted
3
Allouche, Rania. "Effet anti-inflammatoire d’hydrolysats de protéines de surface ou intracellulaires de Streptococcus thermophilus obtenus après action de protéases digestives." Electronic Thesis or Diss., Université de Lorraine, 2022. http://www.theses.fr/2022LORR0344.
Abstract:
L'inflammation offre une protection contre les blessures, traumatismes ou infections causées par des cellules endommagées, des irritants ou des agents pathogènes. Ce processus élimine les agents nuisibles et les composants des tissus endommagés. Néanmoins, une inflammation chronique de bas grade est associée à diverses pathologies. L'alimentation pourrait être un levier d'action. En effet, des peptides bioactifs issus de protéines alimentaires pourraient moduler des facteurs clés de l'inflammation et retarder l'apparition de ces maladies chroniques. En outre, les bactéries lactiques, composantes des produits laitiers fermentés, présentent des propriétés anti inflammatoires in vitro et in vivo. Parmi elles, Streptococcus thermophilus (ST) est régulièrement consommée par une part importante de la population. Certaines souches de ST présentent une activité anti inflammatoire in vitro dont le mécanisme est inconnu. Dans ce travail, l'hypothèse a été émise que des peptides libérés après hydrolyse par des protéases digestives des protéines de surface ou intracellulaires de ST pourraient être impliqués dans cette activité. Des hydrolysats ont été obtenus après rasage des protéines de surface par la trypsine ou la pepsine suivi ou non d'une trypsinolyse. La caractérisation des peptides par spectrométrie de masse en tandem a montré que la majorité appartenait aux protéines de surface. L'activité anti-inflammatoire des hydrolysats a été évaluée dans deux modèles cellulaires enflammés. L'hydrolysat obtenu après rasage trypsique et trypsinolyse des protéines de surface de ST LMD 9 a significativement diminué la sécrétion de la cytokine pro inflammatoire IL 8 dans les cellules HT 29 stimulées par le lipopolysaccharide (LPS) et réduit la production d'IL 8 et de la cytokine pro-inflammatoire IL 1β ainsi que les niveaux d'expression protéique de Pro IL 1β et COX 2 dans les macrophages THP 1 stimulés par le LPS. Les peptides actifs pourraient être issus de la digestion de la protéase de surface PrtS. Pour vérifier cette hypothèse, des hydrolysats ont été préparés par rasage par la pepsine suivi ou non d'une trypsinolyse des protéines de surface de deux souches phénotypiquement distinctes de ST : LMD 9 (PrtS+) et CNRZ 21N (PrtS-). La modulation de IL 8, IL 1β, Pro IL 1β et COX 2 a été évaluée dans les macrophages THP 1 et celle de IL 8 dans les cellules HT 29, stimulés par le LPS. Les hydrolysats issus des deux souches ont montré une action anti inflammatoire mais avec des différences selon la souche, l'hydrolysat et la concentration. Néanmoins, même la souche dépourvue de la protéase PrtS montre une activité anti inflammatoire. Les peptides libérés à partir des protéines de surface de ST par des protéases du tractus gastro intestinal lors de la digestion d'un produit contenant cette bactérie pourraient exercer des effets anti-inflammatoires et réduire le risque de maladies chroniques liées à l'inflammation. Enfin, les protéines intracellulaires des souches LMD 9 et CNRZ 21N ont été récupérées par sonication et hydrolysées par la Corolase PP, un mélange de protéases pancréatiques. Les hydrolysats générés à partir d'une fraction de ces protéines issues des deux souches ont démontré une action anti-inflammatoire par modulation des médiateurs pro inflammatoires dans les macrophages THP 1 stimulés par le LPS. A notre connaissance, il s'agit de la première étude mettant en évidence l'activité anti-inflammatoire de peptides issus de protéines de surface et d'une fraction des protéines intracellulaires de ST. Ces paraprobiotiques ou postbiotiques, pouvant être libérés dans le tractus digestif du consommateur, pourraient participer à l'effet anti-inflammatoire global mis en évidence avec certaines souches et avoir des effets bénéfiques sur la santé humaine et ainsi constituer un ingrédient bioactif prometteur pour le développement d'aliments fonctionnels pour la prévention de l'inflammation de bas gradeInflammation is a mechanism that provides protection against injury, trauma, or infection caused by damaged cells, irritants, or pathogens. This process removes harmful agents and damaged tissue components. Nevertheless, chronic low-grade inflammation is often associated with various pathologies. Diet could be a promising way of action. Indeed, bioactive peptides derived from the hydrolysis of dietary proteins could modulate key inflammatory factors and consequently delay the onset of these chronic diseases. Furthermore, lactic acid bacteria, components of fermented milk products, exhibit anti-inflammatory properties both in vitro and in vivo studies. Among them, Streptococcus thermophilus (ST) is regularly consumed by a significant part of the population. Studies have shown that some strains of ST display anti inflammatory activity in vitro with an unknown mechanism of action. In this work, it was hypothesized that peptides released after hydrolysis by digestive proteases of the surface or intracellular proteins of this bacterium could be involved at least partially in this activity. Firstly, hydrolysates were obtained by shaving surface proteins with trypsin or pepsin followed or not by trypsinolysis. The tandem mass spectrometry analysis indicated that the majority of the identified peptides belonged to the surface proteins of this bacterium. Secondly, the anti inflammatory activity of the hydrolysates was evaluated in two inflamed cell models. The hydrolysate obtained after tryptic shaving and trypsinolysis of surface proteins of ST LMD 9 significantly decreased the secretion of the pro-inflammatory cytokine IL 8 in lipopolysaccharide (LPS) stimulated HT 29 cells. The same hydrolysate also reduced production of IL 8 and of the pro-inflammatory cytokine IL 1β as well as protein expression levels of Pro IL 1β and COX 2 in LPS-stimulated THP 1 macrophages. It was proposed that the surface protease PrtS could be a source of active peptides during gastrointestinal digestion. To verify this hypothesis, hydrolysates were prepared by shaving with pepsin followed or not by trypsinolysis of the surface proteins of two phenotypically distinct strains of ST: LMD 9 (PrtS+) and CNRZ 21N (PrtS-). Modulation of pro-inflammatory mediators IL 8, IL 1β, Pro IL 1β and COX 2 was assessed in LPS-stimulated THP 1 macrophages and IL 8 in LPS stimulated HT 29 cells. The hydrolysates from the two strains showed an anti inflammatory action but modulation of all these inflammatory mediators was strain, hydrolysate, and concentration dependent. Interestingly, the strain lacking PrtS also showed anti-inflammatory activity. Therefore, peptides released from surface proteins of ST strains by proteases of the gastrointestinal tract during digestion of a product containing this bacterium could exert anti-inflammatory effects and thus could reduce the risk of inflammation related chronic diseases. Finally, the intracellular proteins of the LMD 9 and CNRZ 21N strains were recovered by sonication and hydrolysed with Corolase PP, a mixture of pancreatic proteases. Hydrolysates generated from a fraction of these proteins of both strains demonstrated anti inflammatory action by modulating some of the pro-inflammatory mediators in LPS stimulated THP 1 macrophages. To our knowledge, this is the first study demonstrating the anti inflammatory activity of peptides derived from surface proteins and a fraction of the intracellular proteins of ST strains. These paraprobiotics or postbiotics, likely to be released in the digestive tract of the consumer, could participate in the overall anti inflammatory effect of S. thermophilus which had been demonstrated with certain strains. They could display beneficial effects on human health and therefore could be a promising bioactive ingredient for the development of novel functional foods for the prevention of low grade inflammation
4
Zou, Minghsueh, and 鄒明學. "Effect of Gastrointestinal Protease on the in vitro Digestion of Milk Fat Globules." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/67199245610325611469.
Abstract:
碩士東海大學
畜產與生物科技學系
101
Milk fat globules are composed of a triglyceride core and a natural biological membrane, milk fat globule membrane (MFGM). Proteins account for 70% of MFGM. Certain of those proteins are important for the secretion and structural stability of milk fat globule. However, composition of MFGM is restructured after homogenization, and the newly formed membrane mainly consists of caseins and whey proteins. The aim of this study was to examine the lipolysis of milk fat in raw milk, HTST milk, and homogenized HTST milk by pancreatic lipase during in vitro intestinal and gastrointestinal digestion, with and without the presence of trypsin. The results of in vitro intestinal digestion indicated that whether presence trypsin or not, homogenized HTST milk showed higher level of free fatty acids release than raw milk and HTST milk. Releasable free fatty acids were not significantly different among raw milk, HTST milk, and homogenized HTST milk on gastrointestinal digestion. During in vitro gastrointestinal digestion, the hydrolysis rate of milk fat in raw milk, HTST milk, and homogenized HTST milk increased on early stage of lipolysis after pepsin digestion. However, trypsin treatment could not further increase milk fat hydrolysis rate on gastrointestinal digestion early stage of lipolysis. Homogenized HTST milk and HTST milk fat hydrolysis rate on early stage of trypsin presence in vitro intestinal digestion were higher than trypsin absence in vitro intestinal digestion. In conclusion, gastrointestinal proteases play a coordinative role to increase fresh milk fat hydrolysis on early stage of in vitro digestion.
Books on the topic "Gastrointestinal proteases":
1
Lendeckel, Uwe, and Nigel M. Hooper, eds. Proteases in Gastrointestinal Tissues. Dordrecht: Kluwer Academic Publishers, 2006. http://dx.doi.org/10.1007/1-4020-4483-6.
2
International FOIPAN Symposium. (1988 Shizuoka, Japan). Therapeutic basis of synthetic protease inhibitor: Proceedings of the International FOIPAN Symposium held as a Satellite of the 7th International Symposium on Gastrointestinal Hormones, November 4, 1988, Shizuoka, Japan. Edited by Kanno Tomio 1933-, Miyoshi A, Biomedical Research Foundation (Japan), and International Symposium on Gastrointestinal Hormones. (7th : 1988 : Shizuoka, Japan). Tokyo: Biomedical Research Foundation, 1989.
3
Hooper, Nigel M., and Uwe Lendeckel. Proteases in Gastrointestinal Tissues. Springer, 2006.
4
Hooper, Nigel M., and Uwe Lendeckel. Proteases in Gastrointestinal Tissues. Springer, 2008.
5
Hooper, Nigel M., and Uwe Lendeckel. Proteases in Gastrointestinal Tissues. Springer, 2010.
6
(Editor), Uwe Lendeckel, and Nigel M. Hooper (Editor), eds. Proteases in Gastrointestinal Tissues (Proteases in Biology and Disease). Springer, 2006.
Book chapters on the topic "Gastrointestinal proteases":
1
Banerjee, Sharmistha, Sumit Ghosh, Krishnendu Sinha, and Parames C. Sil. "Unfolding the Mechanism of Proteases in Pathophysiology of Gastrointestinal Diseases." In Pathophysiological Aspects of Proteases, 583–603. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-6141-7_24.
2
Herszényi, L., F. Farinati, M. Plebani, P. Carraro, M. De Paoli, F. Di Mario, S. Kusstatscher, R. Naccarato, and Z. Tulassay. "Cysteine and Serine Proteases in Duodenal Ulcer." In Cell Injury and Protection in the Gastrointestinal Tract, 259–69. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5392-8_26.
3
Knox, David. "Proteases as Vaccines Against Gastrointestinal Nematode Parasites of Sheep and Cattle." In Parasitic Helminths, 399–420. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527652969.ch24.
4
Herszényi, L., F. Farinati, M. Plebani, P. Carraro, M. De Paoli, G. Roveroni, R. Naccarato, and Z. Tulassay. "The Role of Cysteine and Serine Proteases in Gastric Carcinogenesis and Their Prognostic Impact in Gastric Cancer." In Cell Injury and Protection in the Gastrointestinal Tract, 175–85. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5392-8_18.
5
Escobedo, Alejandro, David Fonseca-Hernández, Arturo Alfaro-Díaz, and Luis Mojica. "Biologically Active Peptides from Mung Bean [Vigna radiata (L.) R. Wilczek]." In Frontiers in Bioactive Compounds, 144–59. BENTHAM SCIENCE PUBLISHERS, 2023. http://dx.doi.org/10.2174/9789815123340123040012.
Abstract:
Mung bean (Vigna radiata L.) is a protein-rich pulse mainly cultivated in Asia, where its consumption has been associated with positive health outcomes. Mung bean protein is especially rich in leucine, lysine, phenylalanine, and tyrosine amino acids and it contains the 8S α-globulin as the major seed storage protein. Protein derived products from pulses, such as protein concentrates, hydrolysates, and purified peptide fractions are becoming popular functional foods. Mung bean peptides are enzymatically generated using gastrointestinal and non-gastrointestinal proteases. Protein hydrolysates generated by one or a combination of enzymes have been demonstrated to exert different biological potentials, including antioxidant, antihypertensive, anticancer, and hypocholesterolemic effects. These properties are attributed to the amino acid sequences, the type of enzyme used for hydrolysis, and the purification method. More robust experimental designs must be performed to understand the role and mechanisms of these bioactive peptides with in vivo studies and clinical trials. Furthermore, there is a lack of information related to the incorporation of bioactive peptides into a food matrix while preserving their bioactivity. This chapter provides an overview of the central aspects of mung bean physical structure and chemical composition, protein characteristics, enzymatic production, and the biological potential of mung bean protein hydrolysates and peptides.
6
Becker, Richard C., and Frederick A. Spencer. "Anticoagulants." In Fibrinolytic and Antithrombotic Therapy. Oxford University Press, 2006. http://dx.doi.org/10.1093/oso/9780195155648.003.0040.
Abstract:
Anticoagulant therapy, particularly when used in combination with fibrinolytics and less often platelet antagonists, can cause life-threatening hemorrhage. This supports the importance of coagulation proteases in several phases of thrombus development; paradoxically, several anticoagulants can also cause microvascular and macrovascular thrombotic disorders. Hemorrhage is the most common adverse effect associated with warfarin administration. To predict the risk of bleeding, Beyth and colleagues (1998) developed a 5-point scoring system, with 1 point given for each of the following: . . . • Age greater than 65 . . . . . . • History of stroke . . . . . . • History of gastrointestinal bleeding . . . . . . • Specific comorbid conditions (recent myocardial infarction [MI], elevated serum creatinine, hematocrit <30%, or diabetes) . . . Low-risk patients have a score of 0; intermediate-risk patients, 1 or 2; and high-risk, 3 or 4. The risk of bleeding in these three groupings at 12 months was 3%, 8%, and 30%, respectively. Many commonly used medications have significant interactions with warfarin. In 1994, Wells and colleagues (1994) reviewed all reports of warfarin–drug interactions and found original reports totaling 186. Potentiation of warfarin effect was observed with six antibiotics, five cardiac drugs, two antiinflammatory agents, two histamine2-blockers, and alcohol in persons with concomitant liver disease. Inhibition of warfarin effect was noted with three antibiotics, three central nervous system (CNS) drugs, cholestyramine, and sucralfate. An important interaction between acetaminophen and warfarin has also been recognized (Hylek et al., 1998), and certain herbal remedies, such as ginkgo biloba, ginseng, and garlic, may enhance the effects of warfarin. The first step in the management of bleeding is to stop the drug; however, recovery of clotting factor levels may take several days, depending upon the vitamin K content of the patient’s diet and rate of intrinsic metabolism. To rapidly raise coagulant factor concentrations in patients with life-threatening hemorrhage, clotting factor concentrates are given (Makris et al., 1997). The older concentrates were plasma-derived and consisted mainly of activated prothrombin complex factors. They had the disadvantages of thrombogenicity and potential for transmission of infectious agents.
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Dale, David C., and Andrew G. Aprikyan. "Cyclic and Congenital Neutropenia Due to Defects in Neutrophil Elastase." In Primary Immunodeficiency Diseases, 565–69. Oxford University PressNew York, NY, 2006. http://dx.doi.org/10.1093/oso/9780195147742.003.0039.
Abstract:
Abstract Severe neutropenia predisposes patients to recurrent bacterial infections (Boxer and Dale, 2002). These infections are usually caused by organisms that are resident on body surfaces— i.e., staphylococci, streptococci, and enteric organisms. In general, the susceptibility is inversely related to the neutrophil count. Infections of two general types occur: superficial infections of the skin and oropharyngeal areas and more serious infections involving the lung and gastrointestinal tract, which may be complicated by sepsis. In general, these infections are poorly responsive to antibiotics. Both cyclic and congenital neutropenias are now effectively treated with the hematopoietic growth factor, granulocyte colony–stimulating factor (G-CSF). Recent studies have shown that both of these diseases are attributable to mutations in the gene for neutrophil elastase, a protease made and packaged in the primary granules of neutrophils early in their differentiation from the hematopoietic stem cells.
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Howbert, J. J., K. L. Lobb, R. F. Brown, J. K. Reel, D. A. Neel,, N. R. Mason, L. G. Mendelsohn, J. P. Hodgkiss,, and J. S. Kelly. "A novel series of non-peptide CCK and gastrin antagonists: medicinal chemistry and electrophysiological demonstration of antagonism." In Multiple Cholecystokinin Receptors in the CNS, 28–37. Oxford University PressOxford, 1992. http://dx.doi.org/10.1093/oso/9780198577560.003.0003.
Abstract:
Abstract The neuropeptides are a rapidly growing class of mediators which have important roles in a great diversity of physiological processes, particularly in the CNS and the gastrointestinal tract. Historically, the tools available for studying these processes have been almost exclusively the peptides themselves and related peptide agonists and antagonists. This has proved a considerable hindrance to research because of the pharmacokinetic shortcomings of many peptides, which include poor oral absorption, protease lability, and poor blood-brain barrier penetration. As a result, attention has recently turned to the development of non-peptide ligands for neuropeptide receptors. One of the most generally successful approaches has been the identification of non-peptide lead structures through broad screening with radio-ligand binding assays. Initial leads are then optimized with respect to potency, selectivity, and other desired properties via systematic manipulation of the structure. This method was previously used to develop non-peptide CCK and gastrin antagonists, using initial screening at a peripheral (CCKA) type CCK receptor (Chang et al. 1985; Evans et al. 1986).
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Shah, Manoj. "Intervention of PAR-2 Mediated CGRP in Animal Model of Visceral Hyperalgesia." In Animal Models and Experimental Research in Medicine [Working Title]. IntechOpen, 2023. http://dx.doi.org/10.5772/intechopen.106859.
Abstract:
Protease-activated receptor-2 (PAR-2) mediates calcitonin gene-related peptide (CGRP) release and collectively plays a crucial role in inflammation-induced visceral hyperalgesia (VH). The present review chapter outlines the substantial advances that elucidated the underlying role of PAR-2 and CGRP in gut inflammation-induced VH and highlights their relevancies in the management of VH. PAR-2 is expressed in a wide range of gastrointestinal cells and its activation on primary afferent nerves by tryptase, trypsin or cathepsin-S is the key mechanism of sensitization during intestinal inflammation. The activated PAR-2 sensitizes transient receptor potential vanilloid subtype-1 receptors and triggers the release of substance-P (SP) and CGRP that are involved both in the transmission and modulation of VH. Approximately, two-thirds of sensory neurons express PAR-2 and 40% of the PAR-2-expressing sensory neurons also express SP and CGRP. Accumulating set of experiments devised that the blockade or antagonism of PAR-2 in inflammatory diseases of the gut depicts double advantages of reducing inflammation and VH. Simultaneously, the uses of CGRP-antagonists inhibit VH and completely suppress PAR-2-agonists-induced intestinal inflammation in animals. However, further study is imperative to improve our understanding of the blockade or antagonism of PAR-2 and CGRP release before its implication as a novel therapeutic for the clinical management of VH in human patients.
Conference papers on the topic "Gastrointestinal proteases":
1
Guice, Justin, Caroline Best, Morgan Hollins, Kelly Tinker, and Sean Garvey. "Fungal Digestive Enzymes Promote Macronutrient Hydrolysis in the INFOGEST in vitro Simulation of Digestion." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/agsn3911.
Abstract:
Fungal enzymes are common ingredients in dietary supplements that support digestion. At adequate concentrations, exogenous enzymes may improve digestion by hydrolyzing macronutrients beyond acid-mediated hydrolysis, endogenous gastric pepsin, and pancreatic enzymes alone. The purpose of this study was to test the hydrolytic efficacy of 6 commercial fungal enzymes—three proteases, a lipase, an amylase, and a glucoamylase—in the INFOGEST static in vitro simulation of gastrointestinal digestion. The efficacy of 5 doses of each enzyme was determined by measuring free amino nitrogen (FAN), glycerol, maltose, and glucose concentrations following salivary-gastric (SG) and full salivary-gastric-intestinal (SGI) simulations of digestion of an oral nutritional supplement. In the SG simulation, the 3 proteases, lipase, and combination of amylase and glucoamylase promoted greater hydrolysis of dietary protein, fat, and carbohydrates, respectively, compared to control conditions. Acid protease (Aspergillus niger) treatment increased FAN concentrations than controls from 27% at the lowest dose to 142% greater than controls at the highest dose (p<0.0001). Fungal protease (A. oryzae) treatment increased FAN concentration at the highest dose (160,000 HUT, p=0.0115). Peptidase (A. melleus) treatment promoted higher FAN concentrations, up to 50% increase at the highest dose (160 LAPU, p<0.0001). Glycerol concentrations increased across all lipase treatments (p<0.0001), from 4.1-fold to 11.2-fold increases at the lowest and highest doses, respectively. All doses of amylase increased glucose concentrations (p<0.0001), and maltose concentrations started increasing at 4,000 SKB units (p=0.0010). In the SGI simulation, FAN concentrations following protease treatments were similar to control, suggesting little benefit beyond pancreatin alone in this static simulation of healthy digestion. Lipase and amylase/glucoamylase treatments, however, did increase glycerol (p<0.0001) and maltose/glucose concentrations (p<0.0001), respectively, compared to controls in the full SGI simulation. These data demonstrate that exogenous, fungal enzymes can improve macronutrient digestion under the acidic conditions of the gastric simulation, as well as the intestinal simulation.
2
Kumrungsee, Thanutchaporn, Norihisa Kato, Toshiro Matsui, and Yongshou Yang. "Plant and gut microbiota-derived protein metabolites and potential health functions." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/envt3719.
Abstract:
Bioactive peptides can be obtained from protein hydrolysates through in vitro enzymatic hydrolysis, gastrointestinal digestion, and microbial fermentation. Recent emerging research suggests that prebiotic-stimulated gut microbiota also plays a role in generating bioactive peptides and amino acids in gut. In this study, we examined if enzymatic hydrolysis of soybean and wheat germ, plant materials often used in oil industry, can generate antihypertensive peptides and determined if prebiotic digestive enzymes can induce the production of gut microbiota-derived amino acids. In the first experiment, soybean and wheat germ were hydrolyzed by protease enzymes. Then, their hydrolysates were subjected to peptide isolation and identification. Identified peptides were subjected to test for their potential antihypertensive activities. For the second experiment, rodents were fed an Aspergillus-derived protease- or lipase-mixed diet for 2 weeks. Then, cecum contents were collected for bacteria and metabolite analyses. As a result, we found that His-Gly-Lys from soybean hydrolysate strongly inhibited angiotensin II-induced elevated intracellular Ca2+ concentration in vascular smooth muscle cells (VSMCs). Trp-Val and Trp-Ile from wheat germ hydrolysate were found to inhibit Ca2+-calmodulin (CaM)-dependent protein kinase II (CaMK II), a protein kinase promoting hypertension by inducing Ca2+ influx into VSMCs, in rat thoracic aorta rings. These findings suggest the potential of the plant-derived peptides in preventing hypertension and vascular-related diseases. In the second experiment, we found that the dietary protease and lipase increased Bifidobacterium and Lactobacillus probiotics and induced the production of probiotic-derived amino acids, taurine, ornithine, and γ-aminobutyric acid. Since these amino acids have versatile functions including in gut health modulation and brain functions, it can be hypothesized that the dietary prebiotic-digestive enzymes may be beneficial for gut health and brain functions. This study suggests the possibility of applying oil processing by-products in the production of functional food ingredients including bioactive peptides and amino acids.
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Guice, Justin, Morgan Hollins, Caroline Best, Kelly Tinker, and Sean Garvey. "Fungal Multi-enzyme Blend Promotes Improved Macronutrient Hydrolysis of Mixed Meal Substrates in the INFOGEST in vitro Simulation of Digestion." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/fsgu7847.
Abstract:
Fungal enzymes are often combined in dietary supplements to support digestive health. The purpose of this study was to test the effects of a mixture of 6 fungal enzymes (BC-006) on macronutrient digestion in the INFOGEST static simulation of gastrointestinal digestion in vitro. Substrates included an oral nutritional supplement (ONS), heated test meal (HTM) with grilled chicken, steamed peas, and potatoes, and a canned test meal (CTM) version. BC-006 contains fungal protease (Aspergillus oryzae), acid protease (A. niger), peptidase (A. melleus), lipase (Candida cylindracea), alpha-amylase (A. oryzae), and glucoamylase (A. niger). Three doses of BC-006 (0.5X, 1X, and 2X recommended dose) were evaluated on free amino nitrogen (FAN), glycerol, maltose, and glucose release from substrates. Following the gastric simulation, all doses of BC-006 increased FAN concentrations across all substrates, compared to control conditions with pepsin alone (p≤0.0001). HPLC analysis showed that BC-006 treatment increased the concentrations of leucine (ONS: 4.5-fold, HTM: 4.1-fold, CTM: 3.7-fold) and total essential amino acids (2.8-fold, 87%, 71%, respectively), compared to controls (p<0.05). In the intestinal phase, however, no differences in FAN concentrations were observed. BC-006 (1X) increased glycerol concentrations at least 3.3-fold higher in the gastric simulation (HTM, p=0.0446) and at least 76% higher in the intestinal simulation (HTM, p=0.0003). Glucose released increased with BC-006 dose for all substrates in the gastric and intestinal simulations (p<0.0001). Maltose release increased with BC-006 dose in the gastric simulation of ONS digestion (p<0.0001), but no differences were observed with HTM and CTM. In the intestinal simulation, maltose release increased with BC-006 dose in the gastric simulation of ONS digestion (p=0.0002), but decreased with increasing BC-006 dose in the gastric simulation with HTM (p=0.0077) and CTM (p=0.0083). Altogether, the BC-006 blend improved hydrolysis of all macronutrients in the gastric simulation, and lipid and carbohydrate hydrolysis in the intestinal simulation.
4
Alsulami, Haneen Hamed. "INVESTIGATING THE EFFECT OF CIGARETTE SMOKING ON THE NKX3.1 AND TMPRSS2 GENES ASSOCIATED WITH MALE FERTILITY." In Dubai International Conference on Research in Life-Science & Healthcare, 22-23 February 2024. Global Research & Development Services, 2024. http://dx.doi.org/10.20319/icrlsh.2024.3041.
Abstract:
Cigarette's smoking has a wide negative impact on human health, and it's have been related to many serious issues like cancer, heart disease, respiratory system, and number of health problems. Also, smoking can affect fertility in men by affecting the sperm on several levels. Our research will investigate the genetic risk factors in male by focusing on NKX3.1 and TMPRSS2 genes related to male fertility and investigate the correlation between the gene’s polymorphisms of three groups (smokers, non-smokers, and infertile men). The NKX3.1 or NK3 homeobox 1 located on chromosome 8 is the first known prostate epithelium-specific marker it is an androgen regulated transcriptional and tumor suppressor gene this gene encodes for a homeobox-containing transcription factor and the transcription factor involved in development of the testes and prostate. there are not enough research data about NKX3.1 single nucleotide’s DNA variations and interaction with cigarettes smoking. The TMPRSS2 gene or transmembrane serine protease 2 is located on chromosome 21 is an endothelial cell surface gene encodes a protein that belongs to the serine protease family. TMPRSS2 is expressed in prostate epithelial cells and is needed for normal prostate function. It’s also expressed across the gastrointestinal (digestive) tract, such as in intestinal epithelial cells and across the respiratory tract. This gives TMPRSS2 gene an advantage to study or investigate gene expression influenced by lifestyle habits such as cigarettes smoke. Most of today research is confined to respiratory and cardiovascular system affected by cigarettes smoke but this research will investigate the relation between cigarettes smoking and fertility problems in men by selecting two fertility related genes (NKX3.1 and TMPRSS2) and analyzing single nucleotide polymorphisms (SNP) From 75 blood samples collected from 25 smokers ,25 control and 25 infertile\sub-fertile men. To amplify the regions of interest within the applied gene from extracted DNA, a polymerase chain reaction (qPCR) will be used, and ELISA technique to measure serum hormones level (Testosterone and prolactin and Estrogen). We expect this research to provide new information from a new aspect about the effect of cigarettes smoking on those genes and their relation to male infertility.