Journal articles: 'Bowman-Birk inhibitor'

1

Wu, Y. Victor, and David J. Sessa. "Conformation of Bowman-Birk Inhibitor." Journal of Agricultural and Food Chemistry 42, no. 10 (October 1994): 2136–38. http://dx.doi.org/10.1021/jf00046a012.

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Chen, Xi, Dong Chen, Linyuan Huang, Xiaoling Chen, Mei Zhou, Xinping Xi, Chengbang Ma, Tianbao Chen, and Lei Wang. "Identification and Target-Modification of SL-BBI: A Novel Bowman–Birk Type Trypsin Inhibitor from Sylvirana latouchii." Biomolecules 10, no. 9 (August 28, 2020): 1254. http://dx.doi.org/10.3390/biom10091254.

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The peptides from the ranacyclin family share similar active disulphide loop with plant-derived Bowman–Birk type inhibitors, some of which have the dual activities of trypsin inhibition and antimicrobial. Herein, a novel Bowman–Birk type trypsin inhibitor of the ranacyclin family was identified from the skin secretion of broad-folded frog (Sylvirana latouchii) by molecular cloning method and named as SL-BBI. After chemical synthesis, it was proved to be a potent inhibitor of trypsin with a Ki value of 230.5 nM and showed weak antimicrobial activity against tested microorganisms. Modified analogue K-SL maintains the original inhibitory activity with a Ki value of 77.27 nM while enhancing the antimicrobial activity. After the substitution of active P1 site to phenylalanine and P2′ site to isoleucine, F-SL regenerated its inhibitory activity on chymotrypsin with a Ki value of 309.3 nM and exhibited antiproliferative effects on PC-3, MCF-7 and a series of non-small cell lung cancer cell lines without cell membrane damage. The affinity of F-SL for the β subunits in the yeast 20S proteasome showed by molecular docking simulations enriched the understanding of the possible action mode of Bowman–Birk type inhibitors. Further mechanistic studies have shown that F-SL can activate caspase 3/7 in H157 cells and induce apoptosis, which means it has the potential to become an anticancer agent.

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Wan, X. Steven, David G. Serota, Jeffrey H. Ware, James A. Crowell, and Ann R. Kennedy. "Detection of Bowman-Birk Inhibitor and Anti-Bowman-Birk Inhibitor Antibodies in Sera of Humans and Animals Treated With Bowman-Birk Inhibitor Concentrate." Nutrition and Cancer 43, no. 2 (July 2002): 167–73. http://dx.doi.org/10.1207/s15327914nc432_7.

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Othman, Tajul Ariffien, Norliza Abu Bakar, Rabiatul Adawiah Zainal Abidin, Maziah Mahmood, Noor Baity Saidi, and Noor Azmi Shaharuddin. "Potential of Plantâ€™s Bowman-Birk Protease Inhibitor in Combating Abiotic Stresses: A Mini Review." Bioremediation Science and Technology Research 2, no. 2 (January 31, 2015): 25–33. http://dx.doi.org/10.54987/bstr.v2i2.179.

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Bowman-Birk Inhibitor (BBI) is one of the subfamilies of serine protease inhibitors. Numerousstudies have shown that in plants, BBI functions as part of their defense mechanism againstpathogens and microorganisms. The BBI is also known to have anti-carcinogenic properties.Furthermore, the BBI has been reported to function in controlling abiotic stresses such assalinity and drought stresses.. Abiotic stresses are the major problems in agricultural industry.Therefore, numerous researches have been carried out to characterize the BBI and to determineits roles during biotic and abiotic stresses. This paper presents a review regarding therelationship between Bowman-Birk inhibitor and the plant defensive mechanism against abioticstresses.

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Pusztai, A., G. Grant, S. Bardocz, K. Baintner, E. Gelencser, and S. W. Ewen. "Both free and complexed trypsin inhibitors stimulate pancreatic secretion and change duodenal enzyme levels." American Journal of Physiology-Gastrointestinal and Liver Physiology 272, no. 2 (February 1, 1997): G340—G350. http://dx.doi.org/10.1152/ajpgi.1997.272.2.g340.

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Secretion of pancreatic digestive enzymes was measured in pancreatic cannulated rats after duodenal stimulation with Kunitz or Bowman-Birk protease inhibitors or their complexes with trypsin and/or chymotrypsin. Free and complexed inhibitors were bound by the duodenal epithelium, stimulated the discharge of cholecystokinin, and significantly increased secretion rates of alpha-amylase, trypsinogen, and chymotrypsinogen. Inasmuch as secretion rates returned to basal levels with cholecystokinin-A receptor antagonists, the stimulation was likely to be mediated by cholecystokinin. Soya factors also influenced the duodenal concentration of pancreatic enzymes under simulated feeding conditions. Thus the level of alpha-amylase increased while the trypsin concentration decreased in rats gavaged with free or complexed inhibitors. The same was true for chymotrypsin when the Bowman-Birk inhibitor was used, but the Kunitz inhibitor and its trypsin complex actually raised the luminal concentration of chymotrypsin. Accordingly, because soya inhibitors remained effective in stimulating pancreatic secretion after elimination of their inhibitory activity by complex formation, it is questionable whether the signal for cholecystokinin secretion was solely due to lowering of duodenal protease levels.

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&NA;. "Bowman-Birk inhibitor concentrate for chemoprevention?" Inpharma Weekly &NA;, no. 1272 (January 2001): 11. http://dx.doi.org/10.2165/00128413-200112720-00024.

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Song, Hyun Kyu, and Se Won Suh. "Preliminary X-ray crystallographic analysis of Bowman–Birk trypsin inhibitor from barley seeds." Acta Crystallographica Section D Biological Crystallography 54, no. 3 (May 1, 1998): 441–43. http://dx.doi.org/10.1107/s0907444997010986.

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Bowman–Birk trypsin inhibitor from barley seeds has been crystallized at room temperature using polyethylene glycol as precipitant. The crystal is tetragonal, belonging to the space group P41212 (or P43212), with unit cell parameters of a = b = 62.48 and c = 94.63 Å. The asymmetric unit contains one molecule of Bowman–Birk trypsin inhibitor with corresponding crystal volume per protein mass (Vm ) of 2.89 Å3 Da−1 and the solvent content of 57% by volume. The crystals diffract to at least 1.9 Å Bragg spacing upon exposure to synchrotron X-rays. X-ray data to 1.9 Å have been collected from a native crystal.

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Miao, Yuxi, Guanzhu Chen, Xinping Xi, Chengbang Ma, Lei Wang, James F. Burrows, Jinao Duan, Mei Zhou, and Tianbao Chen. "Discovery and Rational Design of a Novel Bowman-Birk Related Protease Inhibitor." Biomolecules 9, no. 7 (July 14, 2019): 280. http://dx.doi.org/10.3390/biom9070280.

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Anuran amphibian skin secretions are a rich source of peptides, many of which represent novel protease inhibitors and can potentially act as a source for protease inhibitor drug discovery. In this study, a novel bioactive Bowman-Birk type inhibitory hexadecapeptide of the Ranacyclin family from the defensive skin secretion of the Fukien gold-striped pond frog, Pelophlax plancyi fukienesis, was successfully isolated and identified, named PPF-BBI. The primary structure of the biosynthetic precursor was deduced from a cDNA sequence cloned from a skin-derived cDNA library, which contains a consensus motif representative of the Bowman-Birk type inhibitor. The peptide was chemically synthesized and displayed a potent inhibitory activity against trypsin (Ki of 0.17 µM), as well as an inhibitory activity against tryptase (Ki of 30.73 µM). A number of analogues of this peptide were produced by rational design. An analogue, which substituted the lysine (K) at the predicted P1 position with phenylalanine (F), exhibited a potent chymotrypsin inhibitory activity (Ki of 0.851 µM). Alternatively, a more potent protease inhibitory activity, as well as antimicrobial activity, was observed when P16 was replaced by lysine, forming K16-PPF-BBI. The addition of the cell-penetrating peptide Tat with a trypsin inhibitory loop resulted in a peptide with a selective inhibitory activity toward trypsin, as well as a strong antifungal activity. This peptide also inhibited the growth of two lung cancer cells, H460 and H157, demonstrating that the targeted modifications of this peptide could effectively and efficiently alter its bioactivity.

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de Freitas, Sonia Maria, Luciano Paulino Silva, Jose Roberto S. A. Leite, and Carlos Bloch Jr. "Stability of a black eyed pea trypsin/chymotrypsin inhibitor (BTCI)." Protein & Peptide Letters 7, no. 6 (December 2000): 397–401. http://dx.doi.org/10.2174/092986650706221207164315.

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Abstract: The stability of BTCI has been investigated as function of pH and temperature, following its inhibitory activity against trypsin. The isolated inhibitor of 9,084 Oa is stable over pH 3 to 12 at 25°C. BTCI showed high thermal stability ranging from 25 to 95°C at pH 3 and 7. However, the protein lost about 20% of its inhibitory activity over 75°C at pH 8.2. The results indicated that BTCI is extremely stable to heat and pH as typical of Bowman-Birk inhibitors.

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10

Ahmed, E. M., and J. A. Applewhite. "Characterization of Trypsin Inhibitor in Florunner Peanut Seeds (Arachis hypogaea L.)1." Peanut Science 15, no. 2 (July 1, 1988): 81–84. http://dx.doi.org/10.3146/i0095-3679-15-2-10.

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Abstract Florunner peanut seeds contained five trypsin isoinhibitors. Amino acid profiles of the trypsin inhibitors fraction showed high levels of aspartic acid, half-cystine and serine and low levels of histidine and tyrosine. The molecular weight of the inhibitor was 8.3 KDa. The presence of multiforms of this inhibitor, its low molecular weight and the high amount of half-cystine indicate that peanut trypsin inhibitor is of the Bowman-Birk type.

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Yang, Jie, Chengliang Tong, Junmei Qi, Xiaoying Liao, Xiaokun Li, Xu Zhang, Mei Zhou, et al. "Engineering and Structural Insights of a Novel BBI-like Protease Inhibitor Livisin from the Frog Skin Secretion." Toxins 14, no. 4 (April 12, 2022): 273. http://dx.doi.org/10.3390/toxins14040273.

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The Bowman–Birk protease inhibitor (BBI) family is a prototype group found mainly in plants, particularly grasses and legumes, which have been subjected to decades of study. Recently, the discovery of attenuated peptides containing the canonical Bowman–Birk protease inhibitory motif has been detected in the skin secretions of amphibians, mainly from Ranidae family members. The roles of these peptides in amphibian defense have been proposed to work cooperatively with antimicrobial peptides and reduce peptide degradation. A novel trypsin inhibitory peptide, named livisin, was found in the skin secretion of the green cascade frog, Odorrana livida. The cDNA encoding the precursor of livisin was cloned, and the predicted mature peptide was characterized. The mature peptide was found to act as a potent inhibitor against several serine proteases. A comparative activity study among the native peptide and its engineered analogs was performed, and the influence of the P1 and P2′ positions, as well as the C-terminal amidation on the structure–activity relationship for livisin, was illustrated. The findings demonstrated that livisin might serve as a potential drug discovery/development tool.

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12

BIRK, YEHUDITH. "The Bowman-Birk inhibitor. Trypsin- and chymotrypsin-inhibitor from soybeans." International Journal of Peptide and Protein Research 25, no. 2 (January 12, 2009): 113–31. http://dx.doi.org/10.1111/j.1399-3011.1985.tb02155.x.

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13

CLARKE, E. J., and J. WISEMAN. "Developments in plant breeding for improved nutritional quality of soya beans II. Anti-nutritional factors." Journal of Agricultural Science 134, no. 2 (March 2000): 125–36. http://dx.doi.org/10.1017/s0021859699007443.

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Nutritional value of most plant materials is limited by the presence of numerous naturally occurring compounds which interfere with nutrient digestion and absorption. Although processing is employed widely in removal of these factors, selection of cultivars of soya beans with inherently low levels would have a considerable impact on efficiency of non-ruminant livestock production. The review considers the role of plant breeding in achieving this objective. The most abundant trypsin inhibitors are the Kunitz and the Bowman–Birk inhibitors, containing 181 and 71 amino acids respectively. The Kunitz inhibitor is present at a concentration of 1·4 g/kg of total seed contents and the Bowman–Birk inhibitor 1·6 g/kg. A large number of isoforms of the Bowman–Birk inhibitor have been described in soya bean cultivars and it has been shown that the general properties of the inhibitor are, in fact, attributable to different isoforms. Nulls for both Bowman–Birk and Kunitz trypsin inhibitors have been identified, allowing new low trypsin inhibitor cultivars to be produced. However, research into breeding for low trypsin inhibitor cultivars currently has limited application as trypsin inhibitors contribute a major proportion of the methionine content of soya beans. Trypsin inhibitors are thought to be involved in the regulation of and protection against unwanted proteolysis in plant tissues and also act as a defence mechanism against attack from diseases, insects and animals. Hence, in breeding programmes for low trypsin inhibitor cultivars, alternative protection for growing plants must be considered. Use of soya beans in non-ruminant animal feeds is limited by the flatulence associated with their consumption. The principal causes appear to be the low molecular weight oligosaccharides containing α-galactosidic and β-fructosidic linkages; raffinose and stachyose. Non-ruminants do not have the α-galactosidase enzyme necessary for hydrolysing the α-galactosidic linkages of raffinose and stachyose to yield readily absorbable sugars. Soya beans contain between 6·8 and 17·5 g of phytic acid/kg; a ring form of phosphorus (P) which chelates with proteins and minerals to form phytates not readily digested within the gut of non-ruminants. One approach for over-coming the effects of phytic acid is through synthesis of phytase in the seeds of transgenic plants. Currently, recombinant phytase produced in soya beans is not able to withstand the processing temperatures necessary to inactivate proteinaceous anti-nutritional factors present. Soya bean lectins have the ability to bind with certain carbohydrate molecules (N-acetyl-D-galactosamine and galactose) without altering the covalent structure. Lectins are present in raw soya bean at a concentration of between 10 and 20 g/kg. Purified soya bean agglutinin is easily inactivated by hydrothermal treatment but in complex diets binding with haptenic carbohydrates may confer protection against denaturation. The majority of research into soya bean lectins is carried out using laboratory animals so very limited information is available on their in vivo effects in farm animals. This review is concerned specifically with breeding but there are other means of improving nutritive value, for example processing which may alter protein structure and therefore functionality of proteinaceous anti-nutritional factors present.

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Lisak, Katarina, Jose Toro-Sierra, Ulrich Kulozik, Rajka Božanić, and Seronei Chelulei Cheison. "Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification." Journal of Dairy Research 80, no. 1 (September 21, 2012): 14–20. http://dx.doi.org/10.1017/s0022029912000416.

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The present study examines the resistance of the α-lactalbumin to α-chymotrypsin (EC 3.4.21.1) digestion under various experimental conditions. Whey protein isolate (WPI) was hydrolysed using randomised hydrolysis conditions (5 and 10% of WPI; pH 7·0, 7·8 and 8·5; temperature 25, 37 and 50 °C; enzyme-to-substrate ratio, E/S, of 0·1%, 0·5 and 1%). Reversed-phase high performance liquid chromatography (RP-HPLC) was used to analyse residual proteins. Heat, pH adjustment and two inhibitors (Bowman–Birk inhibitor and trypsin inhibitor from chicken egg white) were used to stop the enzyme reaction. While operating outside of the enzyme optimum it was observed that at pH 8·5 selective hydrolysis of β-lactoglobulin was improved because of a dimer-to-monomer transition while α-la remained relatively resistant. The best conditions for the recovery of native and pure α-la were at 25 °C, pH 8·5, 1% E/S ratio, 5% WPI (w/v) while the enzyme was inhibited using Bowman–Birk inhibitor with around 81% of original α-la in WPI was recovered with no more β-lg. Operating conditions for hydrolysis away from the chymotrypsin optimum conditions offers a great potential for selective WPI hydrolysis, and removal, of β-lg with production of whey protein concentrates containing low or no β-lg and pure native α-la. This method also offers the possibility for production of β-lg-depleted milk products for sensitive populations.

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Ciric, Bogoljub, Tarik Touil, Anjali Gupta, Kenneth Shindler, and Abdolmohamad Rostami. "The protease inhibitor, Bowman-Birk inhibitor, suppresses experimental autoimmune encephalomyelitis (131.33)." Journal of Immunology 178, no. 1_Supplement (April 1, 2007): S244. http://dx.doi.org/10.4049/jimmunol.178.supp.131.33.

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Abstract The Bowman-Birk inhibitor (BBI) is a soybean-derived serine protease inhibitor. BBI concentrate (BBIC) is enriched with BBI, but is predominantly made up of other ingredients. In our previous study we found that oral administration of BBIC to Lewis rats with EAE resulted in significant clinical and histological suppression of disease. In the present study we investigated the effect of BBI using mouse EAE models and pure BBI. We found that both I.P. and oral treatment with BBI (typically 1 mg/day BBI) in SJL/PLP139–151, or C57BL/6/MOG35–55 models, significantly improved clinical and histological parameters of EAE (disease onset, severity, weight loss, inflammation and demyelination). This was true for different treatment regimens as regards the day of treatment initiation relative to immunization for EAE induction. In most experiments antigen-specific proliferation of immune cells derived from BBI-treated mice was significantly lower relative to control groups. In the SJL model of optic neuritis BBI significantly reduced the incidence of neuritis, inhibited inflammation and prevented loss of retinal ganglion cells. Using Boyden’s chamber assay we found that BBI inhibited invasiveness of activated splenocytes through the matrigel barrier. These results indicate that BBI is an excellent candidate for oral therapy in multiple sclerosis.

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Grant, Grorge, Patrica M. Dorward, Wendy C. Buchan, Julia C. Armour, and Arpad Pusztai. "Consumption of diets containing raw soya beans (Glycine max), kidney beans (Phaseolus vulgaris), cowpeas (Vigna unguiculata) or lupin seeds (Lupinus angustifolius) by rats for up to 700 days: effect on body composition and organ weights." British Journal of Nutrition 73, no. 1 (January 1995): 17–29. http://dx.doi.org/10.1079/bjn19950005.

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Feeding trials have been done with rats to assess the effects of long-term (700 d) consumption of diets based on raw cowpeas (Vigna unguiculata; moderate Bowman–Birk inhibitor content, low lectin content), lupin seeds (Lupinus angustifolius; low lectin and protease inhibitor content) or soya beans (Glycine max; high Kunitz inhibitor content, moderate Bowman–Birk inhibitor content, moderate lectin content) or diets containing low levels of raw kidney bean (Phaseolus vulgaris; high lectin content, low Bowman–Birk inhibitor content) on body weight and composition and organ weights. All the legume-based diets reduced feed conversion efficiency and growth rates during the initial 250 d. However, after 250 d the weight gains by rats given legume-based diets were similar to those of controls given the same daily feed intake. Long-term consumption of diets containing low levels of kidney bean significantly altered body composition of rats. The levels of lipid in the body were significantly reduced. As a result, carcasses of these rats contained a higher proportion of muscle/protein than did controls. Small-intestine relative weight was increased by short- and long-term consumption of the kidney-bean-based diet. However, the increase in relative pancreatic weight observed at 30d did not persist long term. None of the other legume-based diets caused any significant changes in body composition. However, long-term exposure to a soya-bean- or cowpea-based diet induced an extensive increase in the relative and absolute weights of the pancreas and caused an increase in the incidence of macroscopic pancreatic nodules and possibly pancreatic neoplasia. Long-term consumption of the cowpea-, kidney-bean-, lupin-seed- or soya-bean-based diets by rats resulted in a significant increase in the relative weight of the caecum and colon.

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17

Dong, Shu Ting, Hong Zhang, Na Xu, Ping Li, Si Si Xu, and Chun Yu Xi. "Effects of Two Trypsin Inhibitors on Trypsin in Activity and Structure." Advanced Materials Research 1073-1076 (December 2014): 1824–27. http://dx.doi.org/10.4028/www.scientific.net/amr.1073-1076.1824.

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Two reversible trypsin inhibitors, Kunitz trypsin inhibitor (KTI) and Bowman-Birk trypsin inhibitor (BBI) were compared to find the more optimal one as the inhibit factor during trypsin immobilization. Fluorescence spectroscopy, UV–visible absorption spectroscopy and circular dichroism (CD) spectroscopy were used to explore the effects of the two inhibitors on trypsin in activity and structure. The results showed that both inhibitors combined with trypsin in 1:1. CD circular dichroism spectroscopy showed that KTI and BBI led to different changes in trypsin second structure. The results can help us find out the mechanism between the two inhibitors and trypsin and select the more optimal inhibitor in trypsin immobilization.

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Elden, T. C. "Effects of Proteinase Inhibitors and Plant Lectins on the Adult Alfalfa Weevil (Coleoptera: Curculionidae)." Journal of Entomological Science 35, no. 1 (January 1, 2000): 62–69. http://dx.doi.org/10.18474/0749-8004-35.1.62.

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The effects of selected proteinase inhibitors and plant lectins of alfalfa weevil, Hypera postica (Gyllenhal), adult foliar feeding and fecundity were significantly inhibited by the cysteine proteinase inhibitors E-64, pHMB, and leupeptin at a concentration of 0.1%. Pepstatin (aspartic inhibitor) at 0.5% and soybean Bowman-Birk trypsin inhibitor (serine) at 1.0% had no significant effect on adult foliar feeding, survival, or fecundity. Three of the four lectins tested significantly inhibited adult foliar feeding and fecundity at a concentration of 0.5%. A lectin from wheat and one from pea were the only two protein inhibitors tested to significantly inhibit adult survival. Results support a previous study that indicates the alfalfa weevil uses cysteine proteinases as major digestive enzymes. This study is one of few which demonstrates the effects of specific protein inhibitors on the adult stage of a foliar feeding insect species.

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19

McBride, Jeffrey, and Robin Leatherbrrow. "Synthetic Peptide Mimics of the Bowman-Birk Inhibitor Protein." Current Medicinal Chemistry 8, no. 8 (July 1, 2001): 909–17. http://dx.doi.org/10.2174/0929867013372832.

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Morris, C. A., J. T. Selsby, L. D. Morris, K. Pendrak, and H. L. Sweeney. "Bowman-Birk inhibitor attenuates dystrophic pathology in mdx mice." Journal of Applied Physiology 109, no. 5 (November 2010): 1492–99. http://dx.doi.org/10.1152/japplphysiol.01283.2009.

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Bowman-Birk inhibitor concentrate (BBIC), a serine protease inhibitor, has been shown to diminish disuse atrophy of skeletal muscle. Duchenne muscular dystrophy (DMD) results from a loss of dystrophin protein and involves an ongoing inflammatory response, with matrix remodeling and activation of transforming growth factor (TGF)-β1 leading to tissue fibrosis. Inflammatory-mediated increases in extracellular protease activity may drive much of this pathological tissue remodeling. Hence, we evaluated the ability of BBIC, an extracellular serine protease inhibitor, to impact pathology in the mouse model of DMD (mdx mouse). Mdx mice fed 1% BBIC in their diet had increased skeletal muscle mass and tetanic force and improved muscle integrity (less Evans blue dye uptake). Importantly, mdx mice treated with BBIC were less susceptible to contraction-induced injury. Changes consistent with decreased degeneration/regeneration, as well as reduced TGF-β1 and fibrosis, were observed in the BBIC-treated mdx mice. While Akt signaling was unchanged, myostatin activitation and Smad signaling were reduced. Given that BBIC treatment increases mass and strength, while decreasing fibrosis in skeletal muscles of the mdx mouse, it should be evaluated as a possible therapeutic to slow the progression of disease in human DMD patients.

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Kennedy, Ann R., Paul C. Billings, X. Steven Wan, and Paul M. Newberne. "Effects of Bowman-Birk Inhibitor on Rat Colon Carcinogenesis." Nutrition and Cancer 43, no. 2 (July 2002): 174–86. http://dx.doi.org/10.1207/s15327914nc432_8.

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Madden, M. "Proteolysis of soybean bowman-birk trypsin inhibitor during germination,." Phytochemistry 23, no. 12 (November 26, 1985): 2811–15. http://dx.doi.org/10.1016/s0031-9422(00)80583-x.

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Cheng, Y. "Methionine-induced stabilization of Bowman–Birk protease inhibitor mRNA." Phytochemistry 52, no. 2 (September 1999): 225–31. http://dx.doi.org/10.1016/s0031-9422(99)00107-7.

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Larionova, Natalia I., Inna P. Gladysheva, and Dimitri P. Gladyshev. "Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor." FEBS Letters 404, no. 2-3 (March 10, 1997): 245–48. http://dx.doi.org/10.1016/s0014-5793(97)00089-6.

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Madden, Marian A., Anna L. Tan-Wilson, and Karl A. Wilson. "Proteolysis of soybean bowman-birk trypsin inhibitor during germination." Phytochemistry 24, no. 12 (November 1985): 2811–15. http://dx.doi.org/10.1016/0031-9422(85)80005-4.

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Armstrong, William B., X. Steven Wan, Ann R. Kennedy, Thomas H. Taylor, and Frank L. Meyskens. "Development of the Bowman-Birk inhibitor for oral cancer chemoprevention and analysis of neu immunohistochemical staining intensity with Bowman-Birk inhibitor concentrate treatment." Laryngoscope 113, no. 10 (September 3, 2010): 1687–702. http://dx.doi.org/10.1097/00005537-200310000-00007.

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Csáky, I., and S. Fekete. "Soybean: feed quality and safety. Part 1: Biologically active components. A review." Acta Veterinaria Hungarica 52, no. 3 (September 1, 2004): 299–313. http://dx.doi.org/10.1556/avet.52.2004.3.6.

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A large number of soybean components have diverse biological activities. These include hormonal, immunological, bacteriological and digestive effects. The presently known allergens are listed. The divergence between chemical evaluation and biological value is highlighted. The following components are discussed: Kunitz inhibitor, Bowman-Birk inhibitor, saponins, soyacystatin, phytoestrogens (daidzein, glycitein, genistein), Maillard products, soybean hydrophobic protein, soy allergens, lecithin allergens, raffinose, stachyose, 2-pentyl pyridine. The studies describing the effects of the isolated components are reviewed.

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Bueno, Norlene R., Hans Fritz, Ennes A. Auerswald, Reinhart Mentele, Misako Sampaio, Claudio A. M. Sampaio, and Maria Luiza V. Oliva. "Primary Structure of Dioclea glabra Trypsin Inhibitor, DgTI, a Bowman–Birk Inhibitor." Biochemical and Biophysical Research Communications 261, no. 3 (August 1999): 838–43. http://dx.doi.org/10.1006/bbrc.1999.1099.

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Gu, Chunmei, Xinxiu Song, Linlin Zhao, Shu Pan, and Guixin Qin. "Purification and Characterization of Bowman-Birk Trypsin Inhibitor from Soybean." Journal of Food and Nutrition Research 2, no. 9 (August 24, 2014): 546–50. http://dx.doi.org/10.12691/jfnr-2-9-3.

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Kennedy, A. R. "The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent." American Journal of Clinical Nutrition 68, no. 6 (December 1, 1998): 1406S—1412S. http://dx.doi.org/10.1093/ajcn/68.6.1406s.

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31

Oreffo, Victor I. C., Paul C. Billings, Ann R. Kennedy, and Hanspeter Witschi. "Acute effects of the Bowman-Birk protease inhibitor in mice." Toxicology 69, no. 2 (January 1991): 165–76. http://dx.doi.org/10.1016/0300-483x(91)90228-s.

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Wang, YuePing, XiongTing Chen, and LiJuan Qiu. "Novel alleles among soybean Bowman-Birk proteinase inhibitor gene families." Science in China Series C: Life Sciences 51, no. 8 (August 2008): 687–92. http://dx.doi.org/10.1007/s11427-008-0096-7.

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Larionova, Nathalia I., Stepan S. Vartanov, Nadezhda V. Sorokina, Inna P. Gladysheva, and Sergey D. Varfolomeyev. "Conjugation of the bowman-birk soybean proteinase inhibitor with hydroxyethylstarch." Applied Biochemistry and Biotechnology 62, no. 2-3 (March 1997): 175–82. http://dx.doi.org/10.1007/bf02787993.

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Muzard, Julien, Conor Fields, James John O’Mahony, and Gil U. Lee. "Probing the Soybean Bowman–Birk Inhibitor Using Recombinant Antibody Fragments." Journal of Agricultural and Food Chemistry 60, no. 24 (June 6, 2012): 6164–72. http://dx.doi.org/10.1021/jf3004724.

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35

Ye, X. Y., T. B. Ng, and P. F. Rao. "A Bowman–Birk-Type Trypsin-Chymotrypsin Inhibitor from Broad Beans." Biochemical and Biophysical Research Communications 289, no. 1 (November 2001): 91–96. http://dx.doi.org/10.1006/bbrc.2001.5965.

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36

McBride, Jeffrey D., Emma M. Watson, Arnd B. E. Brauer, Agn�s M. Jaulent, and Robin J. Leatherbarrow. "Peptide mimics of the Bowman-Birk inhibitor reactive site loop." Biopolymers 66, no. 2 (2002): 79–92. http://dx.doi.org/10.1002/bip.10228.

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37

Oliva, Maria Luiza V., and Misako U. Sampaio. "Action of plant proteinase inhibitors on enzymes of physiopathological importance." Anais da Academia Brasileira de Ciências 81, no. 3 (September 2009): 615–21. http://dx.doi.org/10.1590/s0001-37652009000300023.

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Obtained from leguminous seeds, various plant proteins inhibit animal proteinases, including human, and can be considered for the development of compounds with biological activity. Inhibitors from the Bowman-Birk and plant Kunitz-type family have been characterized by proteinase specificity, primary structure and reactive site. Our group mostly studies the genus Bauhinia, mainly the species bauhinioides, rufa, ungulata and variegata. In some species, more than one inhibitor was characterized, exhibiting different properties. Although proteins from this group share high structural similarity, they present differences in proteinase inhibition, explored in studies using diverse biological models.

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38

Krishna Murthy, H. M., K. Judge, L. DeLucas, S. Clum, and R. Padmanabhan. "Crystallization, characterization and measurement of MAD data on crystals of dengue virus NS3 serine protease complexed with mung-bean Bowman–Birk inhibitor." Acta Crystallographica Section D Biological Crystallography 55, no. 7 (July 1, 1999): 1370–72. http://dx.doi.org/10.1107/s0907444999007064.

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Crystallization and preliminary characterization of the essential dengue virus NS3 serine protease complexed with a Bowman–Birk-type inhibitor from mung beans are reported. As the structure proved resistant to solution by molecular replacement and multiple isomorphous replacement methods, multi-wavelength anomalous diffraction data at the L III edge of a holmium derivative have been measured. Promising Bijvoet and dispersive signals which are largely consistent with expected values have been extracted from the data. The structure, when determined, will provide a structural basis for the design, synthesis and evaluation of inhibitors of the protease for chemotherapy of dengue infections.

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39

Tornøe, Christian, Eva Johansson, and Per-Olof Wahlund. "Divergent Protein Synthesis of Bowman–Birk Protease Inhibitors, their Hydrodynamic Behavior and Co-crystallization with α-Chymotrypsin." Synlett 28, no. 15 (May 24, 2017): 1901–6. http://dx.doi.org/10.1055/s-0036-1588840.

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A divergent protein synthesis strategy was executed to effectively synthesize Bowman–Birk protease inhibitor (BBI) analogues using native chemical ligation of peptide hydrazides. Grafting selected residues from a potent trypsin inhibitor, sunflower trypsin inhibitor-1, onto the α-chymotrypsin-binding loop of BBI, resulted in a fourfold improvement of α-chymotrypsin inhibition. The crystal structure of a synthetic BBI analogue co-crystallized with α-chymotrypsin confirmed the correct protein fold and showed a similar overall structure to unmodified BBI in complex with α-chymotrypsin. Dynamic light scattering showed that C-terminal truncation of BBI led to increased self-association.

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40

Ekrami, Hossein, Ann R. Kennedy, Hanspeter Witschi, and Wei-Chiang Shen. "Cationized Bowman-Birk Protease Inhibitor as a Targeted Cancer Chemopreventive Agent." Journal of Drug Targeting 1, no. 1 (January 1993): 41–49. http://dx.doi.org/10.3109/10611869308998763.

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41

Miles, Steven M., Robin J. Leatherbarrow, Stephen P. Marsden, and William J. Coates. "Synthesis and bio-assay of RCM-derived Bowman–Birk inhibitor analogues." Org. Biomol. Chem. 2, no. 3 (2004): 281–83. http://dx.doi.org/10.1039/b312908j.

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42

Scarpi, D., J. D. McBride, and R. J. Leatherbarrow. "Inhibition of human β-tryptase by Bowman-Birk inhibitor derived peptides." Journal of Peptide Research 59, no. 2 (February 2002): 90–93. http://dx.doi.org/10.1046/j.1397-002x.2001.00001_950.x.

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43

Kimura, Makoto, Yoshiaki Kouzuma, Kei Abe, and Nobuyuki Yamasaki. "On a Bowman-Birk Family Proteinase Inhibitor from Erythrina variegata Seeds." Journal of Biochemistry 115, no. 3 (March 1994): 369–72. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a124345.

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44

Baek, J. M., and S. Kim II. "Nucleotide Sequence of a cDNA Encoding Soybean Bowman-Birk Proteinase Inhibitor." Plant Physiology 102, no. 2 (June 1, 1993): 687. http://dx.doi.org/10.1104/pp.102.2.687.

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45

Ma, Tong-Cui, Le Guo, Run-Hong Zhou, Xu Wang, Jin-Biao Liu, Jie-Liang Li, Yu Zhou, Wei Hou, and Wen-Zhe Ho. "Soybean-derived Bowman-Birk inhibitor (BBI) blocks HIV entry into macrophages." Virology 513 (January 2018): 91–97. http://dx.doi.org/10.1016/j.virol.2017.08.030.

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46

Losso, Jack N. "The Biochemical and Functional Food Properties of the Bowman-Birk Inhibitor." Critical Reviews in Food Science and Nutrition 48, no. 1 (January 2, 2008): 94–118. http://dx.doi.org/10.1080/10408390601177589.

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47

Dittmann, K., G. Wanner, C. Mayer, and H. P. Rodemann. "74 Selective radioprotection of normal tissue by Bowman-Birk proteinase inhibitor." Radiotherapy and Oncology 78 (March 2006): S25—S26. http://dx.doi.org/10.1016/s0167-8140(06)80568-2.

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48

Billings, Paul C., David L. Brandon, and Joan M. Habres. "Internalisation of the Bowman-Birk protease inhibitor by intestinal epithelial cells." European Journal of Cancer and Clinical Oncology 27, no. 7 (July 1991): 903–8. http://dx.doi.org/10.1016/0277-5379(91)90144-3.

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49

Song, Ganhong, Mei Zhou, Wei Chen, Tianbao Chen, Brian Walker, and Chris Shaw. "HV-BBI—A novel amphibian skin Bowman–Birk-like trypsin inhibitor." Biochemical and Biophysical Research Communications 372, no. 1 (July 2008): 191–96. http://dx.doi.org/10.1016/j.bbrc.2008.05.035.

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Li, Jieliang, Li Ye, Denise R. Cook, Xu Wang, Jinping Liu, Dennis L. Kolson, Yuri Persidsky, and Wen-Zhe Ho. "Soybean-derived Bowman-Birk inhibitor inhibits neurotoxicity of LPS-activated macrophages." Journal of Neuroinflammation 8, no. 1 (2011): 15. http://dx.doi.org/10.1186/1742-2094-8-15.

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Journal articles on the topic 'Bowman-Birk inhibitor'

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