Bowman‐Birk inhibitor modifies transcription of autophagy and apoptosis genes in an in vitro model of Alzheimer's disorder

Akbari, Samaneh; Akrami, Hassan; Mostafaei, Ali; Kiani, S

doi:10.1002/jcb.28391

Cited by 5 publications

(4 citation statements)

References 34 publications

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“…It has been suggested that soybean BBI could be effective in the inhibition of Alzheimer's disease. Akbari et al [205] studied the effect of BBI on in vitro model of Alzheimer's disorder in which accumulation of amyloid β (Aβ) in PC12 cells was stimulated with HgCl 2 . It was shown that BBI inhibited the accumulation of Aβ by inducing autophagy and decreased apoptosis, which is regarded as a key event in neurodegenerative diseases.…”

Section: Alzheimer's Diseasementioning

confidence: 99%

Bowman-Birk Inhibitors: Insights into Family of Multifunctional Proteins and Peptides with Potential Therapeutical Applications

2020

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Bowman-Birk inhibitors (BBIs) are found primarily in seeds of legumes and in cereal grains. These canonical inhibitors share a highly conserved nine-amino acids binding loop motif CTP1SXPPXC (where P1 is the inhibitory active site, while X stands for various amino acids). They are natural controllers of plants’ endogenous proteases, but they are also inhibitors of exogenous proteases present in microbials and insects. They are considered as plants’ protective agents, as their elevated levels are observed during injury, presence of pathogens, or abiotic stress, i.a. Similar properties are observed for peptides isolated from amphibians’ skin containing 11-amino acids disulfide-bridged loop CWTP1SXPPXPC. They are classified as Bowman-Birk like trypsin inhibitors (BBLTIs). These inhibitors are resistant to proteolysis and not toxic, and they are reported to be beneficial in the treatment of various pathological states. In this review, we summarize up-to-date research results regarding BBIs’ and BBLTIs’ inhibitory activity, immunomodulatory and anti-inflammatory activity, antimicrobial and insecticidal strength, as well as chemopreventive properties.

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Section: Alzheimer's Diseasementioning

confidence: 99%

Bowman-Birk Inhibitors: Insights into Family of Multifunctional Proteins and Peptides with Potential Therapeutical Applications

2020

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“…BBIC has been reported to prevent the initiation of tumors and cause cell death in in vivo and invitro cancer models (Kennedy, 1998;Kennedy and Wan, 2002). Besides its chemo-preventive and anti-inflammatory properties (Clemente et al,2011), BBI has been recently reported to be effective in the treatment of Alzheimer's disease (Akbari et al, 2019) and inhibition of HIV replication in macrophages (Ma et al, 2016). Further, in the backdrop of the fact that SARS-CoV-2, the causative agent of COVID-19 pandemic, requires the expression of self-encoded chymotrypsin-like protease for its replication in the host cell (Cascella et al, 2020), BBI in soybean may show an inhibitory effect on the multiplication of this novel virus in human cell due to its chymotrypsin inhibiting property.…”

Section: Academicpresmentioning

confidence: 99%

Bowman-Birk inhibitor in soybean: Genetic variability in relation to total trypsin inhibitor activity and elimination of Kunitz trypsin inhibitor

et al. 2021

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DOI: 10.15835/nsb13110836 Bowman-Birk inhibitor (BBI) is a soybean seed serine protease inhibitor whose nutraceutical properties far exceed its anti-nutritional property arising from its trypsin and chymotrypsin inhibitor activity. High BBI soybean genotypes are sought for the commercial preparation of this nutraceutical biomolecule while low BBI content in Kunitz trypsin inhibitor (KTI)-free genetic background is desirable in soymeal manufacturing. In the present investigation, monoclonal antibody assay of 95 soybean genotypes revealed 11-fold genetic variation for BBI concentration. The study led to the identification of 3 very high (>20 mg/g defatted soy flour) and 5 very low BBI (< 4 mg/g defatted soy flour) soybean genotypes. Contribution of BBI to total trypsin inhibition activity ranged from 2.2 to 53.5% with average value of 11.6%. Genotypes with varying level of BBI raised consecutively for two years exhibited non-significant (p>0.05) effect of growing year on the trait. BBI content in BC3F2 derived KTI-free lines was at par with the recurrent parent. Low and high BBI content genotypes with diverse genetic background identified in the study may be exploited to develop mapping population to identify genomic regions underlying BBI in soybean.

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“…9,10 BBIs have been studied extensively due to their therapeutic potential, against certain types of cancer, 11 Alzheimer's disease, 12 autoimmune disease, fungal infections, and inflammatory disorders. 13,14 As the pathogenesis of pancreatitis is associated with the hydrolyzing enzymes, therefore, the BBIs may play their role in the management of pancreatitis by inhibiting such enzymes. Both KTIs and BBIs are present in a wide variety of plants, however, Bowman-Birk-type protease inhibitors have been mostly reported from the legume family of plants.…”

Section: Introductionmentioning

confidence: 99%

“…Whereas, the Bowman–Birk‐type of protease inhibitors are relatively large proteins as compared to Kunitz type‐inhibitors, with several disulfide bonds 9,10 . BBIs have been studied extensively due to their therapeutic potential, against certain types of cancer, 11 Alzheimer's disease, 12 autoimmune disease, fungal infections, and inflammatory disorders 13,14 . As the pathogenesis of pancreatitis is associated with the hydrolyzing enzymes, therefore, the BBIs may play their role in the management of pancreatitis by inhibiting such enzymes.…”

Section: Introductionmentioning

confidence: 99%

Insight into the structural basis of the dual inhibitory mode of Lima bean (Phaseolus lunatus) serine protease inhibitor

2022

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Bovine pancreatic trypsin was crystallized, in-complex with Lima bean trypsin inhibitor (LBTI) (Phaseolus lunatus L.), in the form of a ternary complex. LBTI is a Bowman-Birk-type bifunctional serine protease inhibitor, which has two independent inhibitory loops. Both of the loops can inhibit trypsin, however, only the hydrophobic loop is specific for inhibiting chymotrypsin. The structure of trypsin incomplex with the LBTI has been solved and refined at 2.25 Å resolution, in the space group P4 1, withfree values of 18.1/23.3. The two binding sites of LBTI differ in only two amino acids. Lysine and leucine are the key residues of the two different binding loops positioned at the P1, and involved in binding the S1 binding site of trypsin. The asymmetric unit cell contains two molecules of trypsin and one molecule of LBTI.The key interactions include hydrogen bonds between LBTI and active site residues of trypsin. The 3D structure of the enzyme-inhibitor complex provided details insight into the trypsin inhibition by LBTI. To the best of our knowledge, this is the first report on the structure of trypsin incomplex with LBTI.

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Bowman‐Birk inhibitor modifies transcription of autophagy and apoptosis genes in an in vitro model of Alzheimer's disorder

Cited by 5 publications

References 34 publications

Bowman-Birk Inhibitors: Insights into Family of Multifunctional Proteins and Peptides with Potential Therapeutical Applications

Bowman-Birk Inhibitors: Insights into Family of Multifunctional Proteins and Peptides with Potential Therapeutical Applications

Bowman-Birk inhibitor in soybean: Genetic variability in relation to total trypsin inhibitor activity and elimination of Kunitz trypsin inhibitor

Insight into the structural basis of the dual inhibitory mode of Lima bean (Phaseolus lunatus) serine protease inhibitor

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