Biospecific haemosorbents based on proteinase inhibitor

Platè, N.A.; Валуев, Л. И.; Valueva, T. A.; Chupov, V. V.

doi:10.1016/0142-9612(93)90075-d

Cited by 29 publications

(10 citation statements)

References 9 publications

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“…The mode of action of cysteine-rich peptides typically involves the disruption of the pathogen's membrane via both specific and nonspecific electrostatic and hydrophobic interactions with cell surface groups, ribosomal inactivation, and related forms of protein inhibition (Chen et al 2002;Shai 2002;Thevissen et al 2003;Vivanco et al 1999). High levels of protease inhibitors are often found in many plants belonging to the Solanaceae family (Plate et al 1993). Plant protease inhibitors can suppress enzyme activities triggered in response to attack by proteases produced by phytopathogenic microorganisms (Valueva et al 2003).…”

Section: Discussionmentioning

confidence: 98%

The new CaSn gene belonging to the snakin family induces resistance against root-knot nematode infection in pepper

et al. 2011

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The new CaSn gene belonging to the snakin family in pepper (Capsicum annuum) encodes a novel antimicrobial peptide and responds to rootknot nematode (Meloidogyne spp.) infection. CaSn was isolated and cloned using suppression subtractive hybridization (SSH), and the gene was characterized and expressed in Escherichia coli. The CaSnakin protein encoded by CaSn is an antimicrobial peptide consisting of a signal peptide of 23 amino acid residues, an acidic peptide of 14 amino acid residues (pI=4.18), and a mature protein of 66 amino acid residues that corresponds to a molecular mass of 7.03 kDa. The peptide sequence has 12 conserved cysteines forming six disulfide bridges. CaSnakin is highly homologous to the peptide snakin-2 (StSN2) of potato (Solanum tuberosum); CaSnakin also shows 88.5% identity to StSN2. Phylogenetic tree analysis indicated that the CaSn gene belongs to subfamily II of the snakin family. Real-time quantitative reverse transcriptase polymerase chain reaction (RT-qPCR) results showed that the CaSn gene was induced and expressed evidently by root-knot nematode infection; CaSn is also expressed in buds, stems, roots and leaves. The CaSnakin protein expressed in E. coli showed strong antimicrobial activity against freeliving nematodes (Caenorhabditis elegans) and rootknot nematodes in vitro. In addition, the virusinduced gene silencing (VIGS) results revealed that the CaSn gene participates in the defense of plants against nematodes. In conclusion, the CaSn gene can be activated by nematode infections, and it plays an important role in host defense. As far as we know, this is the first investigation reporting the role of a snakin gene in the defense of plants against nematodes. In addition, the CaSn gene is the first gene of the snakin family isolated from pepper.

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Section: Discussionmentioning

confidence: 98%

The new CaSn gene belonging to the snakin family induces resistance against root-knot nematode infection in pepper

et al. 2011

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“…Although protease inhibitors are found in plants belonging to different kinds of systematic groups, high levels of protease inhibitors are often reported in many plants belonging to the Solanaceae family (Plate et al, 1993). The effect of a protease inhibitor extracted from potatoes (POT II) which increase CCK release, on food intake was examined in 11 lean subjects by Hill et al (1990).…”

Section: Roles Of Plant Protease Inhibitors In Health and Disease Conmentioning

confidence: 99%

Plant Protease Inhibitors in Therapeutics-Focus on Cancer Therapy

2016

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Plants are known to have many secondary metabolites and phytochemical compounds which are highly explored at biochemical and molecular genetics level and exploited enormously in the human health care sector. However, there are other less explored small molecular weight proteins, which inhibit proteases/proteinases. Plants are good sources of protease inhibitors (PIs) which protect them against diseases, insects, pests, and herbivores. In the past, proteinaceous PIs were considered primarily as protein-degrading enzymes. Nevertheless, this view has significantly changed and PIs are now treated as very important signaling molecules in many biological activities such as inflammation, apoptosis, blood clotting and hormone processing. In recent years, PIs have been examined extensively as therapeutic agents, primarily to deal with various human cancers. Interestingly, many plant-based PIs are also found to be effective against cardiovascular diseases, osteoporosis, inflammatory diseases and neurological disorders. Several plant PIs are under further evaluation in in vitro clinical trials. Among all types of PIs, Bowman-Birk inhibitors (BBI) have been studied extensively in the treatment of many diseases, especially in the field of cancer prevention. So far, crops such as beans, potatoes, barley, squash, millet, wheat, buckwheat, groundnut, chickpea, pigeonpea, corn, and pineapple have been identified as good sources of PIs. The PI content of such foods has a significant influence on human health disorders, particularly in the regions where people mostly depend on these kind of foods. These natural PIs vary in concentration, protease specificity, heat stability, and sometimes several PIs may be present in the same species or tissue. However, it is important to carry out individual studies to identify the potential effects of each PI on human health. PIs in plants make them incredible sources to determine novel PIs with specific pharmacological and therapeutic effects due to their peculiarity and superabundance.

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“…Protease inhibitors are ubiquitously plentiful in tubers and plant seeds [17]. Proteinase inhibitors are found in plants belonging to a variety of systematic groups, although high levels of proteinase inhibitors are often found in many plants belonging to the Solanaceae family [18]. Protease inhibitors in plants are usually considered to work as storage proteins (nitrogen source) and as a defense mechanism [19].…”

Section: Introductionmentioning

confidence: 99%

Protease Inhibitors from Plants with Antimicrobial Activity

Kim

Park

Hwang

et al. 2009

IJMS

201

137

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Antimicrobial proteins (peptides) are known to play important roles in the innate host defense mechanisms of most living organisms, including plants, insects, amphibians and mammals. They are also known to possess potent antibiotic activity against bacteria, fungi, and even certain viruses. Recently, the rapid emergence of microbial pathogens that are resistant to currently available antibiotics has triggered considerable interest in the isolation and investigation of the mode of action of antimicrobial proteins (peptides). Plants produce a variety of proteins (peptides) that are involved in the defense against pathogens and invading organisms, including ribosome-inactivating proteins, lectins, protease inhibitors and antifungal peptides (proteins). Specially, the protease inhibitors can inhibit aspartic, serine and cysteine proteinases. Increased levels of trypsin and chymotrypsin inhibitors correlated with the plants resistance to the pathogen. Usually, the purification of antimicrobial proteins (peptides) with protease inhibitor activity was accomplished by salt-extraction, ultrafiltration and C18 reverse phase chromatography, successfully. We discuss the relation between antimicrobial and anti-protease activity in this review. Protease inhibitors from plants potently inhibited the growth of a variety of pathogenic bacterial and fungal strains and are therefore excellent candidates for use as the lead compounds for the development of novel antimicrobial agents.

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Biospecific haemosorbents based on proteinase inhibitor

Cited by 29 publications

References 9 publications

The new CaSn gene belonging to the snakin family induces resistance against root-knot nematode infection in pepper

The new CaSn gene belonging to the snakin family induces resistance against root-knot nematode infection in pepper

Plant Protease Inhibitors in Therapeutics-Focus on Cancer Therapy

Protease Inhibitors from Plants with Antimicrobial Activity

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