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V V Mosolov

Publications and source records attributed to V V Mosolov.

At least 19 recordsLinked to original sources
PubMed2006

Participation of proteolytic enzymes in the interaction of plants with phytopathogenic microorganisms.

Different forms of participation of proteolytic enzymes in pathogenesis and plant defense are reviewed. Together with extracellular proteinases, phytopathogenic microorganisms produce specific effectors with proteolytic activity and are able to act on proteins inside the plant cell. In turn, plants use both extracellular and intracellular proteinases for defense against phytopathogenic microorganisms. Among the latter, a special role belongs to vacuolar processing enzymes (legumains), which perform the function of caspases in the plant cell.

Bacteria↗
PubMed2004

Role of inhibitors of proteolytic enzymes in plant defense against phytopathogenic microorganisms.

This review analyzes the literature on various mechanisms of proteolytic enzyme inhibitors involved in plant defense against attack by phytopathogenic microorganisms. The action of proteinase inhibitors from plants upon the enzymes from pathogenic microorganisms and viruses is reviewed. Considerable attention is given to the induction of proteinase inhibitors in plants in response to the invasion of pathogens. Some aspects of application of proteinase inhibitors in biotechnology for production of transgenic plants with enhanced resistance to diseases are discussed.

Adaptation, Biological↗
PubMed2000

Primary structure of potato kunitz-type serine proteinase inhibitor.

The serine proteinase inhibitor (PSPI-21) isolated from potato tubers (Solanum tuberosum L.) comprises two protein species with pI 5.2 and 6.3, denoted as PSPI-21-5.2 and PSPI-21-6.3, respectively. They were separated by anion exchange chromatography on a Mono Q FPLC column. Both species tightly inhibit human leukocyte elastase, whereas their interaction with trypsin and chymotrypsin is substantially weaker. The sequences of both PSPI-21-5.2 and PSPI-21-6.3 were determined by analysis of overlapping peptides obtained from the oxidized or reduced and S-pyridylethylated proteins after digestion with trypsin or pepsin. Both species of PSPI-21 are composed of two chains, named chains A and B, which are linked by a disulfide bridge between Cys(146) and Cys(157). The other disulfide bridge is located within the A chains between Cys(48) and Cys(97). The amino acid sequences of the large A chains of the two forms, consisting of 150 amino acids residues each, differ in a single residue at position 52. The small chains B, containing 37 and 36 residues in PSPI-21-6.3 and PSPI-21-5.2, respectively, have nine different residues. The entire amino acid sequences of the two inhibitors show a high degree of homology to the other Kunitz-type proteinase inhibitors from plants.

Amino Acid Sequence↗
PubMed1999

Reactive sites of the 21-kD protein inhibitor of serine proteinases from potato tubers.

The effect of modifications of Met, Arg, and Lys residues on the inhibitory activity of a serine proteinase-inhibiting 21-kD protein from potato tubers has been studied. The data indicate that the 21-kD protein has two independent reactive sites for human leukocyte elastase (or chymotrypsin) and trypsin. It is concluded that the 21-kD inhibitor has Met and Arg residues in the P1 position of the reactive sites responsible for interactions with elastase (or chymotrypsin) and trypsin. It is shown that the 21-kD protein is capable of forming a triple complex binding simultaneously one molecule of trypsin and one molecule of chymotrypsin.

Chromatography, High Pressure Liquid↗
PubMed1999

Primary structure of a 21-kD protein from potato tubers.

A 21-kD protein isolated earlier from potato tubers (Solanum tuberosum L.) has two isoforms, with pI 6.3 and 5.2, which were separated by fast protein ion-exchange chromatography on a Mono Q column. The primary structures of the two forms consisted of 187 and 186 amino acid residues. Both isoforms are composed of two polypeptide chains, designated A and B, linked by a single disulfide bond between Cys-146 of the A chain and Cys-7 of the B chain. The amino acid sequences of the A chains of the two forms, consisting of 150 residues each, differ in a single amino acid residue at position 52 (Val --> Ile), while the B chains, containing 37 and 36 residues, respectively, have substitutions at nine positions (Leu-8 --> Ser-8, Lys-25--Asp-26 --> Asn-25--Glu-26, Ile-31--Ser-32 --> Val-31--Leu-32, Lys-34--Gln-35--Val-36--Gln-37 --> Gln-34--Glu-35--Val-36). Both isoforms form stable inhibiting complexes with human leukocyte elastase and are less effective against chymotrypsin and trypsin.

Amino Acid Sequence↗
PubMed1998

Kunitz-type proteinase inhibitors from intact and Phytophthora-infected potato tubers.

Three protein proteolytic enzyme inhibitors with molecular masses 21, 22, and 23 kDa have been isolated from intact potato tubers (Solanum tuberosum L. cv. Istrinskii). The 21 and 22 kDa proteins denoted as PSPI-21 and PSPI-22, respectively, are serine proteinase inhibitors with different specificity. The 23 kDa protein denoted as PCPI-23 is an inhibitor of plant cysteine proteinases. The PSPI-21 molecule consists of two disulfide-linked polypeptide chains with molecular masses of 16.5 kDa and 4.5 kDa. The PSPI-22 and PCPI-23 have one polypeptide chain. Their amino-termini numbered 21-25 amino acid residues have significant homology to other plant inhibitors which are members of the soybean Kunitz inhibitor family. It is found that at least PSPI-21 and PSPI-22 can predominantly accumulate in potato tubers infected with Phytophthora infestans zoospores.

Amino Acid Sequence↗
PubMed1998

[New studies on natural inhibitors of proteolytic enzymes].

New data on proteolytic enzyme inhibitors and mechanisms of their interaction with the enzymes are reviewed. In recent years, a number of new inhibitors comprising families earlier unknown have been described such as proteins from the parasitic nematode Ascaris lumbricoides, ecotin from the periplasm of Escherichia coli, proteins PMP-C and PMP-D from locust Locusta migratoria, and hirustasin from the medicinal leech Hirudo medicinalis. At the same time, some proteins that may be assigned to inhibitors on the basis of their structures were found to perform other (not inhibitory) functions. Thus, the family of the Kunitz soybean trypsin inhibitor includes plant storage proteins and proteins whose synthesis is induced by stress factors. Numerous inhibitors interacting with the enzymes by mechanisms other than the substrate-like ones were identified, such as ornithodorin and anticoagulant peptide from tick Ornithodoros moubata (inhibitors of the blood clotting system proteases), an inhibitor from snake (Bothrops jararaca) venom, and ecotin, an inhibitor of serine proteases with an unusually broad specificity range. Special emphasis is placed on enzyme inhibition with propeptides and the mechanism of this process.

Animals↗
PubMed1997

Potato tuber protein proteinase inhibitors belonging to the Kunitz soybean inhibitor family.

Three protein inhibitors of proteolytic enzymes with molecular weights 21, 22, and 23 kD were isolated from potato tubers (Solanum tuberosum L.) by ammonium sulfate precipitation followed by gel and ion-exchange chromatography. The 21- and 22-kD proteins were shown to be serine proteinase inhibitors with different specificities. The 21-kD protein inhibits human leucocyte elastase and trypsin effectively, but it is less effective towards chymotrypsin. The 22-kD protein is an inhibitor of cysteine proteinases and suppresses the activities of papain, ficin, and bromelain with the same affinities. None of the isolated proteins inhibit subtilisin, pepsin, or cathepsin D. The 21-kD protein consists of two disulfide-linked polypeptide chains with molecular weights of 16.5 +/- 1 kD and 4.5 +/- 1 kD. The 22-kD and 23-kD proteins have a single polypeptide chain. The N-terminal 22-25 amino acid sequences of these three proteins were determined. These sequences have significant homology to other plant inhibitors from the Kunitz soybean inhibitor superfamily.

Amino Acid Sequence↗
PubMed1996

A novel human leukocyte elastase inhibitor from duck egg white.

A serine proteinase inhibitor (ovomucoid) has been isolated from duck egg white. The duck ovomucoid effectively inhibited HLE, PPE, chymotrypsin, and HCG in a 1:1 molar ratio, and trypsin in a 1:2 molar ratio. Inhibition of human plasmin and porcine pancreatic kallikrein was not observed. The ovomucoid shows equilibrium dissociation constants of 0.002; 2.4; 2.2; 6.1; and 18.0 nM for HLE, PPE, chymotrypsin, trypsin, and HCG, respectively. The molecule of inhibitor can simultaneously bind two trypsin molecules and one molecule of elastase (or chymotrypsin).

Animals↗
PubMed1995

[Cysteine proteinase inhibitors from soy seeds].

Protein inhibitors of cysteine proteinases possessing unusual properties have been found in soya (Glycine max) seeds. One of the inhibitor forms has also been detected in Bowman-Birk inhibitor preparations (both commercial and purified by affinity chromatography on chymotrypsin-Sepharose ones). A peculiarity of the inhibitors is that they irreversibly lose their activity in the presence of reducing agents; therefore their effects are normally unobserved under standard conditions of cysteine proteinase inhibitor assays. Soybean inhibitors are represented by two forms with pI of 5.9 and 3.2. The molecular mass of the inhibitor whose pI is equal to 5.8 is about 14 kDa. Both inhibitors suppress the activity of papain, ficin and bromelain.

Bromelains↗
PubMed1995

[Isolation and characteristics of a new trypsin and chymotrypsin inhibitor from potato tubers].

A novel trypsin and chymotrypsin inhibitor has been isolated from potato (Solanum tuberosum L.) tubers. The isolation procedure included ammonium sulfate precipitation, gel-chromatography on Sephadex G-75 and ion-exchange chromatography on DEAE-cellulose. The inhibitor interacts with trypsin and chymotrypsin at a molar ratio of 1:1. The substrate-dependent dissociation of the enzyme-inhibitor complexes is observed. The inhibitor displays no activity towards subtilisin and pancreatic elastase. The ability of the inhibitor to form a ternary complex containing simultaneously both trypsin and chymotrypsin molecules testifies to the presence of two independent reactive sites for these enzymes.

Amino Acid Sequence↗
PubMed1994

[Proteolytic enzyme inhibitors of protein nature].

New data on the mechanism of interaction between proteolytic enzymes and protein inhibitors are presented. Most of known serine proteinase inhibitors bind to proteolytic enzymes through a substrate-like mechanism. A different mechanism is observed in the case of the inhibition of thrombin by hirudin and of papain by cystatin (from egg white) and stephin B. Protopeptides released during activation of some proteinase zymogens may act as efficient enzyme inhibitors. Such zymogens can be considered as covalently bound enzyme-inhibitor complexes.

Amino Acid Sequence↗
PubMed1993

Enzymatic oxidation of the bifunctional wheat inhibitor of subtilisin and endogenous alpha-amylase.

Oxidation of the bifunctional wheat inhibitor of subtilisin and endogenous alpha-amylase catalyzed by horseradish peroxidase results in the loss of the inhibitory activity against both enzymes. The enzymatic oxidation is accompanied by modification of one methionine and two tryptophan residues in the protein. The results obtained, together with data on chemical modification and limited proteolysis, allow us to conclude that Met34-Ala35 is the reactive site of the inhibitor responsible for the interaction with subtilisin. It is supposed that the reactive site of the inhibitor responsible for the interaction with alpha-amylase contains one or two tryptophan residues.

Chromatography, Affinity↗
PubMed1992

Protein proteinase inhibitor therapy in experimental pancreatitis: pharmacological characterization of the inhibitor.

The pharmacodynamical properties of the duck ovomucoid and its effect on the development of experimental pancreatitis in rats have been studied. It has been shown that after intravenous injection the ovomucoid initially accumulated in the liver, kidneys and blood, while after intraperitoneal injection--mainly in the pancreas and kidneys. The inhibitor is removed from circulation by renal filtration, one-half of the injected protein being removed for 4 hr. For the treatment of experimental pancreatitis two modes of ovomucoid administration were used: intravenous and combined (intravenous/intraperitoneal). The ovomucoid intravenous injection in a dose of 16,300 ATU/kg/24 hr resulted in decrease of both the trypsin-like activity and the level of the trypsinogen activation peptide in the blood to the level in intact rats and also in reduction of the primary pancreas destruction. The same effect observed in the case of the ovomucoid combined injection, but with a lower intravenous dose.

Animals↗
PubMed1987

[Interaction of sheep haptoglobin with trypsin inhibitors].

It was found that polymeric sheep haptoglobin C interacts with duck egg ovomucoid and with maize trypsin inhibitor. These inhibitors do not block the region in haptoglobin C molecule which is responsible for the formation of its complex with hemoglobin. The binding of the natural protein inhibitors is suggestive of homology of the haptoglobin site involved in the interaction with the substrate-specific site of trypsin. It is assumed that the regions in these protein molecules adjacent to the active and specific sites also possess a high degree of homology.

Animals↗
PubMed1983

Hirudin from leech heads and whole leeches and "pseudo-hirudin" from leech bodies.

Hirudin from whole leeches behaves like hirudin from leech heads and "pseudohirudin" from leech bodies during isolation and purification by means of acetone and ethanol fractionation, affinity chromatography on trypsin-Sepharose, and isoelectric focusing. However, the antithrombin activity of the hirudin fractions obtained after isoelectric focusing was approximately three times lower than that of the corresponding hirudin fractions from the heads. The "pseudohirudin" fractions had practically no antithrombin activity. In hirudin from whole leeches isoleucine and valine were identified as the N-terminal amino acid. Isoleucine was identified as the dominant amino acid in hirudin from leech heads. The dominant N-terminal amino acid in "pseudohirudin" from leech bodies was valine. The data on antithrombin activity and N-terminal amino acids indicate that hirudin from whole leeches contains admixtures of inactive "pseudohirudin". In contrast to hirudin from leech heads, "pseudohirudin" represents associates of di- and three-isomers. The molecular weight of the "pseudohirudin" molecule is 2000 lower than the molecular weight of hirudin, which corresponds to a difference of 20 amino acid residues, calculated from the total number of amino acid residues in the preparations.

Amino Acid Sequence↗
PubMed1983

[Isolation of a specific inhibitor of microbial serine proteinase from kidney bean seeds].

A protein acting as a specific inhibitor of microbial serine proteinases was isolated from kidney bean seeds. The purification procedure included complex formation between the inhibitor and Aspergillus oryzae proteinase. The protein with a Mr approximately 10 000 inhibits subtilisin and Asp. oryzae proteinase but does not affect trypsin and chymotrypsin. The inhibitor molecule contains no half-cystine residues.

Aspergillus↗