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Biomedical subjects

N I Solov'eva

Publications and source records attributed to N I Solov'eva.

At least 19 recordsLinked to original sources
PubMed1998

[Matrix metalloproteinases and their biological functions].

Matrix metalloproteases (MMPs) play a key role in the metabolism of connective tissue proteins in the norm and in pathology. Major MMP subfamilies (collagenases, gelatinases, and stromelysins) and matrixins, which have not been attributed to any subfamily, are reviewed. The main characteristics of these enzymes; their structural properties; their specificity; the regulation of their activity; and their role in the normal development of the matrix, the oncogenic transformation of the cell, and angiogenesis are discussed.

Animals↗
PubMed1997

[The treatment of periodontal diseases using Diplen-Denta films with chlorhexidine (a clinico-laboratory study)].

Diplen-Denta biopolymer adhesive film with chlorohexidine-was used in the treatment of periodontal inflammations of different severity. The efficacy of treatment of gingivitis and periodontitis is assessed from changes in the clinical parameters and in the activity of neutrophil elastase in the gingival liquid. The new treatment is highly effective in patients with catarrhal gingivitis and generalized periodontitis of light and medium severity.

Adolescent↗
PubMed1995

[Proteolytic enzymes and their biological function].

The paper reviews studies made by the Laboratory of Biochemistry and Chemical Pathology of Proteins, Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, into the properties, structure, active center, biological functions, activity regulation. It accesses them in forming current concepts of the regulatory role of proteolytic enzymes. Their proteolytic features as a regulatory mechanism and various aspects of the regulatory role of proteinases are considered in the paper.

Animals↗
PubMed1994

[Basic metalloproteinases of the connective tissue matrix].

Metalloproteinases play a key role in the destruction of connective tissue matrix both upon normal physiological processes associated with remodelling of connective tissue and in various pathological situations. Variability of the matrix metalloproteinases, their specificity, structural features, activity regulation in vitro and in vivo, as well as their role in processes of oncogenic transformation are reviewed.

Amino Acid Sequence↗
PubMed1994

[Interaction of collagenases with certain peptide substrates and inhibitors].

Interactions of collagenases I and II (clostridiopeptidases) from Clostridium histolyticum with hexapeptide substrates in which some L-proline residues are replaced by their D-analogues, as well as with the tripeptide chloromethyl ketone Z-Gly-Pro-Gly-CH2Cl were studied. A role of stereochemistry of the amino acid residues in the substrate was established and differences between the collagenases, with regard to their specific requirements to substrates, were revealed. The tripeptide chloromethyl ketone is shown to be a specific collagenase inhibitor modifying at the substrate-binding site in the active centre of these enzymes, most likely lysine residues.

Amino Acid Chloromethyl Ketones↗
PubMed1991

[Proteinases as a pathogenetic factor in inflammatory processes in periodontal tissues].

Collagenolytic activity (CA) in cervical fluid of patients with inflammation of periodontium was increased with increasing activity of the pathological process. Enhanced CA in patients with severe forms of periodontitis is probably due to depletion of endogenous inhibitors and to the transition of the latent collagenase to its active form. Studies of the effect of EDTA, PMSF and PCMB on CA show that proteinases are an essential factor in inflammation of periodontium.

Adolescent↗
PubMed1991

[The total proteolytic and collagenolytic activity in the blood cells of patients with systemic scleroderma].

Collagenolytic (CA) and neutral caseinolytic activity (NCA) was studied in extracts from blood cells (neutrophils, mononuclear cells and platelets) of patients suffering from systemic scleroderma (SSD). 23 persons were examined. Of these, 15 had local skin lesions, 8 diffuse lesions. CA, both specific and per 10(6) cells was found to be dramatically decreased (2-4-fold) in all blood cells, whereas NCA was increased in neutrophils and mononuclear cells; in platelets, it remained within normal. The amount of protein in neutrophils and mononuclear cells was lowered 1.2 and 2-fold respectively. In diffuse skin lesions, the amount of protein in cells was lower than in local lesions. It should be noted that in SSD patients examined, the inflammatory process was unmarked. Therefore, the data on substantial changes in proteolytic activity cannot be related to the inflammatory process. A reverse correlation was established between CA in neutrophils and circulating immune complexes as was a reverse correlation between CA in mononuclear cells and blood antinuclear factor. The data presented indicate that proteinases are an important factor of the pathogenesis in SSD. Apparently, SSD is characterized not only by enhanced synthesis of collagen but also by a dramatic reduction of the activity of enzymes that specifically hydrolyze this group of proteins, which leads to a decrease of collagen catabolism and hence, to the development of fibrosis in tissues.

Adult↗
PubMed1989

[Study on the effect of some group-specific agents on clostridiopeptidase].

The interaction of clostridiopeptidase of Clostridium histolyticum with EDC, TNM and MA, the specific reagents for COOH-groups, tyrosine and lysine residues was studied. It was shown that at pH 6.0 EDC inactivates the enzyme. The inactivation process follows the pseudo-first order kinetics and is described by a second order rate constant equal to 1 M-1 min-1. The synthetic substrate does not prevent, in practical terms, the enzyme inactivation by EDC. At pH 8.0 TNM modifies about 19 tyrosine residues in the clostridiopeptidase molecule which is accompanied by marked inhibition of the enzyme activity (down to 70-90%). In this case, the inactivation process is not described by simple pseudo-first order kinetics but is characterized by two steps (fast and slow) with second order rate constants of approximately 14 and 3.5 M-1 min-1, respectively. The synthetic substrate partly prevents the inactivation of the enzyme by TNM and protects 11 tyrosine residues. The MA-induced incorporation of 13 +/- 3 maleyl groups into the clostridiopeptidase molecule in partially prevented by the synthetic substrate with protects the enzyme against inactivation. The data obtained suggest that lysine residues are seemingly included into the active center of clostridiopeptidase, whereas tyrosine residues provide for the maintenance of active conformation of the enzyme.

Collagen↗
PubMed1988

[Metabolism of glycoproteins and fibronectin in skin fibroblasts of patients with rheumatoid arthritis].

The distribution in the cellular monolayer of the de novo synthetized pre-labeled glycoproteins and fibronectin upon culturing of fibroblasts in the medium with low serum content was analyzed. It was found that in rheumatoid arthritis (RA) the amount of total glycoproteins on the surface and within fibroblasts is higher and in the extracellular matrix is lower than in skin fibroblasts of healthy donors (HD). However, the amount of pre-labeled fibronectin on the surface of skin fibroblasts from patients with RA was considerably lower than in those from HD This finding as well as a rapid decrease in the amount of pre-labeled fibronectin in the extracellular matrix of RA fibroblasts is indicative of a more rapid metabolism of this protein in RA. In the skin fibroblasts from HD there was a practically uniform decrease in the amount of pre-labeled fibronectin in the cellular monolayer. The presence of caseinolytic activity in the culture medium even upon the first day of cell culturing in the serum-free medium, as well as the effect of various proteinase inhibitors on glycoprotein content in the cellular monolayer provide evidence that the rate of glycoprotein and fibronectin metabolism, especially in connective tissue cells of patients with RA, might possibly be determined not only by the level of their synthesis but also by the level of proteolytic activity in the connective tissue cells.

Arthritis, Rheumatoid↗