Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 4 de 4
Filter
Add more filters










Database
Publication year range
1.
Curr Pharm Des ; 24(20): 2236-2240, 2018.
Article in English | MEDLINE | ID: mdl-30014797

ABSTRACT

Inflammation and the ways for its regulation: The development of an effective system for the treatment of inflammatory diseases requires comprehensive studies of the cellular signaling molecular networks comprising responses to various stressors, including pathogenic and non-pathogenic microorganisms. Significant attention on fundamental and applied research has recently focused on inducers of hemе oxygenase-1 (HO-1) and inhibitors of the expression of this enzyme, which regulates expression of this and other cytoprotective molecules and modulation of inflammation. Recent studies indicate that mycoplasmas (a major group of human pathogens of the Mollicutes) are capable of modulating inflammatory responses through the activation of the Nrf2 and the expression of HO-1. In vitro experiments demonstrate that the membrane lipoproteins (LAMPs), along with lipoprotein derivatives (lipopeptide MALP-2) in mycoplasmas cause a "cross-talk" between the pro- and antiinflammatory signaling pathways. Importantly, lipopeptide/lipoprotein - induced expression of HO-1 tends to suppress inflammation. Conclusion: The study of the molecular network that causes the corresponding outcome can facilitate the development of new approaches for the treatment of inflammatory processes. The derivatives of LAMPs and MALP-2 and of their analogues may prove promising for the treatment of diseases associated with chronic inflammation.


Subject(s)
Enzyme Induction/drug effects , Heme Oxygenase-1/metabolism , Mycoplasma/drug effects , Gene Expression Regulation, Enzymologic/drug effects , Heme Oxygenase-1/antagonists & inhibitors , Mycoplasma Infections/drug therapy
2.
Biofizika ; 52(1): 20-3, 2007.
Article in Russian | MEDLINE | ID: mdl-17348391

ABSTRACT

It has been shown that the use of a special growth medium enriched with amino acids and an inhibitor of aminotransferases alpha-aminooxyacetic acid makes possible the selectivity of labeling of barstar with 15N-leucine and 15N-tryptophan. The system of selective labeling, which was previously optimized with respect to the time of introducing the label relative to the time of introducing the inductor IPTG and the inhibitor of cell polymerase rifampicin, was substantially refined by the use of the transamination inhibitor. The inhibition of aminotransferases enables one to completely eliminate the redistribution of the isotope, which is a necessary step in NMR studies even if the strongly metabolizable 15N-leucine is used. The suppression of the redistribution of the isotope by alpha-aminooxyacetic acid is a successful approach to preparation of any selectively labeled proteins in the T7 polymerase system.


Subject(s)
Bacterial Proteins , Isotope Labeling , DNA-Directed RNA Polymerases , Escherichia coli , Leucine , Nitrogen Isotopes , Tryptophan , Viral Proteins
3.
Mikrobiologiia ; 74(1): 34-8, 2005.
Article in Russian | MEDLINE | ID: mdl-15835776

ABSTRACT

The investigation of the effect of some components of the medium on the distribution of the secretory guanyl-specific ribonuclease of Bacillus intermedius (EC 3.1.4.23) among various cell fractions and culture liquid showed that the amount of this enzyme in the culture liquid does not depend on the concentration of calcium ions in the medium (within 1-5 mM). The study of the effect of the amino acid substitutions Trp34Asn and Trp70Asn in the ribonuclease molecule showed that the secretion of ribonuclease depends on the formation rate of its secondary structure. The amino acid substitution Trp34Asn completely inhibits ribonuclease secretion.


Subject(s)
Bacillus/enzymology , Ribonucleases/metabolism , Bacillus/genetics , Culture Media , Enzyme Activation , Escherichia coli/enzymology , Escherichia coli/genetics , Mutation , Recombinant Proteins/metabolism , Ribonucleases/genetics
4.
Biochemistry (Mosc) ; 69(7): 806-8, 2004 Jul.
Article in English | MEDLINE | ID: mdl-15310282

ABSTRACT

Selective labeling of barstar by the stable (15)N isotope of the valine residue with high selectivity of the label incorporation resulting from the process of gene expression in Escherichia coli BL21(DE3) has been optimized. We have shown that alpha-aminooxyacetic acid (AOAA) significantly reduces the isotope redistribution, thus increasing the selectivity of (15)N incorporation into the synthesized protein, as detected by 2D-NMR. Quantitative measurements were used to determine the selectivity for the incorporation of isotope-labeled valine residue, which was 96% in the case using AOAA. Studies of the dynamics of barstar synthesis showed that no suppression of barstar yield is observed under the regulation of the T7 polymerase expression system by isopropylthio-beta-D-galactoside (IPTG) and rifampicin using AOAA.


Subject(s)
Bacterial Proteins/metabolism , DNA-Directed RNA Polymerases/metabolism , Valine/metabolism , Viral Proteins/metabolism , Aminooxyacetic Acid/chemistry , Aminooxyacetic Acid/metabolism , Bacterial Proteins/chemistry , Bacterial Proteins/pharmacology , Catalysis/drug effects , Escherichia coli/drug effects , Escherichia coli/genetics , Escherichia coli/metabolism , Isopropyl Thiogalactoside/pharmacology , Magnetic Resonance Spectroscopy , Nitrogen Isotopes , Rifampin/pharmacology , Transaminases/antagonists & inhibitors , Transaminases/metabolism , Valine/chemistry
SELECTION OF CITATIONS
SEARCH DETAIL
...