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1.
Lik Sprava ; (8): 108-16, 2013 Dec.
Article in Russian | MEDLINE | ID: mdl-25726686

ABSTRACT

Is established that at intestinal dysbacteriosis in the organism of experimental animals develop reactions of inflammatory type (early and late), leading to an accumulation in the blood serum of humoral immunity factors, blocking reactions mediated by lymphocytes ormacrophages, while maintaining their cytotoxic activity. Introduction of animals of tne probiotic endosporin promotes restoration of quantitative and qualitative indicators of intestinal microbiocenosis and the normalization of the immune system.


Subject(s)
Bacillus , Colon/drug effects , Dysbiosis/drug therapy , Immunity, Humoral/drug effects , Probiotics/therapeutic use , Animals , Colon/immunology , Colon/metabolism , Cytotoxicity Tests, Immunologic , Disease Models, Animal , Dysbiosis/immunology , Dysbiosis/microbiology , Lymphocytes/drug effects , Lymphocytes/immunology , Macrophage Activation/drug effects , Macrophage Activation/immunology , Macrophages/drug effects , Macrophages/immunology , Mice, Inbred BALB C , Microbial Consortia/drug effects , Probiotics/administration & dosage , Treatment Outcome
2.
Vestn Khir Im I I Grek ; 162(6): 16-9, 2003.
Article in Russian | MEDLINE | ID: mdl-14997807

ABSTRACT

Sixty five patients with peritonitis were examined and divided into two groups. The operative intervention in all the patients included transnasal intubation of the small intestine. The basic enteral therapy used in the first group of patients was made with the glucose-saline solution and transition to a balanced polysubstrate mixture "nutrient standard" with the increasing concentration. For the patients of the second group a special program was developed for enteral therapy in which glutamine and pectine were included in the glucose-saline solution as well as nutrient mixtures containing middle chain triglycerides. Active decompression of the small intestine followed by the enteral administration of the nutrient mixtures facilitated quicker correction of the intestinal insufficiency in patients with severe forms of peritonitis.


Subject(s)
Digestive System Surgical Procedures/methods , Gastrointestinal Diseases , Gastrointestinal Motility/physiology , Peritonitis/complications , Peritonitis/surgery , Adult , Female , Gastrointestinal Diseases/etiology , Gastrointestinal Diseases/physiopathology , Gastrointestinal Diseases/therapy , Humans , Male , Middle Aged , Syndrome
3.
Cell Mol Life Sci ; 58(10): 1386-98, 2001 Sep.
Article in English | MEDLINE | ID: mdl-11693521

ABSTRACT

Hydroxyproline-rich glycoproteins (HRGPs) are ubiquitous architectural components of the growing plant cell wall, accounting for as much as 10-20% of the dry weight. HRGPs are implicated in all aspects of plant growth and development, including responses to stress. The HRGP superfamily contains three major groups which represent a continuum of peptide periodicity and hydroxyproline-O-glycosylation. These groups range from the highly periodic and lightly arabinosylated repetitive proline-rich proteins (PRPs), through the cross-linked extensins which are periodic and highly arabinosylated, to the arabinogalactan-proteins (AGPs) which are the most highly glycosylated and least periodic. The repetitive units are small, often only four- to six-residue-glycosylated modules viewed hypothetically as functional motifs, or glycomodules. The Hyp contiguity hypothesis predicts that Hyp arabinosylation increases with Hyp contiguity and that clustered noncontiguous Hyp residues are sites of arabinogalactan polysaccharide addition in the AGPs and gums. Recent results involving glycosylation site mapping of endogenous HRGPs and HRGP design using synthetic genes have corroborated the hypothesis. The uses of synthetic genes in HRGP glycosylation site mapping and structural/functional analysis are also discussed.


Subject(s)
Cell Wall/chemistry , Galactans/chemistry , Galactans/genetics , Glycoproteins/chemistry , Glycoproteins/genetics , Amino Acid Sequence , Base Sequence , Binding Sites , Chromatography, Gel , Glycosylation , Microscopy, Fluorescence , Models, Chemical , Molecular Sequence Data , Plant Proteins/chemistry , Plasmids/metabolism , Protein Conformation , Sequence Homology, Amino Acid , Time Factors
4.
J Biol Chem ; 276(14): 11272-8, 2001 Apr 06.
Article in English | MEDLINE | ID: mdl-11154705

ABSTRACT

Hydroxyproline (Hyp) O-glycosylation characterizes the hydroxyproline-rich glycoprotein (HRGP) superfamily of the plant extracellular matrix. Hyp glycosylation occurs in two modes: Arabinosylation adds short oligoarabinosides (Hyp-arabinosides) while galactosylation leads to the addition of larger arabinogalactan polysaccharides (Hyp-polysaccharides). We hypothesize that sequence-dependent glycosylation of small peptide motifs results in glycomodules. These small functional units in combination with other repetitive peptide modules define the properties of HRGPs. The Hyp contiguity hypothesis predicts arabinosylation of contiguous Hyp residues and galactosylation of clustered noncontiguous Hyp residues. To determine the minimum level of Hyp contiguity that directs arabinosylation, we designed a series of synthetic genes encoding repetitive (Ser-Pro(2))(n), (Ser-Pro(3))(n), and (Ser-Pro(4))(n). A signal sequence targeted these endogenous substrates to the endoplasmic reticulum/Golgi for post-translational proline hydroxylation and glycosylation in transformed Nicotiana tabacum cells. The fusion glycoproteins also contained green fluorescence protein, facilitating their detection and isolation. The (Ser-Pro(2))(n) and (Ser-Hyp(4))(n) fusion glycoproteins yielded Hyp-arabinosides but no Hyp-polysaccharide. The motif (Ser-Pro(3))(n) was incompletely hydroxylated, yielding mixed contiguous/noncontiguous Hyp and a corresponding mixture of Hyp-arabinosides and Hyp-polysaccharides. These results plus circular dichroic spectra of the glycosylated and deglycosylated (Ser-Pro(2))(n), (Ser-Pro(3))(n), and (Ser-Pro(4))(n) modules corroborate the Hyp contiguity hypothesis and indicate that Hyp O-glycosylation is indeed sequence-driven.


Subject(s)
Glycoproteins/metabolism , Hydroxyproline/metabolism , Base Sequence , Glycoproteins/chemistry , Glycoproteins/genetics , Glycosylation , Hydroxyproline/chemistry , Hydroxyproline/genetics , Molecular Sequence Data , Oligonucleotides , Plant Proteins/chemistry , Plant Proteins/genetics , Plant Proteins/metabolism , Plants, Toxic , Nicotiana
5.
Proc Natl Acad Sci U S A ; 96(26): 14736-41, 1999 Dec 21.
Article in English | MEDLINE | ID: mdl-10611282

ABSTRACT

Design of hydroxyproline (Hyp)-rich glycoproteins (HRGPs) offers an approach for the structural and functional analysis of these wall components, which are broadly implicated in plant growth and development. HRGPs consist of multiple small repetitive "glycomodules" extensively O-glycosylated through the Hyp residues. The patterns of Hyp-O-glycosylation are putatively coded by the primary sequence as described by the Hyp contiguity hypothesis, which predicts contiguous Hyp residues to be attachment sites of small arabinooligosaccharides (1-5 Ara residues/Hyp); while clustered, noncontiguous Hyp residues are sites of arabinogalactan polysaccharide attachment. As a test, we designed two simple HRGPs as fusion proteins with green fluorescent protein. The first was a repetitive Ser-Hyp motif that encoded only clustered noncontiguous Hyp residues, predicted polysaccharide addition sites. The resulting glycoprotein had arabinogalactan polysaccharide O-linked to all Hyp residues. The second construct, based on the consensus sequence of a gum arabic HRGP, contained both arabinogalactan and arabinooligosaccharide addition sites and, as predicted, gave a product that contained both saccharide types. These results identify an O-glycosylation code of plants.


Subject(s)
Amino Acid Motifs , Genes, Synthetic , Glycoproteins/genetics , Hydroxyproline/genetics , Nicotiana/genetics , Plants, Toxic , Protein Processing, Post-Translational/genetics , Amino Acid Sequence , Arabinose/metabolism , Base Sequence , Galactans/metabolism , Glycoproteins/metabolism , Glycosylation , Green Fluorescent Proteins , Hydroxyproline/metabolism , Luminescent Proteins/genetics , Molecular Sequence Data , Oligosaccharides/metabolism , Protein Engineering , Recombinant Fusion Proteins , Nicotiana/metabolism
6.
Bioorg Khim ; 22(2): 101-7, 1996 Feb.
Article in Russian | MEDLINE | ID: mdl-8651959

ABSTRACT

A fragment containing the regulatory region of the p. pinII gene was isolated from potato DNA by polymerase chain reaction. Interactions of this DNA region with jasmonate determines the transcriptional activation. The isolated DNA fragment was cloned into the pTE2pb plasmid, which was used for preparing an affinity sorbent. Using this sorbent, four proteins were isolated from the total protein capable of desorption at physiological concentration of jasmonate. These proteins are likely to be subunits of two transcription repressors, whereas jasmonate serves as an inducer. Three sequences of the regulatory regions (boxes G, I, and III) are binding sites for repressors; similar sequences were found in various plant genes activated by jasmonate.


Subject(s)
Cyclopentanes/metabolism , Genes, Plant , Plant Growth Regulators/physiology , Solanum tuberosum/genetics , Transcription, Genetic/physiology , Base Sequence , Cloning, Molecular , Molecular Sequence Data , Oxylipins , Plasmids , Polymerase Chain Reaction , Regulatory Sequences, Nucleic Acid
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