- Klíčová slova
- ADRENAL CORTEX HORMONES *, ADRENAL GLANDS *, EXPERIMENTAL LAB STUDY *, HISTOCYTOCHEMISTRY *, IRON *, RABBITS *, STAINS AND STAINING *,
- MeSH
- barvení a značení * MeSH
- barvicí látky * MeSH
- histocytochemie * MeSH
- hormony kůry nadledvin * MeSH
- králíci MeSH
- nadledviny * MeSH
- výzkum * MeSH
- železo * MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- barvicí látky * MeSH
- hormony kůry nadledvin * MeSH
- železo * MeSH
Z-scan fluorescence correlation spectroscopy (FCS) is employed to characterize the interaction between arenicin-1 and supported lipid bilayers (SLBs) of different compositions. Lipid analogue C8-BODIPY 500/510C5-HPC and ATTO 465 labelled arenicin-1 are used to detect changes in lipid and peptide diffusion upon addition of unlabelled arenicin-1 to SLBs. Arenicin-1 decreases lipid mobility in negatively charged SLBs. According to diffusion law analysis, microdomains of significantly lower lipid mobility are formed. The analysis of peptide FCS data confirms the presence of microdomains for anionic SLBs. No indications of microdomain formation are detected in SLBs composed purely of zwitterionic lipids. Additionally, our FCS results imply that arenicin-1 exists in the form of oligomers and/or aggregates when interacting with membranes of both compositions.
- MeSH
- biologické modely MeSH
- difuze MeSH
- fluorescenční spektrometrie metody MeSH
- kationické antimikrobiální peptidy chemie metabolismus MeSH
- lipidové dvojvrstvy chemie metabolismus MeSH
- lipidy chemie MeSH
- Publikační typ
- časopisecké články MeSH
- hodnotící studie MeSH
- práce podpořená grantem MeSH
- Názvy látek
- kationické antimikrobiální peptidy MeSH
- lipidové dvojvrstvy MeSH
- lipidy MeSH
The rosettes formed by mouse peritoneal macrophages or DCH-5 cells and TNP-erythrocytes coated with anti-TNP antibodies of different isotypes were inhibited to various extent by monosaccharides. The most effective inhibitors were N-acetylglucosamine, glucosamine, mannose and N-acetylneuraminic acid in 1-5 mmol/L concentrations. Even more efficient were glycopeptides isolated from IgG molecules. The Fc receptors (FcRs) released from DCH-5 cells during cultivation and gradually separated by affinity chromatography on immobilized IgG reacted with aggregated IgG and inhibited the rosette formation. The FcRs eluted by monosaccharides influenced mainly the number of rosettes mediated by IgA and IgE while those eluted with a glycine-HCl buffer inhibited preferentially IgG rosettes. As shown by SDS-PAGE the heterogeneity of the fraction eluted with a mixture of monosaccharides revealed one main component with an effective molar mass of 50 kg/mol. The glycine-HCl eluate contained two major components of 55 and 38 kg/mol. The IgG-Sepharose 4B bound all the fractions but only the binding of the 50 kg/mol molecule could be inhibited by monosaccharides.
- MeSH
- diferenciační antigeny metabolismus MeSH
- glykopeptidy metabolismus MeSH
- imunoglobulin G chemie metabolismus MeSH
- kultivované buňky MeSH
- monosacharidy metabolismus MeSH
- myši inbrední A MeSH
- myši MeSH
- prasata MeSH
- receptory Fc metabolismus MeSH
- receptory IgG MeSH
- tvorba rozet MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- diferenciační antigeny MeSH
- glykopeptidy MeSH
- imunoglobulin G MeSH
- monosacharidy MeSH
- receptory Fc MeSH
- receptory IgG MeSH
Fc receptors, belonging to the most important surface structures of a number of cells participating in the immune processes, have been intensely studied during the past decade. The present review summarizes the contemporary knowledge of the specificity and heterogeneity of Fc receptors and of factors influencing their expression, and includes some views on their function. In addition, it mentions their relationship to other cell surface structures, expression of Fc receptors during ontogeny of the organism and in certain diseases. Finally, data concerning the isolation and biochemical characterization of the Fc receptor molecule are presented.
- MeSH
- alergologie a imunologie MeSH
- buňky imunologie MeSH
- chemické modely MeSH
- imunoglobuliny metabolismus MeSH
- lidé MeSH
- metody MeSH
- molekulová hmotnost MeSH
- receptory Fc * analýza genetika izolace a purifikace metabolismus fyziologie MeSH
- specificita protilátek MeSH
- vazebná místa protilátek MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
- Názvy látek
- imunoglobuliny MeSH
- receptory Fc * MeSH
Fc gamma Receptor contained in a mixture of plasma-membrane components released from pig peripheral blood lymphocytes following a 4----37 degrees C temperature shift was isolated by affinity chromatography on immobilized pig IgG. The main component of the receptor preparation exhibited an apparent molecular weight of 40-43 kDa in SDS polyacrylamide gel electrophoresis. Specificity of interaction of isolated Fc gamma receptor with immobilized pig IgG (Ka = 5.4 x 10(6) M-1) was investigated by competitive radioimmunoassay employing labelled Fc gamma receptor. The interaction was specifically inhibited by pig IgG, its Fc fragment, and less so by its pFc' fragment. Inhibition by peptides prepared from the pig IgG CH3 domain pointed to the heavy chain segment between residues 340 and 380 as the probable location of the binding site. In the competitive assay, bovine, human, mouse and guinea pig IgGs were as effective inhibitors as the homologous IgG, while rabbit IgG produced weaker inhibition. The amino acid composition of the pig lymphocyte Fc gamma receptor was determined. Comparison with the amino acid compositions of some other Fc receptors and other proteins revealed its structural relatedness to several Fc gamma receptors of lymphoid cells and to the poly-Ig receptor. In addition, the comparison of amino acid compositions suggested a structural relationship between the pig Fc gamma receptor and some seemingly unrelated proteins.
- MeSH
- aminokyseliny analýza MeSH
- buněčná membrána analýza MeSH
- chromatografie afinitní MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- imunoglobulin G metabolismus MeSH
- lymfocyty analýza MeSH
- prasata MeSH
- radioimunoanalýza MeSH
- receptory Fc izolace a purifikace metabolismus MeSH
- spektrofotometrie MeSH
- teplota MeSH
- vazebná místa protilátek MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- aminokyseliny MeSH
- imunoglobulin G MeSH
- receptory Fc MeSH
The structure of the Fc fragment of monoclonal antibody IgG2b from hybridom M75 of Mus musculus has been determined by single crystal X-ray diffraction. This is the first report of the structure of the murine immunoglobulin isotype IgG2b. The structure refined at 2.1 A resolution provides more detailed structural information about native oligosaccharides than was previously available. High-quality Fourier maps provide a clear identification of alpha-l-fucose with partial occupancy in the first branch of the antennary oligosaccharides. A unique Fc:Fc interaction was observed at the C(H)2-C(H)3 interface.
- MeSH
- glykosylace MeSH
- imunoglobulin G chemie MeSH
- imunoglobuliny - Fc fragmenty chemie MeSH
- imunokomplex chemie MeSH
- krystalizace MeSH
- krystalografie rentgenová metody MeSH
- monoklonální protilátky chemie MeSH
- myši MeSH
- oligosacharidy chemie MeSH
- sekundární struktura proteinů MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- imunoglobulin G MeSH
- imunoglobuliny - Fc fragmenty MeSH
- imunokomplex MeSH
- monoklonální protilátky MeSH
- oligosacharidy MeSH
Precipitating and non-precipitating anti-Dnp antibodies and S-sulpho non-specific IgG in gram quantities were subjected to limited cleavage by trypsin. Upon gel chromatography on Sephadex G-100 the fraction of Fab and Fc fragments was separated from incompletely split molecules and from tFc' fragments. The Fab and Fc fragments were separated from each other either by ion-exchange chromatography on QAE-Sephadex or by preparative electrophoresis in starch block. Both Fab and Fc fragments appeared to be heterogeneous as to electric charge. The Fc fragments were characterized by amino acid composition and N-terminal amino acids. The Fc fragment of non-specific IgG was cleaved by cyanogen bromide, and a C-terminal peptide containing 18 residues was isolated. Partial amino acid sequence of this peptide pointed to a high degree of homology with immunoglobulins of other animal species.
- MeSH
- aminokyseliny analýza MeSH
- bromkyan MeSH
- dinitrofenoly imunologie MeSH
- imunoglobulin G analýza MeSH
- imunoglobuliny - Fab fragmenty izolace a purifikace MeSH
- imunoglobuliny - Fc fragmenty izolace a purifikace MeSH
- imunoglobuliny - fragmenty izolace a purifikace MeSH
- peptidy analýza MeSH
- prasata imunologie MeSH
- precipitiny analýza MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- aminokyseliny MeSH
- bromkyan MeSH
- dinitrofenoly MeSH
- imunoglobulin G MeSH
- imunoglobuliny - Fab fragmenty MeSH
- imunoglobuliny - Fc fragmenty MeSH
- imunoglobuliny - fragmenty MeSH
- peptidy MeSH
- precipitiny MeSH
The effect of bilirubin on the phagocytic activity of mouse peritoneal macrophages and on the expression of Fc receptors and receptors for SRBC was studied. Intraperitoneally administered bilirubin influenced the expression of Fc receptors for IgM, IgG2B, IgA and IgE, whereas the expression of other receptors as well as the phagocytic activity of peritoneal macrophages remained unchanged. The possible mechanism of the effect of bilirubin on Fc receptors is discussed.
- MeSH
- bilirubin farmakologie MeSH
- fagocytóza účinky léků MeSH
- makrofágy účinky léků imunologie MeSH
- myši inbrední BALB C MeSH
- myši MeSH
- receptory Fc účinky léků MeSH
- tvorba rozet MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bilirubin MeSH
- receptory Fc MeSH
Immunoglobulin A (IgA) proteinase from Clostridium ramosum is the enzyme which cleaves IgA of both subclasses; in contrast, the other bacterial proteinases cleave only IgA1 proteins. Previous reports characterized the activity of proteinase naturally secreted by C. ramosum specific for the normal human serum IgA of IgA1 and IgA2m(1) subclasses and also for secretory IgA (SIgA). Its amino acid sequence was determined, and the recombinant proteinase which cleaved IgA of both subclasses was prepared. Here we report the optimized expression, purification, storage conditions and activity testing against purified human milk SIgA. The recombinant C. ramosum IgA proteinase isolated in the high degree of purity exhibited almost complete cleavage of SIgA of both subclasses. The proteinase remained active upon storage for more than 10 month at -20 °C without substantial loss of enzymatic activity. Purified SIgA fragments are suitable for studies of all antigen-binding and Fc-dependent functions of SIgA involved in the protection against infections with mucosal pathogens.
- Klíčová slova
- Clostridium ramosum, Enzymatic activity, IgA proteinase, Storage conditions,
- MeSH
- bakteriální proteiny chemie genetika MeSH
- Firmicutes enzymologie genetika MeSH
- imunoglobulin A sekreční chemie MeSH
- imunoglobuliny - Fab fragmenty * chemie izolace a purifikace MeSH
- imunoglobuliny - Fc fragmenty * chemie izolace a purifikace MeSH
- lidé MeSH
- proteasy chemie genetika MeSH
- rekombinantní proteiny chemie genetika MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bakteriální proteiny MeSH
- imunoglobulin A sekreční MeSH
- imunoglobuliny - Fab fragmenty * MeSH
- imunoglobuliny - Fc fragmenty * MeSH
- proteasy MeSH
- rekombinantní proteiny MeSH
The heterogeneity of resident peritoneal macrophages and peritoneal macrophages was studied in different periods following oral administration of sodium nucleinate according to their ability to bind and phagocytize sheep erythrocytes opsonized by means of specific rabbit IgG. Using a mathematical method developed earlier, it has been possible to demonstrate that resident peritoneal macrophages can be divided into two subpopulations--actively and poorly binding macrophages but, after activation by sodium nucleinate--into three subpopulations. Fractionation of the macrophages according to their ability to adhesion within a temperature gradient has shown that the same peaks are traced in the fractions as in the overall pool of cells, but in different quantitative ratios. It has also been demonstrated that phagocytic activity is reduced in macrophages capable of adhesion to plastic at lower temperatures.
- MeSH
- imunoglobulin G imunologie MeSH
- inbrední kmeny myší MeSH
- makrofágy cytologie imunologie MeSH
- myši MeSH
- receptory Fc analýza MeSH
- receptory IgG MeSH
- separace buněk MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- imunoglobulin G MeSH
- receptory Fc MeSH
- receptory IgG MeSH