Browse
Submit Data
Databases
API
Help

Dataset Information

11 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Immune reactions in polysaccharide media. The effect of hyaluronate, chondroitin sulphate and chondroitin sulphate-protein complex on the precipitin reaction.

ABSTRACT: The influence of the connective-tissue polysaccharides hyaluronate, chondroitin 4-sulphate and a chondroitin 4-sulphate-protein complex (PP-L) from cartilage on the precipitin reaction was investigated. In a system consisting of (125)I-labelled human serum albumin and the immunoglobulin G fraction from rabbit anti-albumin sera, the precipitation is greatly increased in the region of antigen excess. This effect depends on the concentration, molecular weight and configuration of the polysaccharide. The increase parallels a decrease in the amount of soluble immune complexes in the supernatant. It is suggested that the effect is due to steric exclusion of the complexes from the domains of the polysaccharides. The possibility that such a mechanism might enhance precipitation of antigen-antibody complexes in certain pathological conditions is discussed.

SUBMITTER: Hellsing K

PROVIDER: S-EPMC1187735 | biostudies-other | 1969 May

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

Immune reactions in polysaccharide media. Polysaccharide-enhanced precipitin reactions with antigens of various sizes.

Project description:The influence of the size of the antigen in the polysaccharide-enhanced precipitin reaction was investigated. The experiments were carried out by addition of homologous antigens of different molecular sizes (the monomer, dimer and trimer of serum albumin and the monomer and dimer of immunoglobulin G) to the same preparation of antibody in the absence and presence of dextran. Dextran decreased the solubility of the immune complexes to a larger extent when the antigen size increased. This is in accord with the view that the polysaccharide effect is due to steric exclusion.

| S-EPMC1184807 | biostudies-other

Immune reactions in polysaccharide media. The composition of the antigen-antibody complexes in the precipitin reaction.

Project description:The precipitin reaction is enhanced in the presence of polysaccharides (Hellsing, 1966). This reaction has now been studied in detail with labelled antigen ((125)I-labelled human serum albumin) and antibody ((131)I-labelled rabbit anti-albumin immunoglobulin G). The relative proportions of antigen and antibody in the precipitates are unchanged by the addition of dextran in spite of the increased precipitation. The ratio of antibody to antigen in the soluble immune complexes decreases with increasing polysaccharide concentration. This can be interpreted as a decrease in the aggregate size of the complexes. At the same time the amount of free antigen in the solution increases. The results are consistent with a decrease in solubility, primarily of the large immune aggregates, together with a shift in the equilibrium between small and large complexes. The effect is in accord with a steric-exclusion phenomenon.

| S-EPMC1184806 | biostudies-other

Immune reactions in polysaccharide media. Investigation on complex-formation between some polysaccharides, albumin and immunoglobulin G.

Project description:Serum albumin and immunoglobulin G were chromatographed on columns of dextran, hyaluronate and chondroitin 4-sulphate. The partition of the two proteins between hyaluronate and buffer was also measured by equilibrium dialysis. The results accord with the view that there is no complex-formation between the polysaccharides and the proteins in 0.05m-phosphate buffer, pH7.4, containing sodium chloride (0.1m). The observations support the hypothesis that the previously described polysaccharide enhancement of the precipitin reaction is due to exclusion and not to non-specific complex-formation.

| S-EPMC1187736 | biostudies-other

Binding of hyaluronate and chondroitin sulphate to liver endothelial cells.

Project description:Hyaluronate is taken up and metabolized in liver endothelial cells by means of a receptor. To characterize the interaction with the receptor, two preparations of 3H-labelled hyaluronate, of Mr 4 X 10(5) and 6.4 X 10(6), and a series of hyaluronate oligosaccharides were bound to cultured liver endothelial cells at 7 degrees C. The dissociation constant varied between 4.6 X 10(-6) M for an octasaccharide and 9 X 10(-12) M for the largest polymer. The Mr-dependence for the series of oligosaccharides was explained by the increased probability of binding due to the repetitive sequence along the chain. The high affinity of high-Mr hyaluronate for the receptor could also be mainly ascribed to this effect, which rules out any major contribution of co-operative multiple-site attachment to the cell surface. Each liver endothelial cell can bind 10(5) oligosaccharides, about 10(4) molecules with Mr 4 X 10(5) and about 10(3) molecules with Mr 6.4 X 10(6). This is explained by mutual exclusion of large molecules from the cell surface. Chondroitin sulphate is also bound to liver endothelial cells. Inhibition studies showed that it binds to the same receptor as hyaluronate and with an affinity that is about 3-fold higher than that of hyaluronate of the same degree of polymerization.

| S-EPMC1146621 | biostudies-other

Immune reactions in polysaccharide media. Experiments with specific antibodies of different affinities for serum albumin.

Project description:Rabbit antibody fractions of different affinities for human serum albumin were prepared by an immunosorbent technique. The fractions were used in studies on the enhancement of the precipitin reaction by polymers. Dextran increased the immune precipitation to about the same extent regardless of whether antibodies with high and low affinities were used. The effect should considerably facilitate the detection of antibodies with low precipitating ability in immunological assays. The results are discussed in terms of a steric-exclusion mechanism.

| S-EPMC1184808 | biostudies-other

Protein-polyelectrolyte interactions. The concanavalin A precipitin reaction with polyelectrolytes and polysaccharide derivatives.

Project description:1. Concanavalin A formed precipitates with polyelectrolytes such as fucoidan, RNA, heparin and bacterial lipopolysaccharides. 2. Precipitate formation also occurred between ficoll and concanavalin A. 3. Precipitate formation between concanavalin A and dextran or soluble starch was induced by the incorporation of phosphate groups into the unreactive glucans. 4. Introduction of polar groups, such as acetate, formate and phosphate, into glycogen resulted in enhanced precipitation with concanavalin A, whereas the opposite effect was noted on incorporation of hydrophobic (methyl) centres. 5. Neutral sugars and salt partially inhibited complex-formation between polyelectrolytes and concanavalin A. 6. Concanavalin A-glycogen complexes could be dissociated with 5% (w/v) trichloroacetic acid or 44% phenol-water. 7. Concanavalin A lost its glycogen-complexing ability after phenol treatment. 8. Evidence is presented for the existence of common binding sites on concanavalin A for both neutral polysaccharides and polyelectrolytes. 9. Hydrogen bonding appeared to play a major role in neutral polysaccharide-concanavalin A precipitate formation, whereas both hydrogen bonding and electrostatic forces were implicated in polyelectrolyte-concanavalin A complex-formation.

| S-EPMC1198466 | biostudies-other

Aortic endothelial cells synthesize a large chondroitin sulphate proteoglycan capable of binding to hyaluronate.

Project description:Confluent cultures of mouse aortic endothelial (END-D) were incubated with either [35S]methionine or 35SO4 2-, and the radiolabelled proteoglycans in media and cell layers were analysed for their hyaluronate-binding activity. The proteoglycan subfraction which bound to hyaluronate accounted for about 18% (media) and 10% (cell layers) of the total 35S radioactivity of each proteoglycan fraction. The bound proteoglycan molecules could be dissociated from the aggregates either by digestion with hyaluronate lyase or by treatment with hyaluronate decasaccharides. Digestion of [methionine-35S]proteoglycans with chondroitinase and/or heparitinase, followed by SDS/polyacrylamide-gel electrophoresis, indicated that the medium and cell layer contain at least three chondroitin sulphate proteoglycans, one dermatan sulphate proteoglycan, and two heparan sulphate proteoglycans which differ from one another in the size of core molecules. Among these, only the hydrodynamically large chondroitin sulphate species with an Mr 550,000 core molecule was shown to bind to hyaluronate. A very similar chondroitin sulphate proteoglycan capable of binding to hyaluronate was also found in cultures of calf pulmonary arterial endothelial cells (A.T.C.C. CCL 209). These observations, together with the known effects of hyaluronate on various cellular activities, suggest the existence of possible specialized functions of this proteoglycan subspecies in cellular processes characteristic of vascular development and diseases.

| S-EPMC1136614 | biostudies-other

Multifunctional chondroitin sulphate for cartilage tissue-biomaterial integration.

Project description:A biologically active, high-strength tissue adhesive is needed for numerous medical applications in tissue engineering and regenerative medicine. Integration of biomaterials or implants with surrounding native tissue is crucial for both immediate functionality and long-term performance of the tissue. Here, we use the biopolymer chondroitin sulphate (CS), one of the major components of cartilage extracellular matrix, to develop a novel bioadhesive that is readily applied and acts quickly. CS was chemically functionalized with methacrylate and aldehyde groups on the polysaccharide backbone to chemically bridge biomaterials and tissue proteins via a twofold covalent link. Three-dimensional hydrogels (with and without cells) bonded to articular cartilage defects. In in vitro and in vivo functional studies this approach led to mechanical stability of the hydrogel and tissue repair in cartilage defects.

| S-EPMC8128046 | biostudies-literature

Specificity of the hyaluronate lyase of group-B streptococcus toward unsulphated regions of chondroitin sulphate.

Project description:The purification and properties of a hyaluronate lyase secreted by Streptococcus agalactiae, which is believed to facilitate the invasion of host tissues by the organism, have been described previously [Pritchard, Lin, Willingham and Baker (1994) Arch. Biochem. Biophys. 315, 431-436]. The specificity of the limited cleavage of chondroitin sulphate by the enzyme is the subject of this report. To simplify the task, a chondroitin sulphate from the Swarm rat chondrosarcoma, which contains only 4-sulphated and unsulphated disaccharide repeats, was used in this study. Tetrasaccharides from an ovine testicular hyaluronidase digest of the chondroitin sulphate were isolated, identified and tested as substrates of the streptococcal hyaluronate lyase. Only tetrasaccharides with an unsulphated disaccharide at the reducing end were cleaved (by elimination at the N-acetylgalactosaminidic bond). Thus chondroitin sulphate chains are cleaved by the action of this lyase at every unsulphated disaccharide repeat, but release of unsaturated unsulphated disaccharides only occurs from sites where two or more sequential unsulphated disaccharide repeats are present. Analysis of the chondrosarcoma chondroitin sulphate showed that of approximately five unsulphated disaccharide repeats per chain, two are clustered. The ability of group-B streptococcal hyaluronate lyase to cleave chondroitin sulphate may allow the organisms to invade tissues more efficiently. The demonstrated specific and highly limited cleavage of chondroitin sulphate by this bacterial lyase promises to be a useful tool in the determination of chondroitin sulphate structure and variability.

| S-EPMC1218764 | biostudies-other

New Insights Into Human Hyaluronidase 4/Chondroitin Sulphate Hydrolase

Project description:In this review, the current experimental evidence, literature and hypotheses surrounding hyaluronidase 4 [HYAL4, also known as chondroitin sulphate hydrolase (CHSE)] and chondroitin sulphate (CS) are explored. Originally named for its sequence similarity to other members of the hyaluronidase family, HYAL4 is actually a relatively distinct member of the family, particularly for its unique degradation of CS-D (2-O-, 6-O-sulphated CS) motifs and specific expression. Human HYAL4 protein expression and structural features are discussed in relation to different isoforms, activities, potential localisations and protein-protein interaction partners. CS proteoglycan targets of HYAL4 activity include: serglycin, aggrecan, CD44 and sulfatase 2, with other potential proteoglycans yet to be identified. Importantly, changes in HYAL4 expression changes in human disease have been described for testicular, bladder and kidney cancers, with gene mutations reported for several others including: leukaemia, endometrial, ovarian, colorectal, head and neck, stomach, lung and breast cancers. The HYAL4 gene also plays a role in P53 negative human cancer cell proliferation and is linked to stem cell naivety. However, its role in cancer remains relatively unexplored. Finally, current tools and techniques for the detection of specific HYAL4 activity in biological samples are critically assessed. Understanding the role of HYAL4 in human diseases will fortify our understanding of developmental processes and disease manifestation, ultimately providing novel diagnostic opportunities and therapeutic targets for drug discovery.

| S-EPMC8564380 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data