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Results for “HYALURONIC ACID”

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PubMed2005

Use of hyaluronidase in the treatment of granulomatous hyaluronic acid reactions or unwanted hyaluronic acid misplacement.

BACKGROUND: In the past, reactions or misplacement of soft tissue fillers has been fraught with anxiety because time has been the main thrust for improvement in spite of ancillary treatments. Hyaluronidase is an enzyme that dissolves hyaluronic acid in the skin and also assists in the management of granulomatous foreign-body reactions to hyaluronic acid. These reactions may be caused by allergy to the material or immunologic response to the protein contaminants in the hyaluronic acid preparations. Dissolution of material in erroneous placement of material and in allergic reactions can be a time saver and a deterrent to patient dissatisfaction. OBJECTIVE: To evaluate the use of hyaluronidase in the treatment of both allergic reactions and the erroneous misplacement of hyaluronic acid in the skin. METHODS: A case of persistent granulomatous reaction to injectable hyaluronic acid and a case of hyaluronic acid erroneous misplacement with their successful subsequent treatments using intracutaneous hyaluronidase are reported, along with illustrative examples of hyaluronidase use. RESULTS: The use of hyaluronidase reduced the patient discomfort within 24 to 48 hours, deterring any patient anxiety or patient dissatisfaction. CONCLUSIONS: Hyaluronidase has a place in the treatment of allergic reactions to hyaluronic acid [corrected] and in the erroneous misplacement of the material.

Aged↗
PubMedDate not supplied

Stimulatory effects of ascorbic acid on hyaluronic acid synthesis of in vitro cultured normal and glaucomatous trabecular meshwork cells of the human eye.

The outflow of aqueous humor of the primate eye occurs across the filter system of the trabecular meshwork (TM) into Schlemm's canal. Cells of TM derived from a normal (TM-N-cells) and a glaucomatous human eye (TM-G-cells) were established in monolayer culture. The present comparative experiments were performed with cells kept in a defined serum-free medium (the aqueous humor is nearly protein-free!). Under these conditions the cells stay alive for several months in a non-proliferating state. TM-G-cells exhibited a lower synthesis rate of glycosaminoglycans-especially of hyaluronic acid (HA)--than TM-N-cells. Addition of 50-200 micrograms/ml ascorbic acid (the aqueous humor is characterized by a high ascorbic acid concentration of about 150 micrograms/ml) to the culture medium resulted in a significant dose-dependent stimulation of HA-synthesis and secretion, which was relatively stronger in case of TM-G-cells than with TM-N-cells. Thus, the results suggest a role of ascorbic acid in the probably membrane-localized HA-synthesis. Functions of ascorbic acid and HA for the morphological and functional integrity of the TM-cells in vitro and the outflow apparatus in vivo were discussed.

Adult↗
PubMed1977

Interaction of cartilage proteoglycans with hyaluronic acid. The role of the hyaluronic acid carboxyl groups.

Hyaluronic acid-derived oligomers of five to fifteen repeat dissaccharides effectively bind to bovine nasal-cartilage proteoglycan and inhibit the interaction between proteoglycans and high-molecular-weight hyaluronic acid. If, however, the hyaluronic acid oligosaccharides are modified by reaction with diazomethane to form the carboxyl methyl esters of the glucuronic acid residues, their inhibitory activity is abolished. The binding capacity can be fully restored by saponification. The amide derivative, which is formed by condensation of the oligosaccharide carboxyl groups with glycine methyl ester, is also ineffective in blocking the proteoglycan-hyaluronic acid interaction. In this case, binding activity is not restored when the amidated oligomers are subjected to saponification to yield the free carboxylate groups on the glycine residues. Thus the displacement of the carboxylate groups on the polysaccharide chain by the interposition of a glycine residue blocks the interaction between the proteoglycans and the hyaluronic acid oligomers. When the oligosaccharide methyl ester is reduced with NaBH4, the resultant glucose-containing oligomers exhibit decreased binding to proteoglycans. Thus it appears that the hyaluronic acid carboxylate anion in a specific spatial orientation is required for hyaluronic acid-proteoglycan interaction.

Animals↗
PubMed1982

Inhibition of active E rosette forming T lymphocytes by hyaluronic acid. Evidence of a receptor for hyaluronic acid on a lymphocyte subpopulation.

Previous studies have shown the inhibition of active E rosette forming T lymphocytes by a mesenchyme associated antigen. Recent results clearly indicated that this antigen consisted in the association of a glycoprotein named hyaluronectin with hyaluronic acid. Using the active E rosette technique of Wybran and Fudenberg, we have studied the action of hyaluronic acid on T lymphocytes. We obtained evidence of the partial inhibition of active E rosette formation by hyaluronic acid in 19 of 25 healthy subjects. Among them, inhibition percentage was 45 +/- 4. This inhibition remained significant at a concentration of 22.5 micrograms/ml hyaluronic acid. Hyaluronic acid was labelled with peroxidase by the glutaraldehyde technique: 17 +/- 7% lymphocytes were stained by this preparation. The preincubation of peroxydase labelled hyaluronic acid by brain hyaluronectin lowered this staining. This is in agreement with the presence of hyaluronectin on a subpopulation of lymphocytes as it was shown by immunofluorescence techniques. In conclusion, a receptor for hyaluronic acid (hyaluronectin) was detected on a proportion of lymphocytes. These results suggest that hyaluronic acid could have an immunosuppressive activity.

Humans↗
PubMed1999

Capillary electrophoresis of N-acetylneuraminic acid polymers and hyaluronic acid: correlation between migration order reversal and biological functions.

High-resolution analysis of polymers of N-acetylneuraminic acid and hyaluronic acid was performed by capillary electrophoresis in a buffer containing a neutral polymer. Both polysaccharides having more than 100 monosaccharide residues were well separated into their molecular species by capillary electrophoresis using a combination of a chemically modified capillary and a buffer containing poly(ethylene glycol) as an additive. During optimization of the separation conditions, small oligomers of both polysaccharides were observed to migrate in the reverse order of their molecular masses on the electropherograms. However, oligomers larger than pentamer and decamer for N-acetylneuraminic acid polymers and hyaluronic acid, respectively, migrated in the order of their molecular masses. We propose that these unusual migration patterns are closely related to the stereochemical structures and the oligomer migrating the fastest is the minimum unit that forms the regular three-dimensional structure required for the biological function.

Carbohydrate Sequence↗
PubMed1989

Degradation of human proteoglycan aggregate induced by hydrogen peroxide. Protein fragmentation, amino acid modification and hyaluronic acid cleavage.

We have previously shown that treatment of neonatal human articular-cartilage proteoglycan aggregates with H2O2 results in loss of the ability of the proteoglycan subunits to interact with hyaluronic acid and in fragmentation of the link proteins [Roberts, Mort & Roughley (1987) Biochem. J. 247, 349-357]. We now show the following. (1) Hyaluronic acid in proteoglycan aggregates is also fragmented by treatment with H2O2. (2) Although H2O2 treatment results in loss of the ability of the proteoglycan subunits to interact with hyaluronic acid, the loss of this function is not attributable to substantial cleavage of the hyaluronic acid-binding region of the proteoglycan subunits. (3) In contrast, link proteins retain the ability to bind to hyaluronic acid following treatment with H2O2. (4) The interaction between the proteoglycan subunit and link protein is, however, abolished. (5) N-Terminal sequence analysis of the first eight residues of the major product of link protein resulting from H2O2 treatment revealed that cleavage occurred between residues 13 and 14, so that the new N-terminal amino acid is alanine. (6) In addition, a histidine (residue 16) is converted into alanine and an asparagine (residue 21) is converted into aspartate by the action of H2O2. (7) Rat link protein showed no cleavage or modifications in similar positions under identical conditions. (8) This species variation may be related to the different availability of histidine residues required for the co-ordination of the transition metal ion involved in hydroxyl-radical generation from H2O2. (9) Changes in function of these structural macromolecules as a result of the action of H2O2 may be consequences of both fragmentation and chemical modification.

Amino Acid Sequence↗
PubMed1982

Methyl derivatives of 2-acetamido-2-deoxy-3-O-(beta-D-glucopyranosyluronic acid)-D-glucose (hyalobiouronic acid) from methylated hyaluronic acid.

Methanolysis of methylated hyaluronic acid, followed by acetylation, gave, in 70% yield, crystalline methyl 2-acetamido-2-deoxy-4,6-di-O-methyl-3-O-(methyl 4-O-acetyl-2,3-di-O-methyl-beta-D-glucopyranosyluronate) -alpha-D-glucopyranoside. Removal of the O-acetyl and methyl ester groups gave compounds that are useful in the investigation, by 1H-n.m.r. spectroscopy, of interaction within chains of hyaluronic acid in solution.

Carbohydrate Conformation↗
PubMed1988

Antioxidant activity of synovial fluid, hyaluronic acid, and two subcomponents of hyaluronic acid. Synovial fluid scavenging effect is enhanced in rheumatoid arthritis patients.

To test the scavenging of reactive oxygen species (ROS), we added synovial fluids from patients with rheumatoid arthritis (RA) and osteoarthritis, as well as hyaluronic acid (HA) and its 2 subcomponents, D-glucuronic acid and N-acetyl-D-glucosamine, to 2 ROS-generating systems, activated neutrophils and xanthine-xanthine oxidase. Synovial fluid from RA patients, HA, and D-glucuronic acid markedly decreased the O2-, H2O2, OH., and chemiluminescence measured in both systems. HA and synovial fluid, which are known to be susceptible to degradation by excessive ROS in RA patients, also seem to play an active role in protecting articular tissues from oxidative damage.

Acetylglucosamine↗
PubMed1998

The role of cytokines in cervical ripening: correlations between the concentrations of cytokines and hyaluronic acid in cervical mucus and the induction of hyaluronic acid production by inflammatory cytokines by human cervical fibroblasts.

OBJECTIVES: The purpose of our study was (1) to explain the relationship between levels of inflammatory cytokines and levels of hyaluronic acid in cervical mucus of pregnant women and (2) to investigate whether cytokines promote hyaluronic acid production by human cervical fibroblasts in vitro. STUDY DESIGN: The concentration of hyaluronic acid, interleukin-1beta, and interleukin-8 were measured in cervical mucus of pregnant women, and hyaluronic acid production by cytokine-treated (interleukin-1beta and interleukin-8) cultured fibroblasts was measured. RESULTS: Hyaluronic acid concentrations in the mucus of pregnant women with threatened premature labor were higher than in mucus of normal pregnant women (P < .05). Correlations were found between hyaluronic acid concentrations and interleukin-1beta (P = .018) and interleukin-8 (P = .003) concentrations in cervical mucus. Cytokines (especially interleukin-8) stimulated hyaluronic acid production by cultured cervical fibroblasts. CONCLUSION: Cytokines induce hyaluronic acid production by human cervical fibroblasts, which may promote cervical ripening.

Adult↗
PubMed1969

Studies on the structure of hyaluronic acid. Characterization of the product formed when hyaluronic acid is treated with ascorbic acid.

Physical and chemical methods were used to characterize hyaluronic acid before (fraction HAIIBI) and after (fraction HA-AA) treatment with ascorbic acid. Fraction HA-AA was recovered with an almost quantitative yield and was shown to be chemically identical with fraction HAIIBI by all the methods used. These two materials, however, differed markedly in their molecular sizes and degree of polydispersity. By using sedimentation, diffusion and sedimentation-equilibrium analyses, weight-average molecular weights of about 1.2x10(6) and 6.5x10(4) respectively were obtained for fractions HAIIBI and HA-AA. It is concluded from these results that hyaluronic acid has a molecular weight of about 65000 and that the polysaccharide chain of this molecule is not depolymerized by ascorbic acid. It is further proposed that hyaluronic acid molecules in the matrix of connective tissues are present either in an aggregated form or as subunits of heterogeneous macromolecules, and that it is the linkages responsible for the organization of these structures which are broken by ascorbic acid.

Animals↗