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PubMed2005

[Experience with glucosamine hydrochloride in the treatment of patients with osteoarthrosis].

AIM: To study efficacy and tolerance of glucosamine hydrochloride (GH) in osteoarthrosis (OA). MATERIAL AND METHODS: GH was given to patients of the study group (n = 30) for 2 months in a dose 1200 mg/day, while diclofenak was administered to the patients from the control group (n = 24) in a dose 100 mg/day. Clinical, laboratory activity of the disease was estimated before the study, after it, 3 and 6 months later. Side effects were also studied. The efficacy of GH therapy was estimated according to the Lequesne's index, pain intensity on vision-analogy scale (VAS), doses of non-steroidal anti-inflammatory drugs during the day. RESULTS: A decrease in the Lequesne's index and pain by VAS while walking, requirements of NSAIDs in OA patients were revealed. No unfavorable aftereffects of GH were observed. CONCLUSION: GH relieves pain, improves function of the affected joints, reduces necessity in NSAIDs. The effect persists for 3 months. No side effects were registered.

Female↗
PubMed2006

Short-term gene expression changes in cartilage explants stimulated with interleukin beta plus glucosamine and chondroitin sulfate.

OBJECTIVE: To determine the short-term effects of glucosamine (GLN) and chondroitin sulfate (CS) on expression of genes encoding inflammatory mediators and matrix enzymes in bovine cartilage explants stimulated with interleukin 1 (IL-1). METHODS: Dose-response experiments were conducted for IL-1, GLN, and CS to select concentrations of each optimized for detecting treatment effects on cartilage explants. Based on the dose-response experiments, treatments included fetal bovine serum (FBS) control, 15 ng/ml IL-1, and 15 ng/ml IL-1 with the addition of 10 microg/ml GLN and 20 microg/ml CS. Media were measured for nitric oxide (NO) and prostaglandin E2 (PGE2) while explants were frozen for RNA extraction at 8, 16, and 24 hours. Gene expression relative to FBS control for inducible NO synthase (iNOS), cyclooxygenase-2 (COX-2), microsomal PGE synthase-1 (mPGEs1), nuclear factor-kB p65 subunit (NF-kB), matrix metalloproteinase (MMP)-3 and 13, aggrecanase (Agg)-1 and 2, and tissue inhibitor of metalloproteinase-3 (TIMP-3) were assessed by quantitative real-time polymerase chain reaction (RT-PCR). In a separate study using incubation of explants with the same treatments for 48 hours, proteoglycan release was measured with dimethylmethylene blue assay and TIMP-3 protein was evaluated with Western blots. RESULTS: The GLN and CS combination abrogated IL-1-induced gene expression of iNOS, COX-2, mPGEs1, and NF-kB at all timepoints. NO, PGE2, and proteoglycan release were reduced with the combination. The abundance of stimulated MMP-13, Agg-1, and Agg-2 mRNA was repressed, whereas TIMP-3 was upregulated by the combination at all timepoints. The abundance of TIMP-3 protein was increased by the combination relative to IL-1 at 48 hours. CONCLUSION: GLN and CS in combination suppress synthesis and expression of genes encoding inflammatory mediators and proteolytic enzymes while upregulating TIMP-3. This provides a plausible mechanism for the purported mild antiinflammatory and chondroprotective properties of GLN and CS.

Animals↗
PubMedDate not supplied

On the detection of a blood-joint barrier for radiosulfate and [3H]glucosamine in single joints of aging rats.

A blood-joint barrier effect has been detected for two precursors of glycosaminoglycan biosynthesis (35SO4 and [3H]glucosamine) in single joints of adult Wistar rats by calculating the ratio between their blood plasma levels in the equilibrium range and their incorporation rates into joint tissues of knee joints (tibia and femur parts, patella) or femur and humerus heads. The barrier effect appears to be joint specific in the adult rat, because it was not found in joints of one month old rats and in tendon tissue. In 17 months old rats the barrier effect increased indicating a diminished supply of the joints with both precursors. Incorporation rates into the joint tissues, however, were higher than into the isolated glycosaminoglycans of aged rats indicating the barrier effect to be not the only cause for a diminished glycosaminoglycan biosynthesis in joint cartilage of aging rats.

Aging↗
PubMedDate not supplied

[The influence of glucosamine on the antiexudative effect of nonsteroidal anti-inflammatory agents].

The study of the antiexudative activities of voltaren, indomethacin and piroxicam in combination with glucosamine on the model of carrageenan inflammation showed that the combination makes it possible to decrease the effective doses of nonsteroidal anti-inflammatory drugs by 2-2.7 times with the preservation of the pronounced antiexudative activity. A diverse influence of aminosugar on the anti-inflammatory effect of nonsteroidal anti-inflammatory drugs depending on the sequence and routes of administration is connected with their membrane mechanisms and metabolic features of amino sugar.

Acute Disease↗
PubMed1991

Antiarthritic effects of glucosamine sulfate studied in animal models.

The antireactive activity of glucosamine sulfate (GS) (CAS 29031-19-4) was tested in the rat in experimental models of subacute inflammation (sponge granuloma and croton oil granuloma), on subacute mechanical arthritis (kaolin arthritis) and in immunological-reactive arthritis and generalized inflammation (adjuvant arthritis). On these models GS was found effective in oral daily doses of 50-800 mg/kg. Tne potency of GS in comparison of that of indometacin used in the same tests as reference substance was found 50-300 times lower. Since, however, the toxicity of indometacin in chronic toxicity experiments is 1000-4000 times larger, the therapeutic margin with regard to prolonged treatments of inflammatory disorders results 10-30 times more favourable for GS than for indometacin. GS can therefore be considered as a drug of choice for prolonged oral treatment of rheumatic disorders.

Animals↗
PubMed1990

Non-specific protective activity of synthetic lipid A-subunit analogs against microbial infections is influenced by their 2-N- and 3-O-linked acyl substituents in the D-glucosamine backbone.

Non-specific protective activities against vaccinia virus (VV) and Pseudomonas aeruginosa infections as well as interferon (IFN)-inducing, natural killer (NK) cell and macrophage activation activities of chemically synthesized lipid A-subunit analogs were investigated. The analogs are 4-O-phosphono-D-glucosamine derivatives carrying different 2-N- and 3-O-linked acyl substituents such as (R)-3-tetradecanoyloxytetradecanoyl (C14-O-(C14)), (R)-3-hydroxytetradecanoyl (C14-OH) and tetradecanoyl (C14) groups. Compounds GLA-59 and GLA-60, which possess C14-OH and C14-O-(C14) groups as their acyl substituents, showed stronger IFN-inducing and anti-vaccinia virus activities than GLA-27 and GLA-68, which possess a C14 group instead of the C14-OH group in GLA-59 and GLA-60, although NK cell activation activity was similarly high in all of these compounds. In protective activity against P. aeruginosa infection and macrophage activation activity, GLA-60 and GLA-68, which carry a C14-O-(C14) group at the 3-O-position, expressed higher activities than GLA-27 and GLA-59, which carry the acyloxyacyl group at the 2-N-position. These results indicate that the acyl substituent (whether the counterpart of the C14-O-(C14) group is a C14 or a C14-OH group) and the binding position of the acyloxyacyl group at the 2-N- or the 3-O-position strongly influence the manifestation of antimicrobial and immunomodulating activities in different ways depending on the activity. Among the compounds, GLA-60 satisfied the structure requirements for protection against both VV and P. aeruginosa infections. This compound is a hopeful immunomodulator for prevention against broad microbial infections.

Adjuvants, Immunologic↗
PubMedDate not supplied

In-vivo biosynthesis of acid glycosaminoglycans with radiosulfate and [3H]glucosamine in single joints from rats of different age.

Administration intraperitoneally of 35SO4 plus D-[6-3H]glucosamine of similarly specific radioactivity to rats of different ages showed uptake rates and incorporation to be higher with 35SO4 in articular cartilage. Comparing the joints studied: knee joints (femur and tibia parts), humerus, and femur heads, cartilage cells appeared to be most metabolically active (age-dependently) in femur heads. All cells, in addition to glycoproteins, synthesized in vivo isomeric chondroitin sulfates and hyaluronate at different rates.

Aging↗
PubMed1979

Stabilization and purification of glucosamine 6-phosphate isomerase from rat kidney.

1. Glucosamine 6-phosphate (GlcN-6-P) isomerase of rat kidney was resistant to heating at 50--55 degrees in crude extract but not after several purification steps. GlcN-6-P and N-acetylglucosamine 6-phosphate were found to stabilize the isomerase under these conditions. They also protected the enzyme from tryptic digestion, but only GlcN-6-P was effective against inactivation by p-chloromercuribenzoate. 2. When GlcN-6P isomerase was purified from fresh kidney and kidney stored at -20 degrees, separately and under GlcN-6-P, the two preparations were different in elution profile from a hydroxyapatite column. It was subsequently found that storage of crude extract at -20 degrees resulted in molecular alterations of the enzyme. Prolonged purification appeared to affect the enzyme similarly. The molecular alterations, however, were suppressed if the extract was stored at -70 degrees. 3. These findings have been utilized to develop a procedure, which enables us to purify rat kidney GlcN-6-P isomerase without any molecular alteration and in good yield.

Aldose-Ketose Isomerases↗
PubMed1986

Effects of D-glucosamine and 6-azauridine on nucleotide contents, 5-fluorouridine uptake, and cytotoxicity in TA3 mammary tumor cells.

In TA3 mammary carcinoma cells in suspension culture, D-glucosamine X HCl (GlcN) induced a diversion of uridylate from UTP into UDP-N-acetylhexosamines, reducing the intracellular pool of UTP and eliciting an increased rate of de novo uridylate synthesis. This rise in de novo synthesis was completely suppressed by addition of 6-azauridine (6-AzaUrd) to the cell suspension in vitro or in the solid TA3 mammary tumor in NMRI mice in vivo. A synergistic depletion of UTP pools to less than 6% of the UTP in controls was observed in TA3 cell suspensions exposed to GlcN and 6-AzaUrd. In solid TA3 tumors in vivo, UTP was reduced by this combination to 19% of the control value. A high sensitivity of the solid tumor to inhibition of pyrimidine synthesis de novo was indicated by the reduction of the UTP content after administration of 6-AzaUrd alone. UTP deficiency in TA3 tumor cells was accompanied by CTP deficiency. In addition, 6-AzaUrd caused a lowering of GTP in the neoplastic tissue. Host liver was resistant to 6-AzaUrd but responded to treatment with GlcN with a decrease in UTP to 67%. Uridine-cytidine kinase was less inhibited in the presence of lowered UTP and CTP, which are potent feedback inhibitors of the enzyme, and enabled an enhanced formation of phosphorylated derivatives of 5-fluorouridine (FUrd). Aside from the formation of 5-fluoro-UTP, we have identified 5-fluoro-UDP-N-acetylhexosamines (FUDPHexNAc), which accumulated when FUrd and GlcN were sequentially administered. Treatment of TA3 cells with FUrd after a pretreatment with 6-AzaUrd and GlcN resulted in a 2.5-fold increase in [14C]FUrd uptake and a duplication of 5-fluorouridylate incorporation into the RNA. The proportion of FUDPHexNAc increased to 58% of the phosphorylated FUrd metabolites, as compared to 6% in TA3 cells exposed exclusively to FUrd. In vivo chemotherapy of mice bearing TA3 ascites tumors was most effective with respect to tumor growth inhibition and animal survival when GlcN and FUrd were combined.

Adenosine Triphosphate↗
PubMed1989

Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine.

Non-acetylated glucosamine is an unusual structural feature shared by all glycosyl phosphatidylinositol (GPI) lipids, including a variety of membrane anchors, the leishmanial lipophosphoglycan, and a mediator of insulin action. We proposed previously a pathway for biosynthesis of glycolipid A, the precursor of the GPI membrane anchor of the trypanosome variant surface glycoprotein (Masterson, W. J., Doering, T. L., Hart, G. W., and Englund, P. T. (1989) Cell 56, 793-800). In this paper we characterize in more detail the initial steps of GPI assembly. The first and committed step in the pathway is the transfer of GlcNAc, from UDP-GlcNAc, to endogenous phosphatidylinositol to form N-acetylglucosaminyl phosphatidylinositol (GlcNAc-PI). The GlcNAc-PI is then efficiently deacetylated to form glucosaminyl phosphatidylinositol (GlcN-PI), the substrate for subsequent reactions en route to glycolipid A.

Acetylation↗
PubMed1989

O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.

Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety. We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase. Glycosylation appears to occur on one or more serine or threonine residues in the following sequence: Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys . This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing. Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides. These results appear to suggest the functional or biological significance of the O-GlcNAc linkage in protein 4.1.

Acetylglucosamine↗
PubMed1987

Determination of binding constants for N-acetyl-D-glucosamine oligomers with lysozyme.

A method to determine intrinsic binding constants of lysozyme with substrate analogues such as N-acetyl-D-glucosamine dimer and trimer is proposed. The method is based on the competitive interaction of an anionic azo dye with substrate analogues for lysozyme. There are two binding sites for substrate analogues and dyes, respectively, on lysozyme. One binding mode of the substrate analogues to subsites D-F on lysozyme was non-competitive, and another binding mode to subsites A-C was competitive with the dye. From the binding constants obtained it is suggested that the binding of the substrate analogues to subsite D on lysozyme is weaker than the binding to the other subsites.

Acetylglucosamine↗
PubMed1986

Polyclonal B cell activation by a B cell differentiation factor, B151-TRF2. II. Evidence for interaction of B151-TRF2 with glycoprotein on B cell membrane via recognition of terminal N-acetyl-D-glucosamine residue(s).

We investigated the role of carbohydrates in the interaction of a B cell differentiation factor designated as B151-TRF2 derived from B151K12 T cell hybridoma with the corresponding receptor on B cells. Induction of polyclonal differentiation of unprimed B cells into IgM-secreting cells by B151-TRF2 was specifically inhibited by addition of N-acetyl-D-glucosamine (GlcNAc) but not by structurally unrelated monosaccharides such as D-galactose, D-glucose, and N-acetyl-D-galactosamine (GalNAc). Absorption of B151-TRF2 activity with spleen cells was specifically inhibited by the presence of GlcNAc. These results indicate that GlcNAc residues are involved in the interaction of B151-TRF2 with the receptor on B cells. To gain insight into mechanism by which GlcNAc inhibits B151-TRF2-mediated B cell responses, the existence of GlcNAc residues was examined on the B151-TRF2 molecule and the corresponding receptor on the B cell surface. The results revealed that B151-TRF2 molecule was not bound to various lectin-coupled agarose beads so far tested, suggesting absence of carbohydrate moieties on the B151-TRF2 molecule. By contrast, pretreatment of spleen cells with trypsin or glycosidase mixture abolished their ability to absorb B151-TRF2 activity. Moreover, B151-TRF2-absorbing ability of spleen cells disappeared by the pretreatment with beta-N-acetylglucosaminidase, which cleaves terminal GlcNAc. The fact that pnitrophenyl (PNP)-GlcNAc specifically inhibited such enzyme activity on target cells indicates that terminal GlcNAc on the B cell surface plays a crucial role in the interaction with B151-TRF2 molecule. Interestingly, it was also found that B151-TRF2 activity was trapped and eluted from GlcNAc-coupled agarose beads. Taken collectively, these results strongly suggest that B cell membrane receptors for B151-TRF2 comprise glycoproteins with a terminal GlcNAc residue(s), and that binding of B151-TRF2 with terminal GlcNAc on the receptor is important for the subsequent activation of B cells.

Acetylglucosamine↗
PubMed1986

Photoaffinity labeling of glyceraldehyde-3-phosphate dehydrogenase by an aryl azide derivative of glucosamine in human erythrocytes.

An aryl azide derivative of glucosamine, N-(4-iodoazidosalicyl)-2-amido-2-deoxy-D-glucopyranose (GlcNAs), was synthesized as a potential photoaffinity label for the facilitative hexose carrier. The derivative inhibited hexose uptake into intact human erythrocytes half-maximally at 3.5 mM and was itself slowly transported into cells. However, photolysis of iodinated GlcNAs with leaky erythrocyte ghosts produced appreciable labeling on gel electrophoresis only of Band 6, which is glyceraldehyde-3-phosphate dehydrogenase. Band 6 photolabeling in leaky ghosts by GlcNAs was: saturable, due mostly to the aryl azide moiety, inhibited by agents with known affinity for the enzyme including sulfhydryl reagents and the enzyme substrate glyceraldehyde-3-phosphate, and not inhibited by the free-radical scavenger p-aminobenzoic acid. Moreover, GlcNAs also inhibited erythrocyte glyceraldehyde-3-phosphate dehydrogenase activity in a dose-dependent fashion in the dark and more potently following irradiation. In resealed ghosts, Band 6 labeling was decreased by D-glucose, reflecting inhibition of carrier-mediated uptake of the agent. GlcNAs appears to be a specific photoaffinity label for erythrocyte glyceraldehyde-3-phosphate dehydrogenase, and therefore potentially useful for studies of enzyme activity, compartmentation, or membrane association.

Affinity Labels↗
PubMed1976

Isolation of a human lymphocyte mitogen from wheat germ with N-acetyl-D-glucosamine specificity.

A lectin, isolated from wheat germ by affinity chromatography on chitin, was mitogenic for purified human peripheral blood lymphocytes. Peak incorporation of 3H-thymidine was observed after incubation of lymphocyte cultures with wheat germ mitogen for 7 to 10 days. When lymphocytes were separated into two fractions based on their ability to form rosettes with unsensitized sheep erythrocytes, the mitogen induced a negligible proliferative response in either fraction. Mixing experiments demonstrated a strong response in the T lymphocyte fraction which required the collaboration, but not proliferation, of cells present in the nonrosetting fraction. Stimulation was specifically abolished by addition of N-acetyl-D-glucosamine at initiation of culture.

Acetylglucosamine↗
PubMed1980

[Glucosamine: its importance for the metabolism of articular cartilage. 2. Studies on articular cartilage].

In healthy individuals there exists a balance between cartilage proteoglycan synthesis and degradation. In arthrotic cartilage this metabolic balance is deteriorated in spite of a sometimes enhanced proteoglycan synthesis, since the catabolic rate exceeds the anabolic rate corresponding to the severity of the disease. The extracellular organic matrix of the cartilage is destroyed. With different experimental models it could be demonstrated, that the non steroidal anti-inflammatory drugs commonly used in the treatment of arthrosis inhibit the synthesis of mucopolysaccharides, intensify the already existing metabolic disorder, prevent a normalization of cartilage composition and thus impair the function of the cartilage. Glucosamine on the other hand increases in a dose-dependent way the ability of cartilage to synthesize both sulfated mucopolysaccharides and protein, thus restoring the catabolic-anabolic balance of the cartilage.

Animals↗
PubMed1983

Effects of human brain cell culture conditions on [14C]glucosamine radioactivity incorporation into gangliosides.

Human glioma cells (12-18) and fetal neural cells (CH II) in culture were exposed for 20 hr to [14C]glucosamine to determine the level and distribution of radiolabel incorporated into gangliosides. Cells of identical passage levels at two stages of growth, preconfluent and confluent, were preincubated for 0 to 60 hr in serum-free medium (SFM). Both higher cell densities and longer incubations in SFM caused a change in the amounts and patterns of radiolabeled gangliosides. Preincubation for 60 hr in SFM caused an increase (P less than 0.05) in the percent of total recovered ganglioside radiolabel in GM1 of CH II cells, from 10.5 to 16.7% in preconfluent cells and from 14.1 to 31.9% in confluent cells. Conversely, the proportion of radiolabel in GM3 and GM2 decreased with longer preincubations in SFM. A similar preincubation of glioma cells caused an increase in the proportion of label into GD1a of both preconfluent and confluent cells (P less than 0.02) from 4 to 11% of the total ganglioside radioactivity. Higher cell densities also resulted in consistently higher percent (of total ganglioside) incorporation into GD1a of 12-18 cells (P less than 0.05) and GM1 of CH II (P less than 0.01). These results show that there is a shift in the incorporation of precursor label into more complex gangliosides under conditions associated with the arrest of cell division. These phenomena may represent a regulatory response of the ganglioside biosynthetic apparatus to changes in extracellular environment and cell contact.

Brain↗