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Differential radiosensitivity in cultured B-16 melanoma cells following interrupted melanogenesis induced by glucosamine.

The relationship between cell pigmentation and radiosensitivity was investigated in a cell model in which melanogenesis was suppressed by a glycosylation inhibitor. It was found that X-irradiation of melanotic B-16 melanoma cells and their amelanotic counterparts, obtained by glucosamine treatment, showed an inverse correlation between radiosensitivity and melanin contents. Since melanogenesis interruption by glucosamine does not affect the DNA repair capacity of nonpigmented cells, it is likely that intracellular melanins play a role in the relative resistance of pigmented cells to X-irradiation.

Animals↗

Evidence-based practice: review of clinical evidence on the efficacy of glucosamine and chondroitin in the treatment of osteoarthritis.

PURPOSE: To evaluate past and current evidence from randomized controlled trials on the efficacy of glucosamine sulfate (GS), glucosamine hydrochloride (GH), and chondroitin sulfate (CS) for the treatment of osteoarthritis (OA). DATA SOURCES: An extensive review of four meta-analyses and a review of the findings of the recently published Glucosamine/Chondroitin Arthritis Intervention Trial (GAIT) funded by the National Institutes of Health. FINDINGS: Review of previous studies on the efficacy of GS, GH, and CS in the treatment of OA showed inconclusive results because of weak research design. The GAIT attempted to provide clarity on the use of GH and CS in treating knee pain from OA by using a rigorous research design to elicit cause and effect. The GAIT results showed that GH and CS were not effective in reducing knee pain in the study group overall; however, these may be effective in combination for patients with moderate-to-severe knee pain. IMPLICATIONS FOR PRACTICE: There is now clinical evidence indicating that recommending GS, GH, and CS for the treatment of mild knee pain from OA is ineffective. Further research needs to be done to identify specific characteristics in patients that results in a positive response. Until the findings of the GAIT undergo further peer review, the results of the research needs to be interpreted with caution.

Chondroitin↗

Inhibition of articular cartilage degradation by glucosamine-HCl and chondroitin sulphate.

Glucosamine and chondroitin sulphate in many animal and human trials has improved joint health. In vitro studies are beginning to clarify their mode of action. The objective of this research was to: 1) determine at what concentrations glucosamine-HCl (GLN) and/or chondroitin sulphate (CS) would inhibit the cytokine-induced catabolic response in equine articular cartilage explants and 2) to determine if a combination of the 2 was more effective at inhibiting the catabolic response than the individual compounds. Articular cartilage was obtained from carpal joints of horses (age 1-4 years). Cartilage discs (3.5 mm) were biopsied and cultured. Explants were incubated with lipopolysaccharide (LPS) in the presence of varying concentrations of GLN, CS, or both. Control treatments included explants with no LPS and LPS without GLN or CS. Media were analysed for nitric oxide (NO), prostaglandin E2 (PGE2) and keratan sulphate. Cartilage was extracted for analysis of metalloproteinases (MMP). Four experiments were conducted. In all experiments, GLN at concentrations as low as 1 mg/ml decreased NO production relative to LPS stimulated cartilage without GLN over the 4 day period. In general, CS at either 0.25 or 0.5 mg/ml did not inhibit NO production. The addition of CS to GLN containing media did not further inhibit NO production. GLN at concentrations as low as 0.5 mg/ml decreased PGE2 production, whereas CS did not effect on PGE2. The combination of GLN/CS decreased MMP-9 gelatinolytic activity but had no effect on MMP-2 activity. The combination in 2 experiments tended to decrease MMP-13 protein concentrations and decreased keratan sulphate levels in media. Overall, the combination of GLN (1 mg/ml) and CS (0.25 mg/ml) inhibited the synthesis of several mediators of cartilage degradation. These results further support the effort to understand the role of GLN and CS in preserving articular cartilage in athletic horses.

Animals↗

Direct incorporation of glucosamine and N-acetylglucosamine into exopolymers by Gluconacetobacter xylinus (=Acetobacter xylinum) ATCC 10245: production of chitosan-cellulose and chitin-cellulose exopolymers.

Gluconacetobacter xylinus (=Acetobacter xylinum) ATCC 10245 incorporated 2-amino-2-deoxy-D-glucose (glucosamine) and 2-acetamido-2-deoxy-D-glucose (N-acetylglucosamine), but not 3-O-methyl-D-glucose or 2-deoxy-D-glucose into exopolymers. Incorporation was confirmed by gas chromatography with and without mass spectrometry, Fourier transform infrared, and 1H nuclear magnetic resonance. The average molar percentage of glucosamine and N-acetylglucosamine in the exopolymers was about 18%.

Acetylglucosamine↗

Low endotoxic activities of synthetic Salmonella-type lipid A with an additional acyloxyacyl group on the 2-amino group of beta (1-6) glucosamine disaccharide 1,4'-bisphosphate.

A synthetic lipid A (Salmonella type, compound 516), beta (1-6)-linked D-glucosamine disaccharide 1,4'-bisphosphate, with three acyloxyacyl groups and one hydroxyacyl group, i.e., (R)-3-hexadecanoyloxytetradecanoyl, (R)-3-hydroxytetradecanoyl, (R)-3-dodecanoyloxytetradecanoyl, and (R)-3-tetradecanoyloxytetradecanoyl groups at the 2-amino, 3-hydroxyl, 2'-amino, and 3'-hydroxyl groups, respectively, was less biologically active than the synthetic Escherichia coli-type lipid A (compound 506), which has only two acyloxyacyl groups at the 2' and 3' positions and is substituted with a (R)-3-hydroxytetradecanoyl group at the 2-amino group. Compound 516 exhibited considerably weaker pyrogenic and leukopenic activity than compound 506, and it scarcely prepared rabbit skin for the Shwartzman reaction and lacked lethal toxicity on chicken embryos, although its lethal toxicity in galactosamine-loaded mice was as strong as that of compound 506. Compound 516 was also less active than compound 506 or natural E. coli lipid A (from Restrain F515) in other biological test systems, such as the Limulus test, stimulation of macrophages and lymphocytes, and interferon-inducing activity but not for interleukin-1 induction or complement activation. This observation suggests that there is an optimal number of acyloxyacyl groups on the glucosamine backbone for producing the biological activities of lipid A, especially the endotoxic activities. The 4'-monophosphate analog (compound 514) of compound 516 in general had significantly weaker activity than compound 516 in the above assays, most probably because of its greater hydrophobicity and consequently lower solubility in assay systems. Bacterial R595 lipid A derived from S. minnesota Re-mutant, which is a mixture of compounds 516 and 506, their 4'-monophosphate analogs and other compounds, exerted intermediate degrees of activity between compounds 506 and 516 in the various test systems employed.

Adjuvants, Immunologic↗

Developmental control of glucosamine and galactosamine levels during conidation in Neurospora crassa.

The glucosamine and galactosamine content of mycelia was measured in cultures of Neurospora crassa grown on the surface of dialysis membranes. The glucosamine content was relatively constant throughout the different regions of the mycelial mat. The galactosamine content, however, was always lower in the growing-front region of the mycelial mat than in the older regions. At most, only low levels of galactosamine were necessary for the formation of hyphae at the growing front of a mycelial mat. Thus, galactosamine-containing polymers cannot be a major shape-determining component of the cell walls of these hyphae in Neurospora. The effect of conidiation on the amino sugar content was determined by using the bd (band) strain of N. crassa. When grown on the surface of dialysis membranes, this strain rhythmically produced regions of conidiating and non-conidiating growth. With this strain, it was concluded that conidiation did not affect the amino sugar levels. Since conidia that contained only very low levels of galactosamine were produced from regions of the mycelial mat that contained much higher levels of this amino sugar, there must be some mechanism of spatial differentiation that prevented the accumulation of galactosamine-containing polymers in conidia.

Autoanalysis↗

Bacillus cereus autolytic endoglucosaminidase active on cell wall peptidoglycan with N-unsubstituted glucosamine residues.

An autolytic glycosidase from a lysozyme-resistant strain of Bacillus cereus capable of cleaving the glycosidic linkages of N-unsubstituted glucosamine in the cell wall peptidoglycan was studied. This glycosidase activity, together with N-acetylmuramyl-L-alanine amidase activity, was found in an autolytic enzyme preparation obtained from the 20,000 x g precipitate fraction by means of autolysis followed by ammonium sulfate fractionation. The major saccharide fragments resulting from digestion of the untreated, non-N-acetylated, cell wall peptidoglycan of B. cereus with the autolytic enzyme preparation were identified as N-acetylmuramyl-glucosamine and its dimer. The peptidoglycan N-acetylated with acetic anhydride could also be digested with the same enzyme preparation, giving N-acetylmuramyl-N-acetylglucosamine and its dimer as the major saccharide fragments.

Bacillus cereus↗

Transport and incorporation of N-acetyl-D-glucosamine in Bacillus subtilis.

Bacillus subtilis 168 has been found to possess a high-affinity transport system for N-acetyl-D-glucosamine (GlcNAC). The Km for uptake was approximately 3.7 microM GlcNAc, regardless of the nutritional background of the cells. Apparent increases in Vmax were noted when the bacteria were grown in the presence of GlcNAc. The uptake of GlcNAc by B. subtilis was highly stereoselective; D-glucose, D-glucosamine, N-acetyl-D-galactosamine, D-galactose, D-mannose, and N-acetylmuramic acid did not inhibit GlcNAc uptake. In contrast, glycerol was an effective inhibitor of [3H]GlcNAc transport and incorporation. Partial inhibition of GlcNAc uptake was observed with azide, fluoride, and cyanide anions, carbonyl cyanide-m-chlorophenyl hydrazone, methyltriphenylphosphonium bromide, N,N'-dicyclohexylcarbodiimide, gramicidin, valinomycin, monensin, and nigericin. Two anions, arsenite and iodoacetate, were potent inhibitors of the uptake of GlcNAc in B. subtilis. Results from paper chromatography showed that there was no intracellular pool of free GlcNAc and that the acetylamino sugar was probably phosphorylated during transport. A modification of the Park-Hancock cell fractionation scheme indicated that cells grown on glycerol or D-glucose incorporated [3H]GlcNAc primarily into the cell wall fraction. When GlcNAc was used as the sole carbon source, label could be demonstrated in fractions susceptible to protease and nuclease, as well as lysozyme, showing that the N-acetylamino sugar was utilized in macromolecular synthesis and energy metabolism.

Acetylglucosamine↗

Why does Escherichia coli grow more slowly on glucosamine than on N-acetylglucosamine? Effects of enzyme levels and allosteric activation of GlcN6P deaminase (NagB) on growth rates.

Wild-type Escherichia coli grows more slowly on glucosamine (GlcN) than on N-acetylglucosamine (GlcNAc) as a sole source of carbon. Both sugars are transported by the phosphotransferase system, and their 6-phospho derivatives are produced. The subsequent catabolism of the sugars requires the allosteric enzyme glucosamine-6-phosphate (GlcN6P) deaminase, which is encoded by nagB, and degradation of GlcNAc also requires the nagA-encoded enzyme, N-acetylglucosamine-6-phosphate (GlcNAc6P) deacetylase. We investigated various factors which could affect growth on GlcN and GlcNAc, including the rate of GlcN uptake, the level of induction of the nag operon, and differential allosteric activation of GlcN6P deaminase. We found that for strains carrying a wild-type deaminase (nagB) gene, increasing the level of the NagB protein or the rate of GlcN uptake increased the growth rate, which showed that both enzyme induction and sugar transport were limiting. A set of point mutations in nagB that are known to affect the allosteric behavior of GlcN6P deaminase in vitro were transferred to the nagB gene on the Escherichia coli chromosome, and their effects on the growth rates were measured. Mutants in which the substrate-induced positive cooperativity of NagB was reduced or abolished grew even more slowly on GlcN than on GlcNAc or did not grow at all on GlcN. Increasing the amount of the deaminase by using a nagC or nagA mutation to derepress the nag operon improved growth. For some mutants, a nagA mutation, which caused the accumulation of the allosteric activator GlcNAc6P and permitted allosteric activation, had a stronger effect than nagC. The effects of the mutations on growth in vivo are discussed in light of their in vitro kinetics.

Acetylglucosamine↗

Selective inhibition of Newcastle disease virus-induced glycoprotein synthesis by D-glucosamine hydrochloride.

d-Glucosamine selectively affected the synthesis of virus-induced glycoproteins in Newcastle disease virus-infected chick fibroblasts, but had no effect upon post-translational cleavage of the glycoprotein precursor for one of the two major glycoproteins of the mature virion. In response to glucosamine, at least one of the two virus-induced glycoproteins is formed in reduced quantity and the second is either not formed or has an electrophoretic mobility identical to that of another virus-induced protein.

Animals↗

Effects of 2-deoxyglucose, glucosamine, and mannose on cell fusion and the glycoproteins of herpes simplex virus.

2-Deoxyglucose and glucosamine were found to inhibit cell fusion caused by a syncytial mutant of herpes simplex virus and to inhibit the glycosylation of viral glycoproteins in the infected cells. The inhibition of fusion and the inhibition of glycosylation caused by 2-deoxyglucose were substantially prevented when mannose was also present during infection. When glycosylation was inhibited, three new bands were found in major glycoprotein region on sodium dodecyl sulfate-polyacrylamide gels. These bands may be precursors to the normal glycoproteins. The correlation between fusion and glycosylation in the presence of 2-deoxyglucose, glucosamine, and mannose suggests that the cells cannot fuse if their glycoproteins have a considerably reduced carbohydrate content.

Cell Fusion↗

Is glucosamine worth taking for osteoarthritis?

The food supplement glucosamine has been claimed to modify progression of osteoarthritis and is being extensively marketed as a treatment for patients with the condition. In fact, the UK annual market for glucosamine is now estimated to be over 10 million Pounds. Here, we examine whether the supplement has a place in the management of osteoarthritis.

Antirheumatic Agents↗

Glucosamine protects neonatal cardiomyocytes from ischemia-reperfusion injury via increased protein-associated O-GlcNAc.

Increased levels of protein O-linked N-acetylglucosamine (O-GlcNAc) have been shown to increase cell survival following stress. Therefore, the goal of this study was to determine whether in isolated neonatal rat ventricular myocytes (NRVMs) an increase in protein O-GlcNAcylation resulted in improved survival and viability following ischemia-reperfusion (I/R). NRVMs were exposed to 4 h of ischemia and 16 h of reperfusion, and cell viability, necrosis, apoptosis, and O-GlcNAc levels were assessed. Treatment of cells with glucosamine, hyperglycemia, or O-(2-acetamido-2-deoxy-D-glucopyranosylidene)-amino-N-phenylcarbamate(PUGNAc), an inhibitor of O-GlcNAcase, significantly increased O-GlcNAc levels and improved cell viability, as well as reducing both necrosis and apoptosis compared with untreated cells following I/R. Alloxan, an inhibitor of O-GlcNAc transferase, markedly reduced O-GlcNAc levels and exacerbated I/R injury. The improved survival with hyperglycemia was attenuated by azaserine, which inhibits glucose metabolism via the hexosamine biosynthesis pathway. Reperfusion in the absence of glucose reduced O-GlcNAc levels on reperfusion compared with normal glucose conditions and decreased cell viability. O-GlcNAc levels significantly correlated with cell viability during reperfusion. The effects of glucosamine and PUGNAc on cellular viability were associated with reduced calcineurin activation as measured by translocation of nuclear factor of activated T cells, suggesting that increased O-GlcNAc levels may attenuate I/R induced increase in cytosolic Ca(2+). These data support the concept that activation of metabolic pathways leading to an increase in O-GlcNAc levels is an endogenous stress-activated response and that augmentation of this response improves cell survival. Thus strategies designed to activate these pathways may represent novel interventions for inducing cardioprotection.

Acetylglucosamine↗

2-Deoxyglucose: inhibition of parasitemia and of glucosamine incorporation into glycosylated macromolecules, in malarial parasites (Plasmodium falciparum).

Cultured malarial parasites were incubated with various doses of 2-deoxyglucose (0.5, 1.0, 5.0, and 10.0 mM) for 48 h. Effects of 2-deoxyglucose on parasite survival were determined by counting the number of parasites/10,000 erythrocytes. Effects of 2-deoxyglucose on synthesis of membrane proteins and glycosylated macromolecules were monitored by metabolic labelling using radioactive isoleucine and glucosamine, respectively. 2-deoxyglucose significantly reduced parasite survival and synthesis of glycosylated macromolecules. Further incorporation of radioactive isoleucine was reduced at dose levels of 1.0, 5.0 and 10.0 mM. Inhibition of parasite survival was related closely to inhibition of incorporation of radioactive glucosamine into macromolecules. These results suggest that the antimalarial action of 2-deoxyglucose involves reduced synthesis of membrane glycosylated macromolecules by cultured parasites.

Antimalarials↗

Role of the glucosamine pathway in fat-induced insulin resistance.

To examine whether the hexosamine biosynthetic pathway might play a role in fat-induced insulin resistance, we monitored the effects of prolonged elevations in FFA availability both on skeletal muscle levels of UDP-N-acetyl-hexosamines and on peripheral glucose disposal during 7-h euglycemic-hyperinsulinemic (approximately 500 microU/ml) clamp studies. When the insulin-induced decrease in the plasma FFA levels (to approximately 0.3 mM) was prevented by infusion of a lipid emulsion in 15 conscious rats (plasma FFA approximately 1.4 mM), glucose uptake (5-7 h = 32.5+/-1.7 vs 0-2 h = 45.2+/-2.8 mg/kg per min; P < 0.01) and glycogen synthesis (P < 0.01) were markedly decreased. During lipid infusion, muscle UDP-N-acetyl-glucosamine (UDP-GlcNAc) increased by twofold (to 53.4+/-1.1 at 3 h and to 55.5+/-1.1 nmol/gram at 7 h vs 20.4+/-1.7 at 0 h, P < 0.01) while glucose-6-phosphate (Glc-6-P) levels were increased at 3 h (475+/-49 nmol/gram) and decreased at 7 h (133+/-7 vs 337+/-28 nmol/gram at 0 h, P < 0.01). To discern whether such an increase in the skeletal muscle UDP-GlcNAc concentration could account for the development of insulin resistance, we generated similar increases in muscle UDP-GlcNAc using three alternate experimental approaches. Euglycemic clamps were performed after prolonged hyperglycemia (18 mM, n = 10), or increased availability of either glucosamine (3 micromol/kg per min; n = 10) or uridine (30 micromol/kg per min; n = 4). These conditions all resulted in very similar increases in the skeletal muscle UDP-GlcNAc (to approximately 55 nmol/gram) and markedly impaired glucose uptake and glycogen synthesis. Thus, fat-induced insulin resistance is associated with: (a) decreased skeletal muscle Glc-6-P levels indicating defective transport/phosphorylation of glucose; (b) marked accumulation of the endproducts of the hexosamine biosynthetic pathway preceding the onset of insulin resistance. Most important, the same degree of insulin resistance can be reproduced in the absence of increased FFA availability by a similar increase in skeletal muscle UDP-N-acetyl-hexosamines. In conclusion, our results support the hypothesis that increased FFA availability induces skeletal muscle insulin resistance by increasing the flux of fructose-6-phosphate into the hexosamine pathway.

Animals↗

Carbenoxolone and incorporation of (3H) glucosamine into gastric mucosa.

The effect of carbenoxolone on incorporation of the labelled sugar, (3H) glucosamine, into rat gastric mucosa was examined. Rats were treated with either 25 mg/kg, or 50 mg/kg or 75 mg/kg carbenoxolone for 10 days. The rats were then killed and the uptake of (3H) glucosamine by gastric mucosal scrapings measured. There was no statistically significant difference in uptake between treated and untreated scrapings. The results do not confirm earlier findings of other investigators which suggested that carbenoxolone promoted gastric ulcer healing by stimulating specific glycosyl transferases to produce a modified mucus.

Animals↗

FSH stimulation of 3H-glucosamine-incorporation into proteoglycans by porcine granulosa cells in vitro.

Porcine granulosa cells from small follicles were incubated in the presence of 1 muCi/ml 3H-glucosamine and various hormones. Proteoglycans were digested with protease, and the mucopolysaccharides (MPS) were recovered. Most of the labeled MPS was found in secretory products. Maximum incorporation of 3H-glucosamine into MPS occurred after incubation with FSH for 8--16 h. Cell concentrations of 0.5--4.0 x 10(6)/ml proved to be ample. Highly purified porcine or human FSH gave consistent, significant stimulation by doses in the order of 100 pg/ml. Linear log-dose response curves occurred from 0.1 to 10.0 ng/ml, and maximal stimulation at 10 ng/ml was 22-fold above control. Preparations of hCG, hTSH and NIH-LH-S18 were not effective. Incubations with 1--10 mM dibutyryl cyclic AMP significantly increased incorporation into MPS, suggesting that effects of FSH may be mediated by cyclic AMP.

Animals↗