Characterization and role of fucose mutarotase in mammalian cells

Park, Dongkyu; Ryu, Kyoung‐Seok; Choi, Daeseon; Kwak, Jaechan; Park, Chankyu

doi:10.1093/glycob/cwm066

Cited by 22 publications

(26 citation statements)

References 26 publications

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“…Although the anomers spontaneously interconvert slowly in aqueous solution, an enzyme (mutarotase or aldose-1-epimerase) is responsible for interconverting the two optical varieties in monosaccharide forms in vivo (6,21). Mutarotases are present throughout the prokaryotic and eukaryotic phyla (6,31,34,37). Mutarotase syntheses are also induced in response to specific signals.…”

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confidence: 99%

Induction of the Galactose Enzymes in Escherichia coli Is Independent of the C-1-Hydroxyl Optical Configuration of the Inducer d -Galactose

Lee

Lewis

2008

J Bacteriol

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The two optical forms of aldohexose galactose differing at the C-1 position, ␣-D-galactose and ␤-D-galactose, are widespread in nature. The two anomers also occur in di-and polysaccharides, as well as in glycoconjugates. The anomeric form of D-galactose, when present in complex carbohydrates, e.g., cell wall, glycoproteins, and glycolipids, is specific. Their interconversion occurs as monomers and is effected by the enzyme mutarotase (aldose-1-epimerase). Mutarotase and other D-galactose-metabolizing enzymes are coded by genes that constitute an operon in Escherichia coli. The operon is repressed by the repressor GalR and induced by D-galactose. Since, depending on the carbon source during growth, the cell can make only one of the two anomers of D-galactose, the cell must also convert one anomer to the other for use in specific biosynthetic pathways. Thus, it is imperative that induction of the gal operon, specifically the mutarotase, be achievable by either anomer of D-galactose. Here we report in vivo and in vitro experiments showing that both ␣-D-galactose and ␤-D-galactose are capable of inducing transcription of the gal operon with equal efficiency and kinetics. Whereas all substitutions at the C-1 position in the ␣ configuration inactivate the induction capacity of the sugar, the effect of substitutions in the ␤ configuration varies depending upon the nature of the substitution; methyl and phenyl derivatives induce weakly, but the glucosyl derivative does not.D-Galactose, also known as cerebrose, is a natural aldohexose which is ubiquitous in bacteria, plants, and animals, including human brains (28). It occurs also as part of more complex carbohydrates, e.g., oligo-and polysaccharides, glycoproteins, and glycolipids, and as components of bacterial cell walls. DGalactose has two anomeric forms, ␣-D-galactopyranose and ␤-D-galactopyranose ( Fig. 1) (36). Although the anomers spontaneously interconvert slowly in aqueous solution, an enzyme (mutarotase or aldose-1-epimerase) is responsible for interconverting the two optical varieties in monosaccharide forms in vivo (6,21). Mutarotases are present throughout the prokaryotic and eukaryotic phyla (6,31,34,37). Mutarotase syntheses are also induced in response to specific signals. For example, galactose mutarotase synthesis is induced by retinoic acid in human myeloid cells (30). In the bacterium Escherichia coli, enzymes of D-galactose metabolism (15,20), including the mutarotase (6), are encoded in an operon which is induced by D-galactose. It has been suggested previously that only ␤-Dgalactose is the inducer of the gal operon (7). Since D-galactose moieties in complex carbohydrates are anomerically specific, ␣ or ␤, we hypothesize that the mutarotase enzyme, which interconverts the ␣ and ␤ anomers, must be induced for the interconversion when either one of the two anomers is present in the cell, say, by hydrolysis of D-lactose, which generates ␤-Dgalactose, or of D-melibiose, which generates ␣-D-galactose. In this study, we showed by both in vivo and in vitr...

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confidence: 99%

Induction of the Galactose Enzymes in Escherichia coli Is Independent of the C-1-Hydroxyl Optical Configuration of the Inducer d -Galactose

Lee

Lewis

2008

J Bacteriol

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“…The collected saliva was centrifuged for 10 minutes at (1000 g) to obtain a clear supernatant fluid 15 , then each sample was divided into three portions and they were stored at -20 0 C, until analysis. Methods: 1-Salivary TP was determined by Biuret method described by Gornall et al 19,20 , using a special kit.…”

Section: Saliva Collectionmentioning

confidence: 99%

“…This increase in salivary fucose parameters in periodontitis might represent the breakdown of plasma and tissue glycoproteins which may occur as a result of inflammation 27 . There is indirect evidence to indicate that, increased salivary glycoprotein level is offset by increased fucosidase activity that causes the breakdown of saliva and tissue glycoproteins 15 . Thus periodontitis may cause an increase in fucosidase activity.…”

Section: Figurementioning

confidence: 99%

“…It is found on various cell membranes and play an important role in cell-cell adhesion 14 . Studies have been shown that, serum and salivary fucose and its related parameters are important in the detection of oral disease (gingivitis, periodontitis and oral cancer) 15,16 . The present work was designed to evaluate the salivary fucose and its related parameters in patients with periodontitis.…”

Section: Introductionmentioning

confidence: 99%

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Evaluation of salivary α-L-Fucose and its related parameters in periodontitis

Wsoo

Ahmed

2013

ZJMS

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“…Fucose is naturally found in D-and L-forms.The L-form is the only common form of the sugar , while the D-form is a synthetic galactose analogue (6) .The L-form is found in mammalian tissues and fluids, while D-form is identified in plants. Purified L-Fucose is white powder and it melts at 153-155 ċ o , and L-fucose exist in two different forms α-L-fucose (29.5%)and ß-L-fucose (70.5%) (7) . Fucose is a powerful immune modulator .It is distributed in macrophages, playing a vital role in immune function.…”

Section: Introductionmentioning

confidence: 99%

The Histopathological Effect of Local Injection of Fucose on Bone Fracture :An Experimental Study on Rabbits

2015

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Aim:To evaluate the effect of sulcular injection of 50μl of 150mM fucose on rabbits with bone trauma. Background: α-L-Fucose is a methyl pentose sugar similar to L-galactose except for the loss of alcohol group on carbon number 6.It is found in human serum bound to proteins by covalent bonding and it is a member of a large group of compounds known as covalent bond membranes . Materials and Methods: The present study was carried out on 65 male rabbits, bone trauma was introduced into the mid-labial areas of facial plate of the alveolar bone of lower right central incisor for all rabbits . The rabbits had been left for 7 days after induction of bone trauma, then 5 rabbits were sacrificed and considered as a base line traumatic group . The remaining 60 rabbits were divided randomly into two 2 main groups, first group consist of 30 rabbits and were injected locally with 50μl of 150mM fucose solution into the bottom of gingival sulcus at the mid-labial area of lower right central incisor and were considered as fucose injected group and were divided randomly into six subgroups(each subgroup consist of 5 rabbits) , then periodontal tissue biopsy was collected from injected group at time intervals of 1, 3 ,7 ,14, , 21 , and 28 days after fucose injection , while the second group consist of 30 rabbits with bone trauma only and were not received any fucose injection and considered as non injected group and were divided randomly into six subgroups (each subgroup consist of 5 rabbits), sacrificed at time intervals of 8,10,14,21,28 ,and 35 days after induction of bone fracture. Results:The results showed that fucose injection enhanced bone regeneration and healing of traumatic bone in short duration of time, 1 day after sulucular injection of fucose (8 days after induction of bone fracture). Conclusion: α-L-Fucose can be used as a bone stimulating agent which stimulate and accelerate new bone formation, so fucose can be used in the treatment of alveolar bone defect in periodontitis patient KEY WORDS:α-L-Fucose, periodontal biopsy , sulcular injection .

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Characterization and role of fucose mutarotase in mammalian cells

Cited by 22 publications

References 26 publications

Induction of the Galactose Enzymes in Escherichia coli Is Independent of the C-1-Hydroxyl Optical Configuration of the Inducer d -Galactose

Induction of the Galactose Enzymes in Escherichia coli Is Independent of the C-1-Hydroxyl Optical Configuration of the Inducer d -Galactose

Evaluation of salivary α-L-Fucose and its related parameters in periodontitis

The Histopathological Effect of Local Injection of Fucose on Bone Fracture :An Experimental Study on Rabbits

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