Novel products in hyaluronan digested by bovine testicular hyaluronidase

Chen, Fengchao; Kakizaki, Ikuko; Yamaguchi, Masanori; Kojima, Kaoru; Takagaki, Keiichi; Endo, Masahiko

doi:10.1007/s10719-008-9200-2

Cited by 19 publications

(8 citation statements)

References 24 publications

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“…2), their different pH dependence (differ ent shape and position of the curves on Fig 2a and 2b, respectively), multistage formation of various glyca tion products especially after prolonged incubation play evident roles in this process [9][10][11]15]. In addi tion, bovine testicular HU preparation may be con taminated with N deacetylase, an accompanying enzyme that catalyzed conversion of N acetylglu cosamine at the reducing end into glucosamine [22]. Indeed, inhibition of alkaline phosphatase activity was achieved by the action of glucosamine and galac tosamine [23].…”

Section: Resultsmentioning

confidence: 99%

Do electrostatic interactions determine glycation of hyaluronidase derivatives with N-acetylhexosamines?

Турашев

Tischenko

Maksimenko

2012

Biochem. Moscow Suppl. Ser. B

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Using N acetylglucosamine and N acetylgalactosamine as model agents for glycation of native hyaluronidase and its chondroitin sulfate modified form it has been shown that the modified enzyme exhib ited higher inactivation than the native enzyme, while heparin caused similar inhibition of both forms. Such effect could be attributed to the development of electrostatic interactions as the modified hyaluronidase had altered surface electrostatic potential after chondroitin sulfate binding. However, variations in ionic strength of the medium containing enzyme derivatives have shown that their endoglycosidase activity changed in a similar manner and the effect on glycation represents a multifactor process. N acetylhexosamines are natural labels of endothelial glycocalyx degradation products. Interaction of the hyaluronidase forms with charged hyaluronan fragments revealed significantly higher inactivation of the modified enzyme compared with the native enzyme. The glycation pattern observed in this study was opposite to that observed with mono and di saccharides. Thus, it appears that the investigated hyaluronidase derivatives represent an informative enzy matic test in vivo for determination of the dominant type of glycation agents in blood circulation and their origin.

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Section: Resultsmentioning

confidence: 99%

Do electrostatic interactions determine glycation of hyaluronidase derivatives with N-acetylhexosamines?

Турашев

Tischenko

Maksimenko

2012

Biochem. Moscow Suppl. Ser. B

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“…The second class of useful catalysts is a natural HA and CS degrading enzyme, testicular hyaluronidase (HAase; EC 3.2.1.35). This enzyme can be used in the "reverse" direction to make polymers either by transglycosylation (a disaccharide unit is added to the chain terminus rather than the hydrolysis of the chain by a water molecule), swapping domains of existing GAGs (Chen et al 2009;Kakizaki et al 2012;Table II, reaction VII) or by the polymerization of disaccharide oxazoline transition state intermediates (Ochiai et al 2007; Figure 3; Table II, reaction IV). Unfortunately, there is no known comparable enzyme with the ability to make heparosan or HS by either of these approaches.…”

Section: Gag Chemoenzymatic Synthesismentioning

confidence: 99%

Chemoenzymatic synthesis of glycosaminoglycans: Re-creating, re-modeling and re-designing nature's longest or most complex carbohydrate chains

2013

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Glycosaminoglycans (GAGs) are complex polysaccharides composed of hexosamine-containing disaccharide repeating units. The three most studied classes of GAGs, heparin/heparan sulfate, hyaluronan and chondroitin/dermatan sulfate, are essential macromolecules. GAGs isolated from animal and microbial sources have been utilized therapeutically, but naturally occurring GAGs are extremely heterogeneous limiting further development of these agents. These molecules pose difficult targets to construct by classical organic syntheses due to the long chain lengths and complex patterns of modification by sulfation and epimerization. Chemoenzymatic synthesis, a process that employs exquisite enzyme catalysts and various defined precursors (e.g. uridine 5'-diphosphosphate-sugar donors, sulfate donors, acceptors and oxazoline precursors), promises to deliver homogeneous GAGs. This review covers both theoretical and practical issues of GAG oligosaccharide and polysaccharide preparation as single molecular entities and in library formats. Even at this early stage of technology development, nearly monodisperse GAGs can be made with either natural or artificial structures.

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“…In addition, the bovine testicular HU preparation used might contain some contaminating enzyme-N-deacetylase that could convert the near-reducing terminus N-acetylglucosamine ( Fig. 3b) into glucosamine [37]. These saccharides were reported to inhibit alkaline phosphatase [38].…”

Section: Biochemical Test Of Glycocalyxmentioning

confidence: 99%

Hyaluronidase Proof for Endothelial Glycocalyx as Partaker of Microcirculation Disturbances

Maksimenko¹,

Турашев²,

Fedorovich³

et al. 2013

JLS

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Covalent modification of bovine testicular hyaluronidase with chondroitin sulphate led to changes in the pattern of glycation of native and modified enzyme in its reaction with neutral saccharides and N-acetylhexosamines. Thus, mono-and di-saccharides inactivated the native hyaluronidase to a greater extent than the chondroitin sulfate-modified enzyme. N-acetylhexosamine, on the opposite, inactivated the modified hyaluronidase to a greater extent than the native one. These properties made it possible to use native and modified hyaluronidase as an informative research system for in vivo measurement of the predominant type of saccharide agents in the circulation. The proposed approach was experimentally substantiated by obtained results of the study on these interactions of hyaluronidase derivatives with hyaluronan fragments and their mixture. In a model of post-ischemic perfusion of the rat limb, the effect of hyaluronidase derivatives and their components on restoration of the microcirculation were tracked using laser Doppler flowmetry. Native hyaluronidase accelerated the restoration of initial level of microcirculation, but modified enzyme was markedly inhibited by glycocalyx degradation products. N-acetylhexosamine was positioned at the reducing terminal of these products as a natural label for these glycocalyx fragments. These and other data obtained under various experimental conditions supported the participation of endothelial glycocalyx in microcirculation disturbances.

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Novel products in hyaluronan digested by bovine testicular hyaluronidase

Cited by 19 publications

References 24 publications

Do electrostatic interactions determine glycation of hyaluronidase derivatives with N-acetylhexosamines?

Do electrostatic interactions determine glycation of hyaluronidase derivatives with N-acetylhexosamines?

Chemoenzymatic synthesis of glycosaminoglycans: Re-creating, re-modeling and re-designing nature's longest or most complex carbohydrate chains

Hyaluronidase Proof for Endothelial Glycocalyx as Partaker of Microcirculation Disturbances

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