2017
DOI: 10.3892/etm.2017.4140
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Effect of N-acetylglucosamine administration on cartilage metabolism and safety in healthy subjects without symptoms of arthritis: A case report

Abstract: Abstract. N-acetylglucosamine (GlcNAc) is a widely accepted treatment for osteoarthritis (OA); however, its effect on healthy individuals is poorly understood. To evaluate the effect of GlcNAc administration on healthy subjects that do not exhibit symptoms of arthritis, the present randomized, double-blind, placebo-controlled study was performed. In the present study, 68 male and female Japanese participants, without symptomatic and radiographic evidence of OA, were enrolled and randomly allocated to receive p… Show more

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Cited by 17 publications
(12 citation statements)
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“…[85] Cleavage of ER degradationenhancing alpha-mannosidase-like protein 2 (EDEM2) [86] may disrupt host ERAD of viral glycoproteins [87] or redirect viral glycoproteins away from the cell membrane for internal budding as in SINV-infected mosquito cells. [88,89] Cleavage of phosphoacetylglucosamine mutase (PAGM) may contribute to disruption of glycosaminoglycan polymers in cartilage and contribute to arthritic symptoms, [90] however N-acetylglucosamine (GlcNAc) supplementation sometimes used to treat osteoarthritis (OA) may be counterproductive given (1) it makes up some alphavirus glycans, [91] (2) it promotes replication of many other viruses in vitro and in vivo, [92] and (3) O-linked GlcNAc glycosylation of p65 aggravates TNF-α-mediated inflammation in rheumatoid arthritis (RA). [93] Other predicted cleavages involved in protein degradation include the SUMO-specific E1 enzyme SAE1, the E2 enzyme UBE2Q1, the E3 enzyme UBR4, ubiquitin-1, and tripeptidyl peptidase 2 (TPP2).…”
Section: Discussionmentioning
confidence: 99%
“…[85] Cleavage of ER degradationenhancing alpha-mannosidase-like protein 2 (EDEM2) [86] may disrupt host ERAD of viral glycoproteins [87] or redirect viral glycoproteins away from the cell membrane for internal budding as in SINV-infected mosquito cells. [88,89] Cleavage of phosphoacetylglucosamine mutase (PAGM) may contribute to disruption of glycosaminoglycan polymers in cartilage and contribute to arthritic symptoms, [90] however N-acetylglucosamine (GlcNAc) supplementation sometimes used to treat osteoarthritis (OA) may be counterproductive given (1) it makes up some alphavirus glycans, [91] (2) it promotes replication of many other viruses in vitro and in vivo, [92] and (3) O-linked GlcNAc glycosylation of p65 aggravates TNF-α-mediated inflammation in rheumatoid arthritis (RA). [93] Other predicted cleavages involved in protein degradation include the SUMO-specific E1 enzyme SAE1, the E2 enzyme UBE2Q1, the E3 enzyme UBR4, ubiquitin-1, and tripeptidyl peptidase 2 (TPP2).…”
Section: Discussionmentioning
confidence: 99%
“…Rice syrup was prepared using rice, which is the raw material of rice-koji, and a saccharifying enzyme that has the same composition as koji amazake (Table 1). GlcNAc has been reported to improve cartilage metabolism via the intake of 500 and 1000 mg/day [41]. However, GlcNAc in koji amazake has a lower content than these effect sizes, as mentioned in the section on skin barrier function.…”
Section: Other Functionalitymentioning
confidence: 99%
“…GlcNAc and GlcN are known to exhibit beneficial pharmacological effects in treatment of osteoarthritis (Kubomura et al, 2017). The therapeutic potential of GlcNAc is mainly attributed to its anti-inflammatory and chondroprotective effects (Dalirfardouei et al, 2016).…”
Section: Camp Regulation and Ros Were Not Involved In Glcnac Re-sensimentioning
confidence: 99%