Lysosomal localization of Japanese medaka ( Oryzias latipes ) Neu1 sialidase and its highly conserved enzymatic profiles with human

Ryuzono, Sena; Takase, Ryo; Oishi, Kazuki; Ikeda, Asami; Chigwechokha, Petros Kingstone; Funahashi, Aki; Komatsu, Masaharu; Miyagi, Taeko; Shiozaki, Kazuhiro

doi:10.1016/j.gene.2015.09.028

Cited by 17 publications

(6 citation statements)

References 29 publications

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“…Medaka Neu1 alone shows negligible sialidase activity, but its interaction with cathepsin A induces the stabilization of Neu1 structure, leading to a drastic induction of enzymatic activity toward sialoglycoconjugates. Methylumbelliferyl-N-acetyl neuraminic acid (MU-NANA) and 3′-sialyllactose are good substrates for medaka Neu1, while Neu1 shows moderate activity toward 6′sialyllactose and slight activity toward gangliosides (5). These enzymatic properties are quite similar to human NEU1 (7).…”

Section: B Sialidases In Beloniformesmentioning

confidence: 96%

“…Human NEU4 is reported to desialyze both glycoproteins and gangliosides and to be localized at mitochondria and ER, which are quite different properties from medaka Neu4 (8,9). In addition, a small number of medaka Neu1 and Neu4 are detected at the plasma membrane (5,6).…”

Section: B Sialidases In Beloniformesmentioning

confidence: 99%

“…N-glycosylation sites are also conserved in human and medaka. Furthermore, a lysosomal targeting motif (Tyr-X-X-φ, φ: hydrophobic residue)-like sequence (Tyr-Gly-Gly-Arg) is found at the C-terminus of medaka Neu1 (5). Medaka Neu4 does not possess such N-and C-terminal sequences which are specific to lysosomal sialidase (6).…”

Section: B Sialidases In Beloniformesmentioning

confidence: 99%

“…Treating cultured medaka primary fin cells with chloroquine, a lysosomal inhibitor, results in the lysosomal accumulation of α2-3 sialoglycoproteins, indicating the fish lysosome is a crucial organelle for glycoprotein degradation, as is also seen in mammals (4). In medaka, Neu1 and Neu4 act as lysosomal sialidases (5,6).…”

Section: B Sialidases In Beloniformesmentioning

confidence: 99%

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Functional Characterization of Fish Sialidases and Their Diversity among Different Orders

Shiozaki

Oishi

Honda

2019

TIGG

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Sialidase catalyzes the removal of sialic acids from glycoconjugates. While the physiological functions of mammalian sialidases have been elucidated, sialidases in other vertebrates, including those in fish, are not well understood. Recently, increased genomic resources in fish have become available, which will facilitate research on fish sialidase.Here, three fish orders (Cypriniformes, Beloniformes and Perciformes) have been selected to compare the properties of their sialidases. A Neu1 knockdown in medaka by a morpholino oligo resulted in the accumulation of Sia α2-3 linked sialoglycoproteins, leading to malfunctions in heart beating, embryo growth, hatching, and swimming, indicating that lysosomal Neu1 is a crucial factor for embryogenesis.Fish Neu3 and Neu4 function varies between fish species. Medaka and tilapia Neu3a localize at the plasma membrane, as is seen in humans. Zebrafish Neu3.1 is an ER sialidase, with an optimal pH (pH 2.6). Neu4 shows high diversity in subcellular localization: medaka and zebrafish Neu4 are detected at the lysosome and ER, respectively. Surprisingly, tilapia Neu4 is detected at nucleus, which makes it the first nuclear sialidase to be identified. Moreover, importin has been identified as a regulator of tilapia Neu4 functions. These results demonstrate the diversity of sialidase functions among fish species and the requirement of further fish research.

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Section: B Sialidases In Beloniformesmentioning

confidence: 96%

Section: B Sialidases In Beloniformesmentioning

confidence: 99%

Section: B Sialidases In Beloniformesmentioning

confidence: 99%

Section: B Sialidases In Beloniformesmentioning

confidence: 99%

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Functional Characterization of Fish Sialidases and Their Diversity among Different Orders

Shiozaki

Oishi

Honda

2019

TIGG

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“…NEU1 is the most abundant mammalian sialidase; it primarily presents in lysosomes and acts on glycopeptides and oligosaccharides. NEU1 plays an essential role in the degradation of N-glycans ( 14 , 15 ). Sialidase NEU1 deficiency has been found to affect sialic acid deposition ( 16 – 18 ).…”

Section: Introductionmentioning

confidence: 99%

Correlation Between Sialidase NEU1 mRNA Expression Changes in Autism Spectrum Disorder

Zhang

Gu²,

He³

et al. 2022

Front. Psychiatry

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Abnormal alterations in enzymes functioned in sialic acid modifications may be associated with ASD. In order to study the differences in peripheral blood sialidase (neuraminidase 1; NEU1) mRNA expression between autism spectrum disorder (ASD) children and healthy control, and to examine the correlation between NEU1 mRNA expression and the main behavioral phenotypes in children with ASD, we performed RT-qPCR to measure NEU1 mRNA expression in peripheral blood of 42 children with ASD and 42 healthy controls. In addition, we used the Autism Diagnostic Observation Schedule, Second Edition (ADOS-2) to measure and evaluate the behavioral phenotypes of children with ASD. Our results showed that NEU1 mRNA in the ASD group was significantly higher than in the control group (P < 0.0001). In addition, the ADOS-2 diagnostic scores of 42 children with ASD were correlated with their NEU1 mRNA expression results (R = 0.344, P = 0.0257). Moreover, in general, NEU1 mRNA expression was also positively correlated with the Social Affect (SA) of ADOS-2 (R = 0.3598, P = 0.0193) but not with the Restricted and Repetitive Behavior (RRB) (R = 0.15, P = 0.3432). Our results indicated that sialidase NEU1 mRNA was significantly increased in children with ASD, and its expression was correlated with the SA of children with ASD, which suggested that sialidase NEU1 may affect the SA of ASD. Our data highlighted the potential of NEU1 expression change may play an important role in ASD disease and lay the foundation for further studies on the relationship between NEU1 and ASD.

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Identification of novel fish sialidase genes responsible for KDN-cleaving activity

et al. 2020

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Lysosomal localization of Japanese medaka ( Oryzias latipes ) Neu1 sialidase and its highly conserved enzymatic profiles with human

Cited by 17 publications

References 29 publications

Functional Characterization of Fish Sialidases and Their Diversity among Different Orders

Functional Characterization of Fish Sialidases and Their Diversity among Different Orders

Correlation Between Sialidase NEU1 mRNA Expression Changes in Autism Spectrum Disorder

Identification of novel fish sialidase genes responsible for KDN-cleaving activity

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