A5038832594- Glycosylation and Glycoproteins Research
- Lysosomal Storage Disorders Research
- Cellular transport and secretion
- Enzyme Structure and Function
- Calcium signaling and nucleotide metabolism
- Trypanosoma species research and implications
- Protein purification and stability
- Bacterial Infections and Vaccines
- Carbohydrate Chemistry and Synthesis
- Viral Infectious Diseases and Gene Expression in Insects
- Erythrocyte Function and Pathophysiology
- Infant Nutrition and Health
- Escherichia coli research studies
- Cancer, Hypoxia, and Metabolism
- Parasitic Infections and Diagnostics
- Chemical Synthesis and Analysis
- Click Chemistry and Applications
- Animal Genetics and Reproduction
- Cytomegalovirus and herpesvirus research
- Galectins and Cancer Biology
- Biochemical and Molecular Research
- Toxoplasma gondii Research Studies
- Amino Acid Enzymes and Metabolism
- Biochemical and Structural Characterization
- Diabetes and associated disorders
Tokushima University
2015-2025
Kumamoto University
2019
Abstract Background Mucopolysaccharidosis type I (MPS I) is an inherited lysosomal storage disorder (LSD) caused by recessive mutations in the α-L-iduronidase ( IDUA ) gene. Enzyme replacement therapy (ERT) utilizing terminal mannose-6-phosphate (M6P)-carrying N -glycans attached to therapeutic enzymes produced mammalian cell lines has been clinically applied several LSDs. Recent studies suggested unidentified delivery pathway mediated sialic acid-containing -glycans. However, more...
Galactosialidosis is an autosomal recessive lysosomal storage disease caused by the combined deficiency of β-galactosidase and neuraminidase due to a defect in protective protein/cathepsin A. Patients present with various clinical manifestations are classified into three types according age onset: early infantile type, late juvenile/adult type. We report Japanese female case type galactosialidosis. Clinically, she presented short stature, coarse facies, angiokeratoma, remarkable action...
A traceless thioester-producing protocol featuring carboxypeptidase Y-mediated hydrazinolysis of cysteinyl prolyl leucine-tagged peptides has been developed. The followed by thioesterification affords thioesters. Self-editing the tag and subsequent trans-thioesterification yields peptide developed was successfully applied to conversion recombinant proteins
Galactosialidosis (GS) is a lysosomal cathepsin A (CTSA) deficiency. It associates with simultaneous decrease of neuraminidase 1 (NEU1) activity and sialylglycan storage. Central nervous system (CNS) symptoms reduce the quality life juvenile/adult-type GS patients, but there no effective therapy. Here, we established novel model mouse carrying homozygotic Ctsa IVS6+1g→a mutation causing partial exon 6 skipping concomitant deficiency Ctsa/Neu1. The mice developed juvenile/adult GS-like...
Human cytosolic sialidase (Neuraminidase 2, NEU2) catalyzes the removal of terminal sialic acid residues from glycoconjugates. The effect siastatin B, known as a inhibitor, has not been evaluated toward human NEU2 yet. We studied regulation activity by B in vitro and predicted interaction silico. Inhibitory stabilizing effects were analyzed comparison with DANA (2-deoxy-2,3-dehydro-N-acetylneuraminic acid) 4-umbelliferyl N-acetylneuraminic (4-MU-NANA)- α2,3-sialyllactose-degrading activities...
Human neuraminidase 1 (NEU1) is a lysosomal glycosidase that cleaves the terminal sialic acids of sialylglycoconjugates. NEU1 biosynthesized in endoplasmic reticulum (ER) lumen as an N-glycosylated protein. also associates with cathepsin A (CTSA) ER, migrates to lysosomes, and exerts catalytic activity. Extraordinary cellulo crystallization protein ER despite carrying three N-glycans per molecule at N186, N343, N352, respectively, were observed when single human gene was overexpressed...
In cellulo crystallization is a developing technique to provide crystals for protein structure determination, particularly proteins that are difficult prepare by in vitro crystallization. This method has key advantage: it requires neither purification step nor step. However, there still no systematic strategy improving the of because process occurs spontaneously. Here we report protocol produce and extract human lysosomal neuraminidase-1 (NEU1) cultured cells. Overexpression NEU1...
Neuraminidase 1 (NEU1) is a lysosomal exo-glycosidase and cleaves glycoside bonds of non-reducing terminal sialic acid. The association NEU1 with cathepsin A activates NEU1. Overexpression in mammalian cells causes self-association crystallization rough endoplasmic reticulum (ER). deficiency, called sialidosis, type storage disease. There no fundamental treatment for deficiency. Gene therapy seems effective, but it assumed to be dangerous because crystallizes intracellularly damages by...
ノイラミニダーゼ1（NEU1）は、リソソーム内で非還元末端シアル酸残基を加水分解により遊離するエキソグリコシダーゼである。NEU1は単独では活性がなく、カテプシンA（CTSA）と会合することで活性化される特徴がある。哺乳類細胞にNEU1を過剰発現させると小胞体でNEU1が結晶化する極めて珍しい性質をもつ。NEU1の変異により起こる疾患として、リソソーム病の一種であるシアリドーシスが知られている。シアリドーシスの治療法は実用化されていない。本疾患に対してはNEU1遺伝子を用いる遺伝子治療が有効と考えられるが、その自己会合や結晶化により細胞を傷つける可能性が想定される。本ミニレビューでは、NEU1とCTSAのはたらきや、関連するリソソーム病について概説する。