Neuraminidase-1 (NEU1): Biological Roles and Therapeutic Relevance in Human Disease

Neuraminidases catalyze the desialylation of cell-surface glycoconjugates and play crucial roles in the development and function of tissues and organs. In both physiological and pathophysiological contexts, neuraminidases mediate diverse biological activities via the catalytic hydrolysis of terminal...

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Published inCurrent Issues in Molecular Biology Vol. 46; no. 8; pp. 8031 - 8052
Main Authors Du, Jingxia, Shui, Hanqi, Chen, Rongjun, Dong, Yibo, Xiao, Chengyao, Hu, Yue, Wong, Nai-Kei
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 01.08.2024
MDPI
Subjects
Amino acids
Cardiovascular diseases
Development and progression
disease mechanisms
drug development
Gene therapy
lysosomal sialidase
Medical research
Medicine, Experimental
Muscles
Nervous system diseases
neuraminidase-1
Proteins
Review
sialic acids (SAs)
drug development
lysosomal sialidase
neuraminidase-1
disease mechanisms
sialic acids (SAs)
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Abstract Neuraminidases catalyze the desialylation of cell-surface glycoconjugates and play crucial roles in the development and function of tissues and organs. In both physiological and pathophysiological contexts, neuraminidases mediate diverse biological activities via the catalytic hydrolysis of terminal neuraminic, or sialic acid residues in glycolipid and glycoprotein substrates. The selective modulation of neuraminidase activity constitutes a promising strategy for treating a broad spectrum of human pathologies, including sialidosis and galactosialidosis, neurodegenerative disorders, cancer, cardiovascular diseases, diabetes, and pulmonary disorders. Structurally distinct as a large family of mammalian proteins, neuraminidases (NEU1 through NEU4) possess dissimilar yet overlapping profiles of tissue expression, cellular/subcellular localization, and substrate specificity. NEU1 is well characterized for its lysosomal catabolic functions, with ubiquitous and abundant expression across such tissues as the kidney, pancreas, skeletal muscle, liver, lungs, placenta, and brain. NEU1 also exhibits a broad substrate range on the cell surface, where it plays hitherto underappreciated roles in modulating the structure and function of cellular receptors, providing a basis for it to be a potential drug target in various human diseases. This review seeks to summarize the recent progress in the research on NEU1-associated diseases and highlight the mechanistic implications of NEU1 in disease pathogenesis. An improved understanding of NEU1-associated diseases should help accelerate translational initiatives to develop novel or better therapeutics.
AbstractList Neuraminidases catalyze the desialylation of cell-surface glycoconjugates and play crucial roles in the development and function of tissues and organs. In both physiological and pathophysiological contexts, neuraminidases mediate diverse biological activities via the catalytic hydrolysis of terminal neuraminic, or sialic acid residues in glycolipid and glycoprotein substrates. The selective modulation of neuraminidase activity constitutes a promising strategy for treating a broad spectrum of human pathologies, including sialidosis and galactosialidosis, neurodegenerative disorders, cancer, cardiovascular diseases, diabetes, and pulmonary disorders. Structurally distinct as a large family of mammalian proteins, neuraminidases (NEU1 through NEU4) possess dissimilar yet overlapping profiles of tissue expression, cellular/subcellular localization, and substrate specificity. NEU1 is well characterized for its lysosomal catabolic functions, with ubiquitous and abundant expression across such tissues as the kidney, pancreas, skeletal muscle, liver, lungs, placenta, and brain. NEU1 also exhibits a broad substrate range on the cell surface, where it plays hitherto underappreciated roles in modulating the structure and function of cellular receptors, providing a basis for it to be a potential drug target in various human diseases. This review seeks to summarize the recent progress in the research on NEU1-associated diseases and highlight the mechanistic implications of NEU1 in disease pathogenesis. An improved understanding of NEU1-associated diseases should help accelerate translational initiatives to develop novel or better therapeutics.
Neuraminidases catalyze the desialylation of cell-surface glycoconjugates and play crucial roles in the development and function of tissues and organs. In both physiological and pathophysiological contexts, neuraminidases mediate diverse biological activities via the catalytic hydrolysis of terminal neuraminic, or sialic acid residues in glycolipid and glycoprotein substrates. The selective modulation of neuraminidase activity constitutes a promising strategy for treating a broad spectrum of human pathologies, including sialidosis and galactosialidosis, neurodegenerative disorders, cancer, cardiovascular diseases, diabetes, and pulmonary disorders. Structurally distinct as a large family of mammalian proteins, neuraminidases (NEU1 through NEU4) possess dissimilar yet overlapping profiles of tissue expression, cellular/subcellular localization, and substrate specificity. NEU1 is well characterized for its lysosomal catabolic functions, with ubiquitous and abundant expression across such tissues as the kidney, pancreas, skeletal muscle, liver, lungs, placenta, and brain. NEU1 also exhibits a broad substrate range on the cell surface, where it plays hitherto underappreciated roles in modulating the structure and function of cellular receptors, providing a basis for it to be a potential drug target in various human diseases. This review seeks to summarize the recent progress in the research on NEU1-associated diseases and highlight the mechanistic implications of NEU1 in disease pathogenesis. An improved understanding of NEU1-associated diseases should help accelerate translational initiatives to develop novel or better therapeutics.Neuraminidases catalyze the desialylation of cell-surface glycoconjugates and play crucial roles in the development and function of tissues and organs. In both physiological and pathophysiological contexts, neuraminidases mediate diverse biological activities via the catalytic hydrolysis of terminal neuraminic, or sialic acid residues in glycolipid and glycoprotein substrates. The selective modulation of neuraminidase activity constitutes a promising strategy for treating a broad spectrum of human pathologies, including sialidosis and galactosialidosis, neurodegenerative disorders, cancer, cardiovascular diseases, diabetes, and pulmonary disorders. Structurally distinct as a large family of mammalian proteins, neuraminidases (NEU1 through NEU4) possess dissimilar yet overlapping profiles of tissue expression, cellular/subcellular localization, and substrate specificity. NEU1 is well characterized for its lysosomal catabolic functions, with ubiquitous and abundant expression across such tissues as the kidney, pancreas, skeletal muscle, liver, lungs, placenta, and brain. NEU1 also exhibits a broad substrate range on the cell surface, where it plays hitherto underappreciated roles in modulating the structure and function of cellular receptors, providing a basis for it to be a potential drug target in various human diseases. This review seeks to summarize the recent progress in the research on NEU1-associated diseases and highlight the mechanistic implications of NEU1 in disease pathogenesis. An improved understanding of NEU1-associated diseases should help accelerate translational initiatives to develop novel or better therapeutics.
Audience Academic
Author Xiao, Chengyao
Du, Jingxia
Wong, Nai-Kei
Chen, Rongjun
Dong, Yibo
Hu, Yue
Shui, Hanqi
AuthorAffiliation 2 Clinical Pharmacology Section, Department of Pharmacology, Shantou University Medical College, Shantou 515041, China; 21rjchen@stu.edu.cn
1 College of Basic Medicine and Forensic Medicine, Henan University of Science and Technology, Luoyang 471023, China; shq080700@163.com (H.S.); 17716392921@163.com (Y.D.); xcy0822@126.com (C.X.); 15603861842@163.com (Y.H.)
AuthorAffiliation_xml – name: 2 Clinical Pharmacology Section, Department of Pharmacology, Shantou University Medical College, Shantou 515041, China; 21rjchen@stu.edu.cn
– name: 1 College of Basic Medicine and Forensic Medicine, Henan University of Science and Technology, Luoyang 471023, China; shq080700@163.com (H.S.); 17716392921@163.com (Y.D.); xcy0822@126.com (C.X.); 15603861842@163.com (Y.H.)
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  fullname: Du, Jingxia
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  orcidid: 0000-0003-1303-3170
  surname: Wong
  fullname: Wong, Nai-Kei
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Issue 8
Keywords drug development
lysosomal sialidase
neuraminidase-1
disease mechanisms
sialic acids (SAs)
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Snippet Neuraminidases catalyze the desialylation of cell-surface glycoconjugates and play crucial roles in the development and function of tissues and organs. In both...
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SubjectTerms Amino acids
Cardiovascular diseases
Development and progression
disease mechanisms
drug development
Gene therapy
lysosomal sialidase
Medical research
Medicine, Experimental
Muscles
Nervous system diseases
neuraminidase-1
Proteins
Review
sialic acids (SAs)
Title Neuraminidase-1 (NEU1): Biological Roles and Therapeutic Relevance in Human Disease
URI https://www.ncbi.nlm.nih.gov/pubmed/39194692
https://www.proquest.com/docview/3097853243
https://pubmed.ncbi.nlm.nih.gov/PMC11353077
https://doaj.org/article/28d55a6346104e9d8db600b3f020cea4
Volume 46
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