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Heparan sulfate S-domains and extracellular sulfatases (Sulfs): their possible roles in protein aggregation diseases

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Abstract

Highly sulfated domains of heparan sulfate (HS), also known as HS S-domains, consist of repeated trisulfated disaccharide units [iduronic acid (2S)-glucosamine (NS, 6S)–]. The expression of HS S-domains at the cell surface is determined by two mechanisms: tightly regulated biosynthetic machinery and enzymatic remodeling by extracellular endoglucosamine 6-sulfatases, Sulf-1 and Sulf-2. Intracellular or extracellular deposits of misfolded and aggregated proteins are characteristic of protein aggregation diseases. Although proteins can aggregate alone, deposits of protein aggregates in vivo contain a number of proteinaceous and non-protein components. HS S-domains are one non-protein component of these aggregated deposits. HS S-domains are considered to be critical for signal transduction of several growth factors and several disease conditions, such as tumor progression, but their roles in protein aggregation diseases are not yet fully understood. This review summarizes the current understanding of the possible roles of HS S-domains and Sulfs in the formation and cytotoxicity of protein aggregates.

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Fig. 1: Sulfs post-synthetically remodel HS at the cell surface.
Fig. 2: HS S-domains mediate the interactions of protein aggregates with cells.
Fig. 3: Possible model of the role of HS S-domains in protein aggregation processes.

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Abbreviations

Aβ:

Amyloid β protein

HS:

Heparan sulfate

GAG:

Glycosaminoglycan

AD:

Alzheimer’s disease

AA:

Amyloid A

SAA:

Serum amyloid protein A

AL:

Amyloid immunoglobulin light chain

β2-m:

β2-microglobulin

ATTR:

Amyloid transthyretin

IAPP:

Islet amyloid polypeptide

HSPG:

Heparan sulfate proteoglycan

GlcNAc:

N-acetylglucosamine

GlcA:

Glucuronic acid

IdoA:

Iduronic acid

FGF:

Fibroblast growth factor

VEGF:

Vascular endothelial growth factor

GDNF:

Glial cell line-derived neurotrophic factor

apoA-I:

Apolipoprotein A-I

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Acknowledgments

The author thanks Dr. Kenji Uchimura for critical reading and comments on the manuscript. The author would like to apologize to those whose work could not be directly cited because of space constraints. This work was partly supported by Grants-in-Aid for Young Scientists B-15 K19488 and B-17 K16123 from the Japan Society for the Promotion of Science.

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  1. Department of Biochemistry, Wakayama Medical University, 811-1 Kimiidera, Wakayama, 641-8509, Japan

    Kazuchika Nishitsuji

  2. Department of Pathology and Laboratory Medicine, Graduate School of Biomedical Sciences, Tokushima University, 3-18-15 Kuramoto-cho, Tokushima, 770-8503, Japan

    Kazuchika Nishitsuji

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Nishitsuji, K. Heparan sulfate S-domains and extracellular sulfatases (Sulfs): their possible roles in protein aggregation diseases. Glycoconj J 35, 387–396 (2018). https://doi.org/10.1007/s10719-018-9833-8

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