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ASGR1 and Its Enigmatic Relative, CLEC10A

Hoober, J. Kenneth·2020·International Journal of Molecular Sciences
DOI 10.3390/ijms21144818PMC PMC7404283
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Abstract

The large family of C-type lectin (CLEC) receptors comprises carbohydrate-binding proteins that require Ca2+ to bind a ligand. The prototypic receptor is the asialoglycoprotein receptor-1 (ASGR1, CLEC4H1) that is expressed primarily by hepatocytes. The early work on ASGR1, which is highly specific for N-acetylgalactosamine (GalNAc), established the foundation for understanding the overall function of CLEC receptors. Cells of the immune system generally express more than one CLEC receptor that serve diverse functions such as pathogen-recognition, initiation of cellular signaling, cellular adhesion, glycoprotein turnover, inflammation and immune responses. The receptor CLEC10A (C-type lectin domain family 10 member A, CD301; also called the macrophage galactose-type lectin, MGL) contains a carbohydrate-recognition domain (CRD) that is homologous to the CRD of ASGR1, and thus, is also specific for GalNAc. CLEC10A is most highly expressed on immature DCs, monocyte-derived DCs, and alternatively activated macrophages (subtype M2a) as well as oocytes and progenitor cells at several stages of embryonic development. This receptor is involved in initiation of TH1, TH2, and TH17 immune responses and induction of tolerance in naïve T cells. Ligand-mediated endocytosis of CLEC receptors initiates a Ca2+ signal that interestingly has different outcomes depending on ligand properties, concentration, and frequency of administration. This review summarizes studies that have been carried out on these receptors.

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  • ASGR1 binds to glycoproteins containing galactose or N-acetylgalactosamine, while ASGR2 mediates the internalization and trafficking of the glycoprotein to lysosomes for degradation.

    “ASGR1 binds to glycoproteins containing galactose (Gal) or N-acetylgalactosamine (GalNAc), while ASGR2 mediates the internalization and trafficking of the glycoprotein to the lysosomes for degradation [83].”

    From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [83]

    Section 2 (ASGR1; page not provided) describes ASGR1’s preference for GalNAc over Gal and says that bound glycoprotein ligands are internalized and degraded in lysosomes. It describes this process for the receptor generally, not as a distinct role mediated by ASGR2. The claimed division of labor between ASGR1 and ASGR2 is therefore not supported. (LLM, conf=0.88)

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Metadata

Authors
Hoober, J. K.
Affiliations
Susavion Biosciences, Inc., Tempe, AZ 85281, USA
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2020-07-08
Volume
21
Issue
14
Pages
4818
ISSN
1422-0067
DOI
10.3390/ijms21144818
PMC
PMC7404283
Cited by
74
References
8
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)

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