Cellular interaction and cytotoxicity of ...
Document type :
Article dans une revue scientifique
DOI :
PMID :
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Title :
Cellular interaction and cytotoxicity of the iowa mutation of apolipoprotein A-I (ApoA-IIowa) amyloid mediated by sulfate moieties of heparan sulfate
Author(s) :
Kuwabara, Kaori [Auteur]
Nishitsuji, Kazuchika [Auteur]
Uchimura, Kenji [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Hung, Shang-Cheng [Auteur]
Mizuguchi, Makoto [Auteur]
Nakajima, Hiroyuki [Auteur]
Mikawa, Shiho [Auteur]
Kobayashi, Norihiro [Auteur]
Saito, Hiroyuki [Auteur]
Sakashita, Naomi [Auteur]
Nishitsuji, Kazuchika [Auteur]
Uchimura, Kenji [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Hung, Shang-Cheng [Auteur]
Mizuguchi, Makoto [Auteur]
Nakajima, Hiroyuki [Auteur]
Mikawa, Shiho [Auteur]
Kobayashi, Norihiro [Auteur]
Saito, Hiroyuki [Auteur]
Sakashita, Naomi [Auteur]
Journal title :
The Journal of biological chemistry
Abbreviated title :
J. Biol. Chem.
Volume number :
290
Pages :
24210-24221
Publication date :
2015-10-02
ISSN :
1083-351X
English keyword(s) :
Proteoglycan
Cell Membrane
apolipoprotein
Cricetulus
Humans
Lysosomes
Sulfates
Amyloidogenic Proteins
Glycobiology
familial amyloid polyneuropathy
Swine
Amyloid beta-Peptides
Glycosides
Female
Amyloid
HSulf
Sulfur
CHO Cells
Protein Structure, Tertiary
Heparan sulfate
Cricetinae
Heparitin Sulfate
Animals
Apolipoprotein A-I
Protein Binding
Amyloid Neuropathies, Familial
Mice
Amyloidosis
Mice, Inbred BALB C
Heparin
Microscopy, Fluorescence
Cell Membrane
apolipoprotein
Cricetulus
Humans
Lysosomes
Sulfates
Amyloidogenic Proteins
Glycobiology
familial amyloid polyneuropathy
Swine
Amyloid beta-Peptides
Glycosides
Female
Amyloid
HSulf
Sulfur
CHO Cells
Protein Structure, Tertiary
Heparan sulfate
Cricetinae
Heparitin Sulfate
Animals
Apolipoprotein A-I
Protein Binding
Amyloid Neuropathies, Familial
Mice
Amyloidosis
Mice, Inbred BALB C
Heparin
Microscopy, Fluorescence
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
The single amino acid mutation G26R in human apolipoprotein A-I (apoA-I) is associated with familial amyloid polyneuropathy III. ApoA-I carrying this mutation (apoA-IIowa) forms amyloid fibrils in vitro. Heparan sulfate ...
Show more >The single amino acid mutation G26R in human apolipoprotein A-I (apoA-I) is associated with familial amyloid polyneuropathy III. ApoA-I carrying this mutation (apoA-IIowa) forms amyloid fibrils in vitro. Heparan sulfate (HS) is a glycosaminoglycan that is abundant at the cell surface and in the extracellular matrix. Although HS and its highly sulfated domains are involved in aggregation of amyloid-β and accumulate in cerebral amyloid plaques of patients with Alzheimer disease and mouse models of this disease, the role of HS in familial amyloid polyneuropathy III has never been addressed. Here, we used cell models to investigate the possible role of HS in the cytotoxicity of apoA-IIowa amyloid. Wild-type CHO cells, but not pgsD-677 cells, an HS-deficient CHO mutant, demonstrated uptake of apoA-IIowa amyloid after incubation with the amyloid. Addition of sulfated glycosaminoglycans to culture media prevented interaction with and cytotoxicity of apoA-IIowa amyloid to CHO cells. Elimination of cell surface HS or inhibition of HS sulfation with chemical reagents interfered with interaction of apoA-IIowa amyloid with CHO cells. We also found that cellular interaction and cytotoxicity of apoA-IIowa amyloid were significantly attenuated in CHO cells that stably expressed the human extracellular endoglucosamine 6-sulfatases HSulf-1 and HSulf-2. Our results thus suggest that cell surface HS mediates cytotoxicity of apoA-IIowa amyloid and that enzymatic remodeling of HS mitigates the cytotoxicity.Show less >
Show more >The single amino acid mutation G26R in human apolipoprotein A-I (apoA-I) is associated with familial amyloid polyneuropathy III. ApoA-I carrying this mutation (apoA-IIowa) forms amyloid fibrils in vitro. Heparan sulfate (HS) is a glycosaminoglycan that is abundant at the cell surface and in the extracellular matrix. Although HS and its highly sulfated domains are involved in aggregation of amyloid-β and accumulate in cerebral amyloid plaques of patients with Alzheimer disease and mouse models of this disease, the role of HS in familial amyloid polyneuropathy III has never been addressed. Here, we used cell models to investigate the possible role of HS in the cytotoxicity of apoA-IIowa amyloid. Wild-type CHO cells, but not pgsD-677 cells, an HS-deficient CHO mutant, demonstrated uptake of apoA-IIowa amyloid after incubation with the amyloid. Addition of sulfated glycosaminoglycans to culture media prevented interaction with and cytotoxicity of apoA-IIowa amyloid to CHO cells. Elimination of cell surface HS or inhibition of HS sulfation with chemical reagents interfered with interaction of apoA-IIowa amyloid with CHO cells. We also found that cellular interaction and cytotoxicity of apoA-IIowa amyloid were significantly attenuated in CHO cells that stably expressed the human extracellular endoglucosamine 6-sulfatases HSulf-1 and HSulf-2. Our results thus suggest that cell surface HS mediates cytotoxicity of apoA-IIowa amyloid and that enzymatic remodeling of HS mitigates the cytotoxicity.Show less >
Language :
Anglais
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Submission date :
2020-02-12T15:11:38Z