Publications by authors named "Kaori Kuwabara"

A high mortality rate is found among septic patients with disseminated intravascular coagulation (DIC). Anticoagulants have been used for treating septic DIC especially in Japanese clinical settings; however, their effectiveness is quite controversial across studies. According to several randomized controlled trials and meta-analyses, antithrombin and recombinant thrombomodulin had no therapeutic benefit in the treatment of sepsis.

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The highly sulfated domains of heparan sulfate (HS), alias HS S-domains, are made up of repeated trisulfated disaccharide units [iduronic acid (2S)-glucosamine (NS, 6S)] and are selectively remodeled by extracellular endoglucosamine 6-sulfatases (Sulfs). Although HS S-domains are critical for signal transduction of several growth factors, their roles in amyloidoses are not yet fully understood. Herein, we found HS S-domains in the kidney of a patient with transthyretin amyloidosis.

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Introduction: Apolipoprotein A-I (apoA-I) amyloidosis is either a non-hereditary form with deposits of wild-type apoA-I proteins in atherosclerotic plaques or a hereditary form with progressive accumulation of mutant apoA-I proteins in different tissues. Several small polyphenolic molecules reportedly inhibited formation of fibrillar assemblies of some amyloidogenic proteins and their cytotoxicity, but small molecules that inhibit apoA-I fibril formation have never been reported.

Methods: Our methods included a thioflavin-T-binding assay, atomic force microscopy and dot blot and cell-based assays.

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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.

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