IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-33247-3.html
   My bibliography  Save this article

Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis

Author

Listed:
  • Kichitaro Nakajima

    (Osaka University, Suita
    Osaka University, Suita)

  • Keiichi Yamaguchi

    (Osaka University, Suita
    Osaka University, Suita)

  • Masahiro Noji

    (Kyoto University, Yoshidahonmatsu-cho, Sakyo-ku)

  • César Aguirre

    (Osaka University, Suita)

  • Kensuke Ikenaka

    (Osaka University, Suita)

  • Hideki Mochizuki

    (Osaka University, Suita)

  • Lianjie Zhou

    (Osaka University, Suita)

  • Hirotsugu Ogi

    (Osaka University, Suita)

  • Toru Ito

    (Niigata University)

  • Ichiei Narita

    (Niigata University)

  • Fumitake Gejyo

    (Niigata University of Pharmacy and Applied Life Sciences)

  • Hironobu Naiki

    (University of Fukui)

  • Suguru Yamamoto

    (Niigata University)

  • Yuji Goto

    (Osaka University, Suita
    Osaka University, Suita)

Abstract

Dialysis-related amyloidosis (DRA), a serious complication among long-term hemodialysis patients, is caused by amyloid fibrils of β2-microglobulin (β2m). Although high serum β2m levels and a long dialysis vintage are the primary and secondary risk factors for the onset of DRA, respectively, patients with these do not always develop DRA, indicating that there are additional risk factors. To clarify these unknown factors, we investigate the effects of human sera on β2m amyloid fibril formation, revealing that sera markedly inhibit amyloid fibril formation. Results from over 100 sera indicate that, although the inhibitory effects of sera deteriorate in long-term dialysis patients, they are ameliorated by maintenance dialysis treatments in the short term. Serum albumin prevents amyloid fibril formation based on macromolecular crowding effects, and decreased serum albumin concentration in dialysis patients is a tertiary risk factor for the onset of DRA. We construct a theoretical model assuming cumulative effects of the three risk factors, suggesting the importance of monitoring temporary and accumulated risks to prevent the development of amyloidosis, which occurs based on supersaturation-limited amyloid fibril formation in a crowded milieu.

Suggested Citation

  • Kichitaro Nakajima & Keiichi Yamaguchi & Masahiro Noji & César Aguirre & Kensuke Ikenaka & Hideki Mochizuki & Lianjie Zhou & Hirotsugu Ogi & Toru Ito & Ichiei Narita & Fumitake Gejyo & Hironobu Naiki , 2022. "Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33247-3
    DOI: 10.1038/s41467-022-33247-3
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-33247-3
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-33247-3?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Matthew G. Iadanza & Robert Silvers & Joshua Boardman & Hugh I. Smith & Theodoros K. Karamanos & Galia T. Debelouchina & Yongchao Su & Robert G. Griffin & Neil A. Ranson & Sheena E. Radford, 2018. "The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    Full references (including those not matched with items on IDEAS)

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Nils Bäumer & Eduardo Castellanos & Bartolome Soberats & Gustavo Fernández, 2023. "Bioinspired crowding directs supramolecular polymerisation," Nature Communications, Nature, vol. 14(1), pages 1-9, December.

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Martin Wilkinson & Rodrigo U. Gallardo & Roberto Maya Martinez & Nicolas Guthertz & Masatomo So & Liam D. Aubrey & Sheena E. Radford & Neil A. Ranson, 2023. "Disease-relevant β2-microglobulin variants share a common amyloid fold," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33247-3. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.