IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-29064-3.html
   My bibliography  Save this article

Inhibition of lung microbiota-derived proapoptotic peptides ameliorates acute exacerbation of pulmonary fibrosis

Author

Listed:
  • Corina N. D’Alessandro-Gabazza

    (Mie University Faculty and Graduate School of Medicine
    Mie University
    University of Illinois at Urbana–Champaign)

  • Taro Yasuma

    (Mie University Faculty and Graduate School of Medicine
    Mie University Faculty and Graduate School of Medicine)

  • Tetsu Kobayashi

    (Mie University Faculty and Graduate School of Medicine)

  • Masaaki Toda

    (Mie University Faculty and Graduate School of Medicine
    Mie University)

  • Ahmed M. Abdel-Hamid

    (University of Illinois at Urbana–Champaign
    Minia University)

  • Hajime Fujimoto

    (Mie University Faculty and Graduate School of Medicine)

  • Osamu Hataji

    (Matsusaka Municipal Hospital)

  • Hiroki Nakahara

    (Mie University Faculty and Graduate School of Medicine)

  • Atsuro Takeshita

    (Mie University Faculty and Graduate School of Medicine
    Mie University Faculty and Graduate School of Medicine)

  • Kota Nishihama

    (Mie University Faculty and Graduate School of Medicine)

  • Tomohito Okano

    (Mie University Faculty and Graduate School of Medicine)

  • Haruko Saiki

    (Mie University Faculty and Graduate School of Medicine)

  • Yuko Okano

    (Mie University Faculty and Graduate School of Medicine
    Mie University Faculty and Graduate School of Medicine)

  • Atsushi Tomaru

    (Mie University Faculty and Graduate School of Medicine)

  • Valeria Fridman D’Alessandro

    (Mie University Faculty and Graduate School of Medicine)

  • Miyako Shiraishi

    (University of Illinois at Urbana–Champaign)

  • Akira Mizoguchi

    (Mie University Graduate School of Medicine)

  • Ryoichi Ono

    (Mie University Graduate School of Medicine)

  • Junpei Ohtsuka

    (Mie University Graduate School of Medicine
    BioComo Incorporation)

  • Masayuki Fukumura

    (Mie University Graduate School of Medicine
    BioComo Incorporation)

  • Tetsuya Nosaka

    (Mie University Graduate School of Medicine)

  • Xuenan Mi

    (University of Illinois at Urbana-Champaign)

  • Diwakar Shukla

    (University of Illinois at Urbana-Champaign)

  • Kensuke Kataoka

    (Tosei General Hospital)

  • Yasuhiro Kondoh

    (Tosei General Hospital)

  • Masaki Hirose

    (National Hospital Organization Kinki-Chuo Chest Medical Center)

  • Toru Arai

    (National Hospital Organization Kinki-Chuo Chest Medical Center)

  • Yoshikazu Inoue

    (National Hospital Organization Kinki-Chuo Chest Medical Center)

  • Yutaka Yano

    (Mie University Faculty and Graduate School of Medicine)

  • Roderick I. Mackie

    (University of Illinois at Urbana–Champaign
    The University of Illinois at Urbana–Champaign
    the University of Illinois at Urbana–Champaign)

  • Isaac Cann

    (University of Illinois at Urbana–Champaign
    The University of Illinois at Urbana–Champaign
    the University of Illinois at Urbana–Champaign
    The University of Illinois at Urbana–Champaign)

  • Esteban C. Gabazza

    (Mie University Faculty and Graduate School of Medicine
    Mie University
    University of Illinois at Urbana–Champaign)

Abstract

Idiopathic pulmonary fibrosis is an incurable disease of unknown etiology. Acute exacerbation of idiopathic pulmonary fibrosis is associated with high mortality. Excessive apoptosis of lung epithelial cells occurs in pulmonary fibrosis acute exacerbation. We recently identified corisin, a proapoptotic peptide that triggers acute exacerbation of pulmonary fibrosis. Here, we provide insights into the mechanism underlying the processing and release of corisin. Furthermore, we demonstrate that an anticorisin monoclonal antibody ameliorates lung fibrosis by significantly inhibiting acute exacerbation in the human transforming growth factorβ1 model and acute lung injury in the bleomycin model. By investigating the impact of the anticorisin monoclonal antibody in a general model of acute lung injury, we further unravel the potential of corisin to impact such diseases. These results underscore the role of corisin in the pathogenesis of acute exacerbation of pulmonary fibrosis and acute lung injury and provide a novel approach to treating this incurable disease.

Suggested Citation

  • Corina N. D’Alessandro-Gabazza & Taro Yasuma & Tetsu Kobayashi & Masaaki Toda & Ahmed M. Abdel-Hamid & Hajime Fujimoto & Osamu Hataji & Hiroki Nakahara & Atsuro Takeshita & Kota Nishihama & Tomohito O, 2022. "Inhibition of lung microbiota-derived proapoptotic peptides ameliorates acute exacerbation of pulmonary fibrosis," Nature Communications, Nature, vol. 13(1), pages 1-23, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-29064-3
    DOI: 10.1038/s41467-022-29064-3
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-29064-3
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-022-29064-3?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. Corina N. D’Alessandro-Gabazza & Tetsu Kobayashi & Taro Yasuma & Masaaki Toda & Heejin Kim & Hajime Fujimoto & Osamu Hataji & Atsuro Takeshita & Kota Nishihama & Tomohito Okano & Yuko Okano & Yoichi N, 2020. "A Staphylococcus pro-apoptotic peptide induces acute exacerbation of pulmonary fibrosis," Nature Communications, Nature, vol. 11(1), pages 1-17, December.
    2. Yuelan Yin & Hao Yao & Swapnil Doijad & Suwei Kong & Yang Shen & Xuexue Cai & Weijun Tan & Yuting Wang & Youwei Feng & Zhiting Ling & Guoliang Wang & Yachen Hu & Kai Lian & Xinyu Sun & Yuliang Liu & C, 2019. "A hybrid sub-lineage of Listeria monocytogenes comprising hypervirulent isolates," Nature Communications, Nature, vol. 10(1), pages 1-16, December.
    3. Christopher M. Dobson, 2003. "Protein folding and misfolding," Nature, Nature, vol. 426(6968), pages 884-890, December.
    4. Ivana V Yang & Leah G Luna & Jennifer Cotter & Janet Talbert & Sonia M Leach & Raven Kidd & Julia Turner & Nathan Kummer & Dolly Kervitsky & Kevin K Brown & Kathy Boon & Marvin I Schwarz & David A Sch, 2012. "The Peripheral Blood Transcriptome Identifies the Presence and Extent of Disease in Idiopathic Pulmonary Fibrosis," PLOS ONE, Public Library of Science, vol. 7(6), pages 1-11, June.
    Full references (including those not matched with items on IDEAS)

    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. Jian Tian & Jaie C Woodard & Anna Whitney & Eugene I Shakhnovich, 2015. "Thermal Stabilization of Dihydrofolate Reductase Using Monte Carlo Unfolding Simulations and Its Functional Consequences," PLOS Computational Biology, Public Library of Science, vol. 11(4), pages 1-27, April.
    2. Matthias M. Schneider & Saurabh Gautam & Therese W. Herling & Ewa Andrzejewska & Georg Krainer & Alyssa M. Miller & Victoria A. Trinkaus & Quentin A. E. Peter & Francesco Simone Ruggeri & Michele Vend, 2021. "The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    3. Eri Chatani & Yutaro Tsuchisaka & Yuki Masuda & Roumiana Tsenkova, 2014. "Water Molecular System Dynamics Associated with Amyloidogenic Nucleation as Revealed by Real Time Near Infrared Spectroscopy and Aquaphotomics," PLOS ONE, Public Library of Science, vol. 9(7), pages 1-10, July.
    4. Stefan Auer & Filip Meersman & Christopher M Dobson & Michele Vendruscolo, 2008. "A Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric Aggregates," PLOS Computational Biology, Public Library of Science, vol. 4(11), pages 1-7, November.
    5. Espinoza Ortiz, J.S. & Dias, Cristiano L., 2018. "Cooperative fibril model: Native, amyloid-like fibril and unfolded states of proteins," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 511(C), pages 154-165.
    6. Sheng Chen & Anuradhika Puri & Braxton Bell & Joseph Fritsche & Hector H. Palacios & Maurie Balch & Macy L. Sprunger & Matthew K. Howard & Jeremy J. Ryan & Jessica N. Haines & Gary J. Patti & Albert A, 2024. "HTRA1 disaggregates α-synuclein amyloid fibrils and converts them into non-toxic and seeding incompetent species," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    7. Pengfei Tian & Kresten Lindorff-Larsen & Wouter Boomsma & Mogens Høgh Jensen & Daniel Erik Otzen, 2016. "A Monte Carlo Study of the Early Steps of Functional Amyloid Formation," PLOS ONE, Public Library of Science, vol. 11(1), pages 1-18, January.
    8. Sanne Abeln & Michele Vendruscolo & Christopher M Dobson & Daan Frenkel, 2014. "A Simple Lattice Model That Captures Protein Folding, Aggregation and Amyloid Formation," PLOS ONE, Public Library of Science, vol. 9(1), pages 1-8, January.
    9. Wen-Ting Chu & Ji-Long Zhang & Qing-Chuan Zheng & Lin Chen & Hong-Xing Zhang, 2013. "Insights into the Folding and Unfolding Processes of Wild-Type and Mutated SH3 Domain by Molecular Dynamics and Replica Exchange Molecular Dynamics Simulations," PLOS ONE, Public Library of Science, vol. 8(5), pages 1-9, May.
    10. Noah S Bieler & Tuomas P J Knowles & Daan Frenkel & Robert Vácha, 2012. "Connecting Macroscopic Observables and Microscopic Assembly Events in Amyloid Formation Using Coarse Grained Simulations," PLOS Computational Biology, Public Library of Science, vol. 8(10), pages 1-10, October.
    11. Jaya C Jose & Prathit Chatterjee & Neelanjana Sengupta, 2014. "Cross Dimerization of Amyloid-β and αSynuclein Proteins in Aqueous Environment: A Molecular Dynamics Simulations Study," PLOS ONE, Public Library of Science, vol. 9(9), pages 1-13, September.
    12. Carlos Família & Sarah R Dennison & Alexandre Quintas & David A Phoenix, 2015. "Prediction of Peptide and Protein Propensity for Amyloid Formation," PLOS ONE, Public Library of Science, vol. 10(8), pages 1-16, August.
    13. Bente Vestergaard & Minna Groenning & Manfred Roessle & Jette S Kastrup & Marco van de Weert & James M Flink & Sven Frokjaer & Michael Gajhede & Dmitri I Svergun, 2007. "A Helical Structural Nucleus Is the Primary Elongating Unit of Insulin Amyloid Fibrils," PLOS Biology, Public Library of Science, vol. 5(5), pages 1-9, May.
    14. Arthur Fischbach & Angela Johns & Kara L. Schneider & Xinxin Hao & Peter Tessarz & Thomas Nyström, 2023. "Artificial Hsp104-mediated systems for re-localizing protein aggregates," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    15. Kübra Kaygisiz & Lena Rauch-Wirth & Arghya Dutta & Xiaoqing Yu & Yuki Nagata & Tristan Bereau & Jan Münch & Christopher V. Synatschke & Tanja Weil, 2023. "Data-mining unveils structure–property–activity correlation of viral infectivity enhancing self-assembling peptides," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    16. Mookyung Cheon & Iksoo Chang & Sandipan Mohanty & Leila M Luheshi & Christopher M Dobson & Michele Vendruscolo & Giorgio Favrin, 2007. "Structural Reorganisation and Potential Toxicity of Oligomeric Species Formed during the Assembly of Amyloid Fibrils," PLOS Computational Biology, Public Library of Science, vol. 3(9), pages 1-12, September.
    17. Qi Wang & Joshua L Johnson & Nathalie YR Agar & Jeffrey N Agar, 2008. "Protein Aggregation and Protein Instability Govern Familial Amyotrophic Lateral Sclerosis Patient Survival," PLOS Biology, Public Library of Science, vol. 6(7), pages 1-19, July.
    18. Morten S Dueholm & Daniel Otzen & Per Halkjær Nielsen, 2013. "Evolutionary Insight into the Functional Amyloids of the Pseudomonads," PLOS ONE, Public Library of Science, vol. 8(10), pages 1-1, October.
    19. Allen W Bryan Jr. & Matthew Menke & Lenore J Cowen & Susan L Lindquist & Bonnie Berger, 2009. "BETASCAN: Probable β-amyloids Identified by Pairwise Probabilistic Analysis," PLOS Computational Biology, Public Library of Science, vol. 5(3), pages 1-11, March.
    20. Morten S Dueholm & Mads Albertsen & Daniel Otzen & Per Halkjær Nielsen, 2012. "Curli Functional Amyloid Systems Are Phylogenetically Widespread and Display Large Diversity in Operon and Protein Structure," PLOS ONE, Public Library of Science, vol. 7(12), pages 1-10, 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_s41467-022-29064-3. 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.