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Coiling and maturation of a high-performance fibre in hagfish slime gland thread cells

Timothy Winegard, Julia Herr, Carlos Mena, Betty Lee, Ivo Dinov, Deborah Bird, Mark Bernards, Sam Hobel, Blaire Van Valkenburgh, Arthur Toga and Douglas Fudge ()
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Timothy Winegard: University of Guelph
Julia Herr: University of Guelph
Carlos Mena: Laboratory of Neuro Imaging (LONI), Institute for Neuroimaging and Informatics (INI), Keck School of Medicine, University of Southern California (USC)
Betty Lee: Laboratory of Neuro Imaging (LONI), Institute for Neuroimaging and Informatics (INI), Keck School of Medicine, University of Southern California (USC)
Ivo Dinov: Laboratory of Neuro Imaging (LONI), Institute for Neuroimaging and Informatics (INI), Keck School of Medicine, University of Southern California (USC)
Deborah Bird: University of California Los Angeles
Mark Bernards: University of Guelph
Sam Hobel: Laboratory of Neuro Imaging (LONI), Institute for Neuroimaging and Informatics (INI), Keck School of Medicine, University of Southern California (USC)
Blaire Van Valkenburgh: University of California Los Angeles
Arthur Toga: Laboratory of Neuro Imaging (LONI), Institute for Neuroimaging and Informatics (INI), Keck School of Medicine, University of Southern California (USC)
Douglas Fudge: University of Guelph

Nature Communications, 2014, vol. 5, issue 1, 1-5

Abstract: Abstract The defensive slime of hagfishes contains thousands of intermediate filament protein threads that are manufactured within specialized gland thread cells. The material properties of these threads rival those of spider dragline silks, which makes them an ideal model for biomimetic efforts to produce sustainable protein materials, yet how the thread is produced and organized within the cell is not well understood. Here we show how changes in nuclear morphology, size and position can explain the three-dimensional pattern of thread coiling in gland thread cells, and how the ultrastructure of the thread changes as very young thread cells develop into large cells with fully mature coiled threads. Our model provides an explanation for the complex process of thread assembly and organization that has fascinated and perplexed biologists for over a century, and provides valuable insights for the quest to manufacture high-performance biomimetic protein materials.

Date: 2014
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4534

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DOI: 10.1038/ncomms4534

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