ArticleScientific reports2019
The Functional Mammalian CRES (Cystatin-Related Epididymal Spermatogenic) Amyloid is Antiparallel β-Sheet Rich and Forms a Metastable Oligomer During Assembly.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Altered Brain Extracellular Matrix Structure and Sex-Specific Learning/Memory Dysfunction in Mice Lacking the Functional Amyloid Cystatin-Related Epididymal Spermatogenic (CRES).bioRxiv : the preprint server for biology · 2026Article
- DNA Modulates Structural Transitions and Oligomerization Kinetics of the Functional Amyloid CRES.Journal of the American Chemical Society · 2026Article
- Host defense functions of the epididymal amyloid matrix.Molecular human reproduction · 2022Article
- Differential gene expression and hallmarks of stemness in epithelial cells of the developing rat epididymis.Cell and tissue research · 2022Article
- Maturation of the functional mouse CRES amyloid from globular form.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cross-seeding between the functional amyloidogenic CRES and CRES3 family members and their regulation of Aβ assembly.The Journal of biological chemistryArticle
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
An amyloid matrix composed of several family 2 cystatins, including the reproductive cystatin CRES, is an integral structure in the mouse epididymal lumen and has proposed functions in sperm maturation and protection. Understanding how CRES amyloid assembles in vitro may provide clues on how the epididymal amyloid matrix forms in vivo. We therefore purified full-length CRES under nondenaturing conditions and followed its aggregation from monomer to amyloid under conditions that may approximate those in the epididymal lumen. CRES transitioned into a metastable oligomer that was resistant to aggregation and only over extended time formed higher-ordered amyloids. High protein concentrations facilitated oligomer assembly and also were required to maintain the metastable state since following dilution the oligomer was no longer detected. Similar to other amyloid precursors, the formation of CRES amyloids correlated with a loss of α-helix and a gain of β-sheet content. However, CRES is unique in that its amyloids are rich in antiparallel β-sheets instead of the more common parallel β-sheets. Taken together, our studies suggest that early metastable oligomers may serve as building blocks for functional amyloid assembly and further reveal that antiparallel β-sheet-rich amyloids can be functional forms.
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Registered trials
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