ArticleScientific reports2015
Chemical-Free Technique to Study the Ultrastructure of Primary Cilium.
Article in Scientific reports, 2015. 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.
- Six Decades of History of Hypertension Research at the University of Toledo: Highlighting Pioneering Contributions in Biochemistry, Genetics, and Host-Microbiota Interactions.Current hypertension reports · 2022Review
- Primary cilium: a paradigm for integrating mathematical modeling with experiments and numerical simulations in mechanobiology.Mathematical biosciences and engineering : MBE · 2021Article
- Proteomic Identification Reveals the Role of Ciliary Extracellular-Like Vesicle in Cardiovascular Function.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Primary cilia have a length-dependent persistence length.Biomechanics and modeling in mechanobiology · 2020Article
- The transition structure of chromatin fibers at the nanoscale probed by cryogenic electron tomography.Nanoscale · 2019Article
- HIF Stabilization Weakens Primary Cilia.PloS one · 2016Article
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Authors and funding
4 authors.
Funding
Abstract
A primary cilium is a hair-like structure with a width of approximately 200 nm. Over the past few decades, the main challenge in the study of the ultrastructure of cilia has been the high sensitivity of cilia to chemical fixation, which is required for many imaging techniques. In this report, we demonstrate a combined high-pressure freezing (HPF) and freeze-fracture transmission electron microscopy (FFTEM) technique to examine the ultrastructure of a cilium. Our objective is to develop an optimal high-resolution imaging approach that preserves cilia structures in their best natural form without alteration of cilia morphology by chemical fixation interference. Our results showed that a cilium has a swelling-like structure (termed bulb), which was previously considered a fixation artifact. The intramembrane particles observed via HPF/FFTEM indicated the presence of integral membrane proteins and soluble matrix proteins along the ciliary bulb, which is part of an integral structure within the ciliary membrane. We propose that HPF/FFTEM is an important and more suitable chemical-free method to study the ultrastructure of primary cilia.
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