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Amyloids assemble as part of recognizable structures during oogenesis in Xenopus.

Hayes MH, Weeks DL - Biol Open (2016)

Bottom Line: A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state.There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic.In the nucleus, we find particles associated with transcription by RNA polymerase I, II and III and RNA processing contain amyloids.

View Article: PubMed Central - PubMed

Affiliation: Molecular and Cellular Biology Program, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA Medical Scientist Training Program, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.

No MeSH data available.


Related in: MedlinePlus

Nuclear particles in isolated Xenopus nuclei (GVs) have overlapping but distinctive reactivity to amyloid detecting antibodies and thio-T. Isolated GVs were examined using an anti-oligomeric amyloid antibody A11 and particle identifying antibodies. Panel (A) shows a low magnification view of a GV using A11 (green) and anti-nucleolin (red) antibodies. Arrows point to some of the many nucleolin negative, A11 positive particles. (B-E) are higher magnification images of a single nucleolus with (B) representing the composite of (C) anti-nucleolin (red), (D) A11 antibody (green) and (E) anti-dsDNA (blue) staining. The arrowhead points to an A11 positive sub structure. Scale bars (A) 500µm and (B-E) 10µm. Coilin positive particles, histone locus bodies (F-G) and pearls (H-I) are shown as overlays of coilin (red) and A11 (green) in (F and H). The A11 signal of the histone locus body (G) is higher than that of the pearl (I). Scale bars: 5µm. The composite image of A11 and anti-SC35 used to detect speckles in (J) highlights the variable intensity of the A11 signals. In (J) speckles with low A11 signal are indicated with arrowheads and those with more robust A11 signal with arrows. Scale bar: 50μm.
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BIO017384F3: Nuclear particles in isolated Xenopus nuclei (GVs) have overlapping but distinctive reactivity to amyloid detecting antibodies and thio-T. Isolated GVs were examined using an anti-oligomeric amyloid antibody A11 and particle identifying antibodies. Panel (A) shows a low magnification view of a GV using A11 (green) and anti-nucleolin (red) antibodies. Arrows point to some of the many nucleolin negative, A11 positive particles. (B-E) are higher magnification images of a single nucleolus with (B) representing the composite of (C) anti-nucleolin (red), (D) A11 antibody (green) and (E) anti-dsDNA (blue) staining. The arrowhead points to an A11 positive sub structure. Scale bars (A) 500µm and (B-E) 10µm. Coilin positive particles, histone locus bodies (F-G) and pearls (H-I) are shown as overlays of coilin (red) and A11 (green) in (F and H). The A11 signal of the histone locus body (G) is higher than that of the pearl (I). Scale bars: 5µm. The composite image of A11 and anti-SC35 used to detect speckles in (J) highlights the variable intensity of the A11 signals. In (J) speckles with low A11 signal are indicated with arrowheads and those with more robust A11 signal with arrows. Scale bar: 50μm.

Mentions: Nuclear particles were probed with anti-amyloid antibodies. Indirect immunofluorescence detection of nucleolin (red) and oligomeric amyloid (A11 antibody, green) confirmed that nucleolin positive particles contain oligomeric amyloid (Fig. 3A, overlay of treatments yellow/orange). A triple antibody-stained nucleolus (Fig. 3B) and isolated images provide a closer view of the arrangement of nucleolin (red, Fig. 3C), amyloid (green, Fig. 3D) and dsDNA (blue, Fig. 3E). A smaller amyloid positive but nucleolin and dsDNA negative particle was associated with the nucleolus (arrowhead, Fig. 3B-E), demonstrating the ability to differentiate sub-nuclear organelles with our protocol.Fig. 3.


Amyloids assemble as part of recognizable structures during oogenesis in Xenopus.

Hayes MH, Weeks DL - Biol Open (2016)

Nuclear particles in isolated Xenopus nuclei (GVs) have overlapping but distinctive reactivity to amyloid detecting antibodies and thio-T. Isolated GVs were examined using an anti-oligomeric amyloid antibody A11 and particle identifying antibodies. Panel (A) shows a low magnification view of a GV using A11 (green) and anti-nucleolin (red) antibodies. Arrows point to some of the many nucleolin negative, A11 positive particles. (B-E) are higher magnification images of a single nucleolus with (B) representing the composite of (C) anti-nucleolin (red), (D) A11 antibody (green) and (E) anti-dsDNA (blue) staining. The arrowhead points to an A11 positive sub structure. Scale bars (A) 500µm and (B-E) 10µm. Coilin positive particles, histone locus bodies (F-G) and pearls (H-I) are shown as overlays of coilin (red) and A11 (green) in (F and H). The A11 signal of the histone locus body (G) is higher than that of the pearl (I). Scale bars: 5µm. The composite image of A11 and anti-SC35 used to detect speckles in (J) highlights the variable intensity of the A11 signals. In (J) speckles with low A11 signal are indicated with arrowheads and those with more robust A11 signal with arrows. Scale bar: 50μm.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4920187&req=5

BIO017384F3: Nuclear particles in isolated Xenopus nuclei (GVs) have overlapping but distinctive reactivity to amyloid detecting antibodies and thio-T. Isolated GVs were examined using an anti-oligomeric amyloid antibody A11 and particle identifying antibodies. Panel (A) shows a low magnification view of a GV using A11 (green) and anti-nucleolin (red) antibodies. Arrows point to some of the many nucleolin negative, A11 positive particles. (B-E) are higher magnification images of a single nucleolus with (B) representing the composite of (C) anti-nucleolin (red), (D) A11 antibody (green) and (E) anti-dsDNA (blue) staining. The arrowhead points to an A11 positive sub structure. Scale bars (A) 500µm and (B-E) 10µm. Coilin positive particles, histone locus bodies (F-G) and pearls (H-I) are shown as overlays of coilin (red) and A11 (green) in (F and H). The A11 signal of the histone locus body (G) is higher than that of the pearl (I). Scale bars: 5µm. The composite image of A11 and anti-SC35 used to detect speckles in (J) highlights the variable intensity of the A11 signals. In (J) speckles with low A11 signal are indicated with arrowheads and those with more robust A11 signal with arrows. Scale bar: 50μm.
Mentions: Nuclear particles were probed with anti-amyloid antibodies. Indirect immunofluorescence detection of nucleolin (red) and oligomeric amyloid (A11 antibody, green) confirmed that nucleolin positive particles contain oligomeric amyloid (Fig. 3A, overlay of treatments yellow/orange). A triple antibody-stained nucleolus (Fig. 3B) and isolated images provide a closer view of the arrangement of nucleolin (red, Fig. 3C), amyloid (green, Fig. 3D) and dsDNA (blue, Fig. 3E). A smaller amyloid positive but nucleolin and dsDNA negative particle was associated with the nucleolus (arrowhead, Fig. 3B-E), demonstrating the ability to differentiate sub-nuclear organelles with our protocol.Fig. 3.

Bottom Line: A hallmark of Alzheimer's, Huntington's and similar diseases is the assembly of proteins into amyloids rather than folding into their native state.There is an increasing appreciation that amyloids, under specific conditions, may be non-pathogenic.In the nucleus, we find particles associated with transcription by RNA polymerase I, II and III and RNA processing contain amyloids.

View Article: PubMed Central - PubMed

Affiliation: Molecular and Cellular Biology Program, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA Medical Scientist Training Program, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.

No MeSH data available.


Related in: MedlinePlus