scholarly journals Morphogenesis of Light and Electron Microscopic Lesions in Porcine GM2-Gangliosidosis

1979 ◽  
Vol 16 (1) ◽  
pp. 6-17 ◽  
Author(s):  
S. D. Kosanke ◽  
K. R. Pierce ◽  
W. K. Read
Keyword(s):  
Glial Cells ◽  
Inclusion Bodies ◽  
Cytoplasmic Inclusion ◽  
Particulate Material ◽  
Electron Microscopic ◽  
Cytoplasmic Body ◽  
Cytoplasmic Inclusions ◽  
Neuronal Inclusions ◽  
Cytoplasmic Inclusion Bodies ◽  
Cytoplasmic Structures

The neurons and glial cells of 1- to 140-day-old pigs with GM2-gangliosidosis had membranous cytoplasmic inclusion bodies. These bodies appeared as small vacuolated cytoplasmic structures in paraffin-embedded, hematoxylin and eosin-stained sections and as solid, dark, round granules in 1-micrometer sections embedded in plastic and stained with toluidine blue. Ultrastructurally, the cytoplasmic inclusion bodies appeared as round, dense structures from 0.6 to 1.2 micrometers in diameter, that were filled with various amounts of small to large arrays of membranous lamellae. The cortical neuronal inclusions were seen initially as lysosomes containing a small amount of particulate material. The appearance of these inclusions changed as they progressed through different configurational stages. Inclusions resembled the granulomembranous body, the zebra body, possibly other intermediate forms and, finally, the classical membranous cytoplasmic body. The cytoplasmic inclusions in glial cells resembled membranovesicular bodies and, although also of apparent lysosomal origin, were morphologically different from the neuronal inclusions. The morphologic lesions in the neurons and glial cells of the affected pigs were similar to those described for human gangliosidoses.

Cytoplasmic inclusion bodies in familial dilated cardiomyopathy

1995 ◽  
Vol 53 ◽  
pp. 1000-1001
Author(s):  
W.T. Gunning ◽  
A.F. Gohara ◽  
T.E. Walsh ◽  
E.P. Calomeni
Keyword(s):  
Inclusion Bodies ◽  
Cytoplasmic Inclusion ◽  
Severe Congestive Heart Failure ◽  
Cardiac Transplant ◽  
Light Microscopic Level ◽  
Electron Microscopic ◽  
Familial Dilated Cardiomyopathy ◽  
Pas Staining ◽  
Cytoplasmic Inclusion Bodies ◽  
Band Material

A thirty-six year old male with severe congestive heart failure was given a cardiac transplant. The findings of the evaluation of his native heart is the basis for this presentation. Our findings included the identification of unusual cytoplasmic inclusion bodies found throughout the heart. These inclusions, found most often in a perinuclear location, were eosinophilic and crystalloid at the light microscopic level (Figure 1.). Special histologic stains were not supportive of a diagnosis of nemaline rod disease as a trichrome stain failed to differentiate inclusions from surrounding cytoplasm, yet could be accomplished with PAS staining (Figure 2.) . Furthermore, the ultrastructural morphology of the inclusions did not show any similarity to z-band material, the electron microscopic characteristic of inclusion bodies in nemaline rod myopathy. The shape of these bodies was usually rectangular or elliptical (Figure 3.) and size was found to be quite variable, some measured in excess of 15μ X 4μ. Other characteristics included an amorphous appearance with occasional electron densities within the inclusions (Figure 3), an apparent single limiting membrane (Figure 3 and 4), and for some of the inclusions, there was a suggestion of secondary lysosomal association (Figure 4).

Abstract 4: Macrophage p62/SQSTM1 Ameliorates Atherosclerosis by Sequestering Inclusion Bodies and Mediating Mitophagy

2015 ◽  
Vol 35 (suppl_1) ◽  
Author(s):  
Ismail Sergin ◽  
Somashubhra Bhattacharya ◽  
Carl J Stokes ◽  
John A Curci ◽  
Babak Razani
Keyword(s):  
Inclusion Bodies ◽  
Cytoplasmic Inclusion ◽  
Protein Aggregates ◽  
Whole Body ◽  
Plaque Burden ◽  
Protein Accumulation ◽  
Inflammasome Activation ◽  
Cytoplasmic Inclusions ◽  
Cytoplasmic Inclusion Bodies

Protein and organelle turnover is critical for cellular homeostasis and is prominently mediated by autophagy. Disruptions in autophagy lead to accumulation of protein aggregates and dysfunctional organelles such as mitochondria. Recent evidence suggests that the chaperone protein p62 is a critical link for targeting polyubiquitinated protein aggregates/damaged mitochondria to autophagosomes for degradation. Herein we describe a p62-centric mechanism of handling protein aggregates and dysfunctional mitochondria in atherosclerosis. Macrophages deficient in autophagy (ATG5-/-) or rendered deficient by incubation with atherogenic lipids have significantly increased levels of p62. This coincides with 1) the accumulation of polyubiquitinated proteins co-localizing with p62 and present as cytoplasmic inclusion bodies, and 2) p62 co-localization with mitochondrial markers. Aortas from atherosclerotic (ApoE-/-) mice also have progressive and marked elevations in p62, polyubiquitinated proteins, and mitochondrial reactive oxygen species that predominantly co-localize with plaque macrophages, a process further exacerbated in the autophagy-deficient setting. The formation of cytoplasmic inclusions and maintenance of adequate mitochondrial function appears to be dependent on p62. Lipid-loaded p62-null macrophages show polyubiquitinated protein accumulation present in a diffuse/disrupted cytoplasmic pattern. These macrophages also develop larger dysmorphic mitochondria with increased polarization and decreased oxidative phosphorylation capacity. As a result, p62-null macrophages display apoptotic susceptibility to atherogenic lipids and increased IL-1β secretion likely through mitochondrial-dependent inflammasome activation. Consistent with our in vitro observations, mice with either whole-body p62-deficiency or transplanted with p62-deficient bone marrow show significantly increased atherosclerotic plaque burden and lesion complexity with increased apoptosis and necrotic cores. Taken together, these data demonstrate a previously unrecognized atheroprotective role for macrophage p62 by facilitating the formation of inclusion bodies and maintaining healthy mitochondria.

Molecular diagnosis of avian nephritis: Preliminary report

2006 ◽  
Vol 54 (1) ◽  
pp. 51-60 ◽  
Author(s):  
Míra Mándoki ◽  
M. Dobos-Kovács ◽  
T. Bakonyi ◽  
M. Rusvai
Keyword(s):  
Inclusion Bodies ◽  
Direct Sequencing ◽  
Cytoplasmic Inclusion ◽  
Electron Microscopic Examination ◽  
Electron Microscopic ◽  
Pcr Product ◽  
Avian Nephritis Virus ◽  
Cytoplasmic Inclusion Bodies ◽  
Pcr Method ◽  
Potential Tool

Kidney samples from chickens diagnosed with acute nephritis and gout were subjected to histological and electron microscopic examination. The investigations revealed cytoplasmic inclusion bodies in the tubular epithelial cells containing round virions of about 30 nm in diameter. Since avian nephritis virus (ANV) is known as a potential causative agent of the so-called baby chick nephropathy, an RT-PCR assay was developed for the molecular detection of ANV-specific nucleic acid in the specimen. The specificity of the assay was confirmed by direct sequencing of the amplicon obtained in the reaction. The nucleotide sequence of the PCR product showed 92% identity with the reference ANV sequence deposited in the GenBank database. After having been validated on some other suspicious cases of avian nephritis, the PCR method described in this study can be a potential tool for routine diagnostic examination of samples submitted from cases of gout and nephropathy in chickens.

scholarly journals Searching for the cause of Kawasaki disease — cytoplasmic inclusion bodies provide new insight

2008 ◽  
Vol 6 (5) ◽  
pp. 394-401 ◽  
Author(s):  
Anne H. Rowley ◽  
Susan C. Baker ◽  
Jan M. Orenstein ◽  
Stanford T. Shulman
Keyword(s):  
Kawasaki Disease ◽  
Inclusion Bodies ◽  
Cytoplasmic Inclusion ◽  
Cytoplasmic Inclusion Bodies
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