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Eosinophilic Inclusions (eosinophilic + inclusion)

Distribution by Scientific Domains

Medical Sciences	75%

Selected Abstracts

An intranuclear bacilliform virus associated with near extirpation of Austropotamobius pallipes Lereboullet from the Nant watershed in Ardéche, France

JOURNAL OF FISH DISEASES, Issue 9 2002
B F Edgerton
White-clawed crayfish, Austropotamobius pallipes, were endemic to the Nant watershed, Ardéche, France, until they were extirpated by epizootic mortality at the beginning of the twentieth century. A. pallipes were successfully reintroduced to the Nant watershed in the middle of the twentieth century. However, epizootic mortality was observed in the Nant watershed in the summer of 2000 during which time A. pallipes was extirpated from downstream regions. Dead and moribund crayfish were again detected in several episodes in summer 2001 and by October the range of A. pallipes was reduced to the headwaters of just one of the three streams in the watershed. Water quality for the watershed in summer 2001 was appropriate for crayfish habitation. Bacteriology and mycology on A. pallipes collected during several of the mortality episodes in 2001 failed to reveal a cause. However, histopathology revealed a high occurrence of intranuclear eosinophilic inclusions in hepatopancreatocytes of A. pallipes. The nuclei were hypertrophic and contained bacilliform virions consisting of a cylindrical nucleocapsid surrounded by a trilaminar envelope. Virions in section were approximately 63 × 258 nm and nucleocapsids were approximately 52 × 225 nm. It is unclear whether the intranuclear bacilliform virus was the cause of the mortality episodes or was a contributor to a disease complex involving one or several other undetected pathogens. [source]

Involvement of spinal motor neurons in parkin-positive autosomal recessive juvenile parkinsonism

NEUROPATHOLOGY, Issue 1 2008
Shoichi Sasaki
We intensively examined the spinal cord of an autosomal recessive juvenile parkinsonism (ARJP) female patient with a homozygous exon 3 deletion in the parkin gene, anticipating a possible involvement of anterior horn neurons. Although the clinical features of the patient were consistent with parkinsonism as a result of parkin mutation, her tendon reflex was abolished in the lower limbs. This feature was in contrast with hyperreflexia, usually found in previous reports of ARJP. Histologically, on the level of the cervical, thoracic, and sacral spinal cord, anterior horn neurons were well preserved and normal. However, the lumbar spinal cord exhibited many swellings of proximal axons (spheroids) and degenerative changes in the somata of the large anterior horn neurons such as central chromatolysis, cystatin C-negative small eosinophilic inclusions, and eosinophilic Lewy body-like inclusions. Ultrastructurally, accumulations of neurofilaments and abnormal structures, such as inclusion bodies similar to skein-like inclusions and disorganized rough endoplasmic reticulum, were observed in the somata and neuronal processes. Lewy body-like inclusions in this study were positively immunostained for both ,-synuclein and ubiquitin that closely resemble Lewy bodies, but are different from Lewy body-like inclusions negatively immunostained for ,-synuclein in amyotrophic lateral sclerosis. These findings suggest that eosinophilic inclusions that closely resemble Lewy bodies may be formed in the spinal motor neurons of ARJP patients with parkin mutations and the motor neurons of these patients may be vulnerable to neurodegeneration. [source]

Involvement of Clusterin and the Aggresome in Abnormal Protein Deposits in Myofibrillar Myopathies and Inclusion Body Myositis

BRAIN PATHOLOGY, Issue 2 2005
I. Ferrer
Myofibrillar myopathies (MM) are characterized morphologically by the presence of non-hyaline structures corresponding to foci of dissolution of myofibrils, and hyaline lesions composed of aggregates of compacted and degraded myofibrillar elements. Inclusion body myositis (IBM) is characterized by the presence of rimmed vacuoles, eosinophilic inclusions in the cytoplasm, rare intranuclear inclusions, and by the accumulation of several abnormal proteins. Recent studies have demonstrated impaired proteasomal expression and activity in MM and IBM, thus accounting, in part, for the abnormal protein accumulation in these diseases. The present study examines other factors involved in protein aggregation in MM and IBM. Clusterin is a multiple-function protein which participates in A,-amyloid, PrPres and ,-synuclein aggregation in Alzheimer disease, prionopathies and ,-synucleinopathies, respectively. ,-Tubulin is present in the centrosome and is an intracellular marker of the aggresome. Moderate or strong clusterin immunoreactivity has been found in association with abnormal protein deposits, as revealed by immunohistochemistry, single and double-labeling immunofluorescence and confocal microscopy, in MM and IBM, and in target structures in denervation atrophy. ,-Tubulin has also been observed in association with abnormal protein deposits in MM, IBM, and in target fibers in denervation atrophy. These morphological findings are accompanied by increased expression of clusterin and ,-tubulin in muscle homogenates of MM and IBM cases, as revealed by gel electrophoresis and Western blots. Together, these observations demonstrate involvement of clusterin in protein aggregates, and increased expression of aggresome markers in association with abnormal protein inclusions in MM and IBM and in targets, as crucial events related with the pathogenesis of abnormal protein accumulation and degradation in these muscular diseases. [source]