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PubMed1978

Subacute sclerosing panencephalitis with special reference to the ultrastructure of inclusions in the brain and lung.

A 7-year-old boy, who was diagnosed as typical SSPE by clinical data and laboratory findings, was autopsied and observed by immunofluorescent techniques, light and electron microscope. The morphological characteristics in the brain were perivascular cuffings with plasma cells, lymphocytes and mononuclear cells, gliosis and a large number of intranuclear and intracytoplasmic inclusions in the neuroglias and nerve cells. Various kinds of intranuclear inclusions were elucidated by electron microscopy and the fin structures of these inclusions were described in detail. At least five types of intranuclear inclusions were regarded as specific in SSPE. The presence of intranuclear inclusions of mononuclear cells in the lungs resembling the inclusions in the neuroglias suggested that the disease was not localized in the brain but could be disseminated throughout the body.

Brain↗
PubMed1991

Are bunina bodies of endoplasmic reticulum origin? An ultrastructural study of subthalamic eosinophilic inclusions in a case of atypical motor neuron disease.

We carried out an electron microscopic study of eosinophilic intracytoplasmic inclusions in the subthalamic neurons in a case of atypical motor neuron disease. These inclusions were identical in light microscopic morphology and staining characteristics to Bunina bodies. Ultrastructurally, most of the intracytoplasmic inclusions observed were divisible into two different types (I and II). Type I inclusions had features essentially identical to those of Bunina bodies demonstrated previously in the anterior horn cells in cases of motor neuron disease; they consisted of electron-dense, granular material without a particular limiting membrane and often contained a number of translucent areas with entrapped cell organelle-like structures. Type II inclusions were very similar to structures known as multilaminated bodies; at their margin, they sometimes showed continuity with the cisternae of endoplasmic reticulum. The remainder of the inclusions were considered to be transitional forms between these two types, and some of them showed the respective features of both types I and II. These findings suggest that Bunina bodies are of endoplasmic reticulum origin.

Adult↗
PubMed1995

Ubiquitinated cytokeratin inclusions in lichen amyloidosus: an immunohistochemical analysis.

Eosinophilic hyaline inclusions were consistently seen in the perinuclear cytoplasm of suprabasal keratinocytes in lichen amyloidosus. The inclusions, negative with amyloid staining, were immunoreactive for ubiquitin and cytokeratin, and ultrastructurally showed aggregations of fine filaments of two sizes (central thin and peripheral thick). The thin filaments were the main component in the upper epidermal layer. Four monoclonal antibodies (AE1, AE3, KL1 and CAM5.2) and one antiserum (WSS) were used for characterizing cytokeratin expression. The AE1 antibody normally stained the basal cells, but in lichen amyloidosus basal staining mostly disappeared. Instead, groups of suprabasal keratinocytes were labeled, with AE1-reactive inclusions distributed therein. In contrast, the KL1 antibody, showing suprabasal staining, failed to react with the inclusions. The inclusions were weakly reactive with the AE3 and WSS antibodies, which stained all keratinocytes. The CAM5.2 antibody was unreactive. The subepidermal amyloid deposits were negative with all the antibodies. The inclusions were ubiquitinated especially in the granular layer. Immunoelectron microscopy disclosed that ubiquitin was more densely localized in the thin filaments than in the thick ones. This indicated that cytokeratin expression and metabolism are altered in the affected epidermis, and that ubiquitin functions in the process of degradation of abnormal cytokeratin filaments.

Adolescent↗
PubMed1998

Localization of identified advanced glycation end-product structures, N epsilon(carboxymethyl)lysine and pentosidine, in age-related inclusions in human brains.

The recent identification of age-related accumulation of advanced glycation end-products (AGE) of the Maillard reaction in neurons and vessels of the human brain suggests the involvement of AGE in the aging process. A variety of inclusions such as lipofuscin granules, corpora amylacea, Hirano bodies, granulovacuolar degenerations and ubiquitin-positive granular structures are found in the aged human brain. These age-related inclusions contain insoluble and non-degradable proteins. Advanced glycation end-product-modified proteins are also known to be insoluble and protease resistant. The similarity between proteins in such inclusions and AGE-modified proteins suggests the presence of AGE in inclusions. To investigate this possibility, the presence of two known AGE structures, N epsilon(carboxymethyl)lysine (CML) and pentosidine, was examined in age-related inclusions. Immunohistochemical examination of the medial temporal area of brain tissues obtained at autopsy from seven non-demented elderly individuals demonstrated positive reactions in lipofuscin granules and corpora amylacea but not in other inclusions for anti-CML and anti-pentosidine antibodies. As CML and pentosidine are glycoxidation products among AGE, the results suggest that glycation and/or oxidation may be involved in the formation of lipofuscin granules and corpora amylacea.

Aged↗
PubMed1994

Cytokeratin inclusions in alcoholic liver disease and their relation to the amount of alcohol intake.

In the present study, the frequency and the distribution pattern of immunoreactive hepatocytic cytokeratin (CK) inclusions was investigated using the monoclonal antibody (MAb) CAM 5.2 detecting CKs 8, 18 and 19. The CK antigenicity of the inclusions was confirmed on frozen sections with MAbs for the CKs 7, 8, 17, 18 and 19. The frequency of hepatocytic CK aggregates was compared to the presence of non-alcoholic and alcoholic liver disease (ALD) as well as to the average all-year daily ethanol intake of 195 consecutive males subjected to medico-legal autopsy. Hepatocytic CK inclusions were infrequent in patients with normal liver histology, portal fibrosis and/or portal inflammation. In ALD, however, inclusions were observed in 35.6% of patients with fatty liver, in 63.2% of patients with alcoholic hepatitis, in 30.8% of patients with bridging fibrosis and in 60.0% of patients with liver cirrhosis. In all specimens studied, the inclusions were reactive only for CKs 8 and 18, CKs 7, 17, and 19 being unreactive. The frequency of inclusion bodies increased, paralleling increasing average all-year daily alcohol consumption. Compared to non-drinkers, a daily intake of between 40 and 80 g of absolute alcohol was associated with a statistically significantly (relative risk, RR = 6.6) increased risk of formation of aggregates. Similarly, daily consumption exceeding 80 g was related to increased (RR = 6.0) frequency of CK aggregates. The frequency of full-blown "classical" Mallory bodies (MBs) was, however, increased (RR = 8.9) only in patients with a daily intake exceeding 160 g.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1984

Nuclear and cytoplasmic inclusion bodies in pinealocytes of the cotton rat, Sigmodon bispidus: an electron microscopic study.

Electron microscopic observations on pinealocytes of cotton rats (Sigmodon bispidus) killed in October revealed the presence of cytoplasmic inclusion bodies (CIBs) and two kinds of nuclear inclusions--coiled bodies and granular inclusion bodies. These inclusions were usually not bounded by a membrane. CIBs showed round or irregular profiles and consisted of granular and filamentous materials of moderate electron opacity intermingled with electron-lucent areas. Nuclear granular inclusions appeared as homogeneous or heterogeneous granules of variable electron opacity, which usually exhibited round profiles of variable diameters and consisted of granular and filamentous elements. Electron-opaque granules were observed in perinuclear spaces, dilated cisternae of rough endoplasmic reticulum, as well as in the central portion of CIBs. In CIBs containing granules, the peripheral region was composed of the moderately electron-opaque substance seen in usual CIBs, while the central core was occupied by a granular and filamentous substance and an intervening electron-lucent matrix. Since an electron-opaque granular substance in nuclei, perinuclear spaces, cisternae of rough endoplasmic reticulum, and the central portion of CIBs may occur concomitantly, the granules seen in these sites may be related. Coiled bodies were round in profile and were composed of electron-opaque strands consisting of granular and filamentous elements and intervening material of low electron opacity. This structure, frequently located in close proximity to the nuclear granular inclusions, may play a role in the formation of the intranuclear granules in cotton rat pinealocytes.

Animals↗
PubMed2006

Huntingtin inclusion bodies are iron-dependent centers of oxidative events.

Recently, we reported that the transient expression of huntingtin exon1 polypeptide containing polyglutamine tracts of various sizes (httEx1-polyQ) in cell models of Huntington disease generated an oxidative stress whose intensity was CAG repeat expansion-dependent. Here, we have analyzed the intracellular localization of the oxidative events generated by the httEx1-polyQ polypeptides. Analysis of live COS-7 cells as well as neuronal SK-N-SH and PC12 cells incubated with hydroethidine or dichlorofluorescein diacetate revealed oxidation of these probes at the level of the inclusion bodies formed by httEx1-polyQ polypeptides. The intensity and frequency of the oxidative events among the inclusions were CAG repeat expansion-dependent. Electron microscopic analysis of cell sections revealed the presence of oxidation-dependent morphologic alterations in the vicinity of httEx1-polyQ inclusion bodies. Moreover, a high level of oxidized proteins was recovered in partially purified inclusions. We also report that the iron chelator deferroxamine altered the structure, localization and oxidative potential of httEx1-polyQ inclusion bodies. Hence, despite the fact that the formation of inclusion bodies may represent a defense reaction of the cell to eliminate httEx1 mutant polypeptide, this phenomenon appears inherent to the generation of iron-dependent oxidative events that can be deleterious to the cell.

Acetylcysteine↗
PubMed2006

Eukaryotic lipid body proteins in oleogenous actinomycetes and their targeting to intracellular triacylglycerol inclusions: Impact on models of lipid body biogenesis.

Bacterial neutral lipid inclusions are structurally related to eukaryotic lipid bodies. These lipid inclusions are composed of a matrix of triacylglycerols (TAGs) or wax esters surrounded by a monolayer of phospholipids. Whereas the monolayers of lipid bodies from animal and plant cells harbor specific classes of proteins which are involved in the structure of the inclusions and lipid homoestasis, no such proteins are known to be associated with bacterial lipid inclusions. The present study was undertaken to reveal whether the mammalian lipid body proteins perilipin A, adipose differentiation-related protein, and tail-interacting protein of 47 kDa (TIP47), which comprise the so called PAT family proteins, and the maize (Zea mays L.) oleosin are targeted to prokaryotic TAG bodies in vivo. When fused to enhanced green fluorescent protein, all proteins except the oleosin were mainly located at the surfaces of lipid inclusions when heterologously expressed in the recombinant actinomycetes Rhodococcus opacus PD630 and Mycobacterium smegmatis mc(2)155. A more detailed intracellular distribution analysis of TIP47 in recombinant R. opacus cells by immunocytochemical labeling of ultrathin cryosections and freeze fracture replicas revealed a substantial amount of TIP47 protein also pervading the cores of the inclusions. We discuss the impact of these results on the current model of lipid body biogenesis in prokaryotes.

Actinobacteria↗
PubMed2001

Isolation and characterization of intracellular protein inclusions produced by the entomopathogenic bacterium Photorhabdus luminescens.

Cells of the entomopathogenic bacterium Photorhabdus luminescens contain two types of morphologically distinct crystalline inclusion proteins. The larger rectangular inclusion (type 1) and a smaller bipyramid-shaped inclusion (type 2) were purified from cell lysates by differential centrifugation and isopycnic density gradient centrifugation. Both structures are composed of protein and are readily soluble at pH 11 and 4 in 1% sodium dodecyl sulfate (SDS) and in 8 M urea. Electrophoretic analysis reveals that each inclusion is composed of a single protein subunit with a molecular mass of 11,000 Da. The proteins differ in amino acid composition, protease digestion pattern, and immunological cross-reactivity. The protein inclusions are first visible in the cells at the time of late exponential growth. Western blot analyses showed that the proteins appeared in cells during mid- to late exponential growth. When at maximum size in stationary-phase cells, the proteins constitute 40% of the total cellular protein. The protein inclusions are not used during long-term starvation of the cells and were not toxic when injected into or fed to Galleria mellonella larvae.

Animals↗
PubMed2001

Reovirus sigmaNS protein is required for nucleation of viral assembly complexes and formation of viral inclusions.

Progeny virions of mammalian reoviruses are assembled in the cytoplasm of infected cells at discrete sites termed viral inclusions. Studies of temperature-sensitive (ts) mutant viruses indicate that nonstructural protein sigmaNS and core protein mu2 are required for synthesis of double-stranded (ds) RNA, a process that occurs at sites of viral assembly. We used confocal immunofluorescence microscopy and ts mutant reoviruses to define the roles of sigmaNS and mu2 in viral inclusion formation. In cells infected with wild-type (wt) reovirus, sigmaNS and mu2 colocalize to large, perinuclear structures that correspond to viral inclusions. In cells infected at a nonpermissive temperature with sigmaNS-mutant virus tsE320, sigmaNS is distributed diffusely in the cytoplasm and mu2 is contained in small, punctate foci that do not resemble viral inclusions. In cells infected at a nonpermissive temperature with mu2-mutant virus tsH11.2, mu2 is distributed diffusely in the cytoplasm and the nucleus. However, sigmaNS localizes to discrete structures in the cytoplasm that contain other viral proteins and are morphologically indistinguishable from viral inclusions seen in cells infected with wt reovirus. Examination of cells infected with wt reovirus over a time course demonstrates that sigmaNS precedes mu2 in localization to viral inclusions. These findings suggest that viral RNA-protein complexes containing sigmaNS nucleate sites of viral replication to which other viral proteins, including mu2, are recruited to commence dsRNA synthesis.

Animals↗
PubMed2003

The ND10 component promyelocytic leukemia protein relocates to human papillomavirus type 1 E4 intranuclear inclusion bodies in cultured keratinocytes and in warts.

Human papillomavirus type 1 (HPV1) E4 protein is associated with cytoplasmic and nuclear inclusions in productively infected keratinocytes. Here we have used transient expression of HPV1 E4 (also known as E1E4) protein in keratinocytes to reproduce formation of E4 inclusions. Immunofluorescence analysis showed that progressive formation of inclusions correlated with diminished colocalization between E4 and keratin intermediate filaments (IFs). Our results support a model in which the HPV1 E4-keratin IF association is transient, occurring only at an early stage of inclusion formation. We also demonstrate that E4 induces relocation of the promyelocytic leukemia protein (PML) from multiple intranuclear speckles (ND10 bodies) to the periphery of nuclear E4 inclusions and that this activity is specific to full-length E4 protein. Analysis of HPV1-induced warts demonstrated that nuclear PML-E4 inclusions were present in productively infected keratinocytes, indicating that reorganization of PML occurs during the virus's replication cycle. It has been suggested that ND10 bodies are the sites for papillomavirus genome replication and virion assembly. Our finding that E4 induces reorganization of ND10 bodies in vitro and in vivo is further strong evidence that these domains play an important role in the papillomavirus life cycle. This study indicates that HPV1 is analogous to other DNA viruses that disrupt or reorganize ND10 domains, possibly to increase efficiency of virus infection. We hypothesize that HPV1 E4-induced reorganization of PML is necessary for efficient replication of the virus during the virus-producing phase.

Cells, Cultured↗
PubMed2003

Reovirus sigma NS and mu NS proteins form cytoplasmic inclusion structures in the absence of viral infection.

Reovirus replication occurs in the cytoplasm of infected cells and culminates in the formation of crystalline arrays of progeny virions within viral inclusions. Two viral nonstructural proteins, sigma NS and micro NS, and structural protein sigma 3 form protein-RNA complexes early in reovirus infection. To better understand the minimal requirements of viral inclusion formation, we expressed sigma NS, mu NS, and sigma 3 alone and in combination in the absence of viral infection. In contrast to its concentration in inclusion structures during reovirus replication, sigma NS expressed in cells in the absence of infection is distributed diffusely throughout the cytoplasm and does not form structures that resemble viral inclusions. Expressed sigma NS is functional as it complements the defect in temperature-sensitive, sigma NS-mutant virus tsE320. In both transfected and infected cells, mu NS is found in punctate cytoplasmic structures and sigma 3 is distributed diffusely in the cytoplasm and the nucleus. The subcellular localization of mu NS and sigma 3 is not altered when the proteins are expressed together or with sigma NS. However, when expressed with micro NS, sigma NS colocalizes with mu NS to punctate structures similar in morphology to inclusion structures observed early in viral replication. During reovirus infection, both sigma NS and mu NS are detectable 4 h after adsorption and colocalize to punctate structures throughout the viral life cycle. In concordance with these results, sigma NS interacts with mu NS in a yeast two-hybrid assay and by coimmunoprecipitation analysis. These data suggest that sigma NS and mu NS are the minimal viral components required to form inclusions, which then recruit other reovirus proteins and RNA to initiate viral genome replication.

Animals↗
PubMed1985

Serum alpha interferon and lymphocyte inclusions in systemic lupus erythematosus.

The relationship between serum acid-labile alpha interferon and tubuloreticular inclusions within the cytoplasm of circulating lymphocytes was studied in 46 patients with systemic lupus erythematosus. Elevated levels of interferon (greater than or equal to 8 IU/ml) were found in 17 patients and lymphocyte inclusions in 35. The mean serum interferon concentration in patients with lymphocyte inclusions was significantly higher than in patients without inclusions (17.2 versus 2.4 IU/ml, p less than 0.01). Inclusions were found in 16 of 17 patients with elevated interferon and also in 19 of 29 patients without interferon (p = 0.026). In lupus, serum interferon appears to be a sufficient though not an essential marker for the presence of lymphocyte inclusions.

Humans↗
PubMed2002

Paradoxical absence of nuclear inclusion in cerebellar Purkinje cells of hereditary ataxias linked to CAG expansion.

Degeneration of cerebellar cortex is one of the principal features of hereditary ataxias linked to expansion of CAG repeat. In an attempt to clarify possible correlation between neuronal depletion and neuronal intranuclear inclusions, both triggered by the pathological expansion of CAG repeat, cerebellar sections from SCA1, SCA2, SCA3, and DRPLA cases were immunostained with anti-ubiquitin or anti-expanded polyglutamine antibody (1C2) and were screened for the presence of neuronal intranuclear inclusions. Although the degree of cerebellar degeneration varied greatly, cerebellar Purkinje cells were uniformly characterised by the absence of neuronal intranuclear inclusion. Complete absence of neuronal intranuclear inclusion in Purkinje cells is apparently paradoxical and hardly explained if neuronal intranuclear inclusion formation is positively correlated to a mechanism accelerating neuronal death. It may, otherwise, suggest an intrinsic link between neuronal intranuclear inclusion formation and neurodegeneration in opposite directions in human Purkinje cells, more or less affected in these CAG repeat disorders.

Antibodies, Anti-Idiotypic↗
PubMed2002

Role of porphyrin sequestration in the biogenesis of iron-laden astrocytic inclusions in primary culture.

Astrocytes in subcortical regions of the mammalian brain progressively accumulate iron-rich, autofluorecent cytoplasmic inclusions as a function of aging. Cysteamine (CSH) accelerates the appearance of this senescent glial phenotype in situ and in primary rat astroglial cultures. Porphyrins have been implicated as the source of orange-red autofluorescence in these glial inclusions. Yet, CSH has been shown to suppress porphyrin-heme biosynthesis in cultured astroglia. To determine whether porphyrin biosynthesis or sequestration participates in the biogenesis of these glial inclusions, the porphyrin precursor, (3)H-delta-aminolevulinic acid ((3)H-ALA) was administered to CSH-exposed and control rat astroglial cultures followed by light and electron microscopic autoradiography. Control cultures exhibited faint orange-red autofluorescence, intense (3)H-ALA labeling, numerous normal mitochondria and few cytoplasmic inclusions. In these cells, (3)H-ALA labeling largely occurred over normal mitochondria. The CSH-treated astroglia exhibited diminished (3)H-ALA labeling and contained numerous orange-red autofluorescent inclusions. The latter manifested internal compartments delimited by double membranes characteristic of damaged mitochondria. The complement of normal mitochondria in the CSH-exposed cells was markedly reduced. In the CSH-treated cells, (3)H-ALA labeling predominated over the large multi-compartmental inclusions. CSH attenuates de novo porphyrin-heme biosynthesis in astroglia but may induce punctate orange-red autofluorescence in the cytoplasm of these cells by promoting large numbers of damaged, porphyrin-containing mitochondria to form tight aggregates within the nascent gliosomes.

Aminolevulinic Acid↗
PubMedDate not supplied

Membranous lamellar cytoplasmic inclusions in histiocytes and mesothelial cells of serous fluids. Their relationship to phagocytosis of red blood cells.

OBJECTIVE: To define the composition of cytoplasmic inclusions forming stacks and concentric whorls in histiocytes and mesothelial cells of serous fluids, imparting to them a resemblance to Gaucher cells, and to draw conclusions on the mechanism of their formation. STUDY DESIGN: Three serous fluids (one pleural and two pericardial) containing a fair number of the cells referred to were progressively subjected to the following studies: (1) cytochemistry for mucopolysaccharides, proteins, phospholipids and hemoglobin; (2) immunocytochemistry for immunoglobulins IgA, IgG, IgM and lysozyme; (3) transmission electron microscopy (TEM), and (4) scanning electron microscopy-based energy dispersive X-ray microanalysis (SEM-EDAX). RESULTS: All three specimens were blood stained and contained large numbers of histiocytes and mesothelial cells, arranged singly and in groups, with abundant cytoplasmic inclusions. The inclusions stained strongly positive for phospholipids, weakly positive for hemoglobin and negative for all other substances examined by cytochemistry and immunocytochemistry. By TEM the inclusions had a concentric lamellar membranous structure, reminiscent of myelinosomes or lamellar bodies of lipid-forming or -storing cells. There was also phagocytosis by histiocytes and mesothelial cells of red blood cells, which were mostly in a degenerated state. SEM-EDAX of inclusion-bearing cells showed a modest peak for phosphorus and a variable but small peak for iron, which corroborated the cytochemical and TEM findings. CONCLUSION: Since there was not metabolic or other systemic disease in the patients to account for these cells, we posit that phospholipids derived from cell membranes of phagocytized cells, especially red blood cells, provide the building blocks for the formation of such inclusions as they enter the metabolic pathway of phagocytic cells (mesothelial cells and histiocytes) and appear in their lysosomal structures. It is advantageous for cytologists to be familiar with significance of such changes and not to mistake them for metabolic or other systemic disease.

Adult↗
PubMed1991

A novel DNA virus associated with feather inclusions in psittacine beak and feather disease.

The nature of feather inclusions was characterized in 32 psittacine birds (30 cockatoos, one peach-faced lovebird (Agapornis roseicollis), and one red-lored Amazon parrot (Amazona autumnalis autumnalis] with naturally-acquired psittacine beak and feather disease. Intranuclear inclusions within feather epithelial cells and intracytoplasmic inclusions within macrophages in the feather epithelium and pulp cavity contained psittacine beak and feather disease viral antigen when stained by the avidin-biotin complex immunoperoxidase technique. Ultrastructurally, inclusions were observed primarily within macrophages and to a lesser extent within epithelial cell nuclei. Macrophage inclusions appeared as paracrystalline arrays of viral particles. Intranuclear inclusions were less well defined, although scattered viral particles were present. Intracytoplasmic and intranuclear particles in ultrastructural preparations were identified by colloidal gold labeling as psittacine beak and feather disease virus. Feather epithelium was more frequently and severely involved in the disease process than was adjacent follicular epithelium. Plucked feathers with an intact epidermal collar and feather epithelium were preferred to follicular biopsies for histopathologic examination.

Animals↗
PubMed1974

Lead-induced inclusion bodies: composition and probable role in lead metabolism.

Lead-induced inclusion bodies in renal tubular cells of rats have been studied in vitro after isolation by differential centrifugation. The inclusion bodies are insoluble in physiological media but may be dissolved in denaturants like 6M urea and sodium deoxycholate. They contain about 40-50 mug of lead/mg protein, but only about 10% of this is tightly bound. They also contain calcium, iron, zinc, copper, and cadmium. The protein is rich in glutamic and aspartic acids, glycine and cystine. When dissolved in 6M urea, the protein migrates as a single band on acrylamide gel electrophoresis and has a molecular weight of 27,500. It is suggested that the inclusion bodies function as an intracellular depot of nondiffusible lead. Further studies have been directed toward finding a free, unaggregated lead-containing protein fraction. Nuclear proteins from kidneys of lead-toxic rats were separated into NaCl-, Tris-, and NaOH-soluble fractions and an insoluble acidic fraction. A quantitatively small lead-containing protein was found in the 0.14M NaCl fraction. Amino acid composition, electrophoretic mobility, molecular weight, and ability to bind lead are similar to those of insoluble inclusion body protein. The possible role of this soluble lead-binding protein in the formation of nuclear inclusion bodies is at present time not certain. These studies do suggest, however, that protein-bound lead in renal tubular cells may be partitioned between insoluble and nondiffusible morphologically discrete inclusion bodies and a soluble, extractable fraction which is presumably diffusable.

Amino Acids↗