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F Uchino

Publications and source records attributed to F Uchino.

At least 37 records · Page 2Linked to original sources
PubMed1991

Amyloid fibril formation in the rough endoplasmic reticulum of plasma cells from a patient with localized A lambda amyloidosis.

Evidence for amyloid fibril formation in rough endoplasmic reticulum (RER) of plasma cells from the duodenum of a 62-year-old man with localized A lambda amyloidosis is described. The inclusions in RER of plasma cells were composed of tightly packed, regular arrays of fibrils cut in both longitudinal and cross-sections. The fibrils within the inclusions, measuring 10 nm in width, were oriented parallel to the long axis of the inclusions. By immunoelectron microscopy with an antihuman A lambda antiserum, gold particles labeled the fibrils located both in the RER of plasma cells and in the extracellular space. In addition, electron-dense material in the dilated RER was occasionally labeled. These findings suggest that at least some amyloid fibrils are unequivocally created in the RER of plasma cells.

Amyloid↗
PubMed1990

Carcinosarcoma of the gallbladder. A case report with immunohistochemical and ultrastructural studies.

The authors present the histologic features, immunohistochemical findings, and ultrastructure of a carcinosarcoma of the gallbladder containing rhabdomyosarcoma as a mesenchymal element. A pedunculated polypoid tumor protruded into the lumen from the fundus of the gallbladder. The neoplasm contained two divergent components. One was malignant mesenchymal tissue with rhabdomyoblastic differentiation; the other was ordinary adenocarcinoma which was observed predominantly at the base of the polyp. Immunohistochemically, the cytoplasm of the rhabdomyoblasts stained with anti-myoglobin, myosin, and muscle actin antibodies. Ultrastructurally, there were a large number of malignant mesenchymal tissues in which various stages of differentiated rhabdomyoblasts were noted. Ultrastructural study was particularly valuable for the identification of sarcomatous elements.

Carcinosarcoma↗
PubMed1990

A case of cerebral composite ganglioneuroblastoma: an immunohistochemical and ultrastructural study.

An unusual cerebral tumor is reported in a 14-year-old boy. On light and electron microscopy, the constituent cells were very complex; the majority of the neoplastic cells were primitive neuroectodermal cells dispersed in myxomatous or fibrous stroma. Neoplastic neuronal cells and hypertrophic astrocytes were also observed in these areas. The neuronal cells showed a continuous spectrum of differentiation from very primitive to mature ganglion cells. Furthermore, the tumor contained a highly cellular discrete area consisting of neuroblasts and their precursor cells. From these findings, a diagnosis of composite ganglioneuroblastoma was made.

Adolescent↗
PubMed1989

Ultrastructural evidence for intracellular formation of amyloid fibrils in macrophages.

Early amyloid deposition in the spleen was studied by immunoelectron microscopy following the administration of rapid amyloid-inducing agents to mice. Two days after the injection of an amyloid-enhancing factor and casein solution, a small amount of amyloid material was observed at the border of the white pulp and the marginal zone (perifollicular area) and also within the white pulp. At this stage, amyloid fibrils were seen mainly in an extracellular distribution along the cytoplasmic processes of reticular cells and also in the cytoplasmic invaginations of macrophages. By immunoelectron microscopy, gold particles labelled fibrillar structures in lysosome-derived organelles in some macrophages as well as dense bodies consisted of a homogeneous, granular matrix not having any recognizable fibrillar structures. Similar immuno-labelled organelles were also observed in the amyloid resorption stage, although, at that stage, they commonly contained other phagocytized materials as well. From these findings, we suggest that at least some amyloid fibrils are polymerized in the cytoplasm of the macrophages by the proteolytic cleavage of previously pinocytized serum amyloid A protein (SAA).

Actin Cytoskeleton↗
PubMed1989

Amyloid enhancing factor (AEF) in the aging mouse.

Amyloid enhancing factor (AEF) activity was tested in spleen homogenates from 52, 28, and 9-week-old untreated mice. Strong AEF activity was present in the supernatant of spleen homogenate from the 52-week-old mice. Only weak activity was observed in the supernatant from the 28-week-old mice, and none was seen in that from the 9-week-old mice. Crude spleen homogenates from the 52-week-old mice were subjected to Sephacryl S-300 gel filtration. AEF activity existed in the first gel filtration peak. These findings suggest that AEF increases in the spleens of aged mice and that AEF may be a substance of high molecular weight.

Aging↗
PubMed1989

Amyloid protein of vessels in leptomeninges, cortices, choroid plexuses, and pituitary glands from patients with systemic amyloidosis.

The cerebrum, cerebellum, and choroid plexuses from 16 patients with systemic amyloidosis, and the pituitary glands from 14 of these patients, were investigated histologically and immunohistochemically. Cerebrovascular amyloid (CVA) was found in the leptomeninges and cortices of six patients with systemic amyloidosis, including two patients with amyloid A protein (AA) amyloidosis related to serum amyloid A protein, one with AL amyloidosis related to immunoglobulin light chain (AL), two with familial type I amyloidotic polyneuropathy (FAP), and one with senile systemic amyloidosis (SSA). CVA protein from two patients with FAP reacted with anti-human prealbumin antibody similar to that of the visceral organs of these two patients. CVA in SSA reacted with anti-human prealbumin antibody and anti-beta protein antibody. Vascular amyloid was frequently noted in the pituitary glands and choroid plexuses of patients with systemic amyloidosis, and was found to be identical to that in the visceral organs (heart, kidney, and intestine) of these patients. CVA in the leptomeninges and cortices from two patients with AA amyloidosis and one with AL amyloidosis reacted with anti-beta protein monoclonal antibody but not with anti-human AA monoclonal antibody, anti-human A lambda antisera, and anti-human A kappa antisera. We suggest that amyloid proteins of AA and AL amyloidosis do not readily accumulate in the vessels in the leptomeninges and cortices even though the proteins circulate, and that beta protein is not derived from a serum precursor.

Amyloid↗
PubMed1989

Two familial cases of Jordans' anomaly. Ultrastructural studies and the development of fat-containing vacuoles in the neutrophilic series.

A study was conducted on two brothers with Jordans' anomaly. Fat-containing vacuoles were noticed in all leukocytes of the peripheral blood and cells of the myeloid series including myeloblasts, but the serum lipids showed no abnormalities. However, cells of the erythroid series, megakaryocytes and platelets did not contain these vacuoles. An increase in vacuole number was observed as the leukocytes matured. Histochemically, it was suggested that these vacuoles contained neutral fat based on staining with Sudan III and Nile blue sulfate. Ultrastructurally, these vacuoles were unassociated with lysosomes or other cell organelles. Although the etiology of Jordans' anomaly could not be clarified by this study, genetic factors may be involved.

Adult↗
PubMed1989

Immunocytochemical evidence of amyloid-enhancing factor (AEF) in polymorphonuclear leukocytes.

Amyloid-enhancing factor (AEF) was extracted from spleens of mice that had received amyloidogenic stimulation. Sephacryl S-300 gel filtration of the crude AEF yielded five fractions, among which strong AEF activity was present in the first peak (F1), and confirmed by an amyloid induction experiment. An anti-AEF antiserum was obtained from a rabbit by immunization with F1. This antibody reacted strongly with splenic polymorphonuclear leukocytes (PML) from mice given amyloidogenic stimulation, and weakly with those from normal untreated mice. Isoelectric focusing (IEF) analysis of both F1 and sera from mice given amyloidogenic stimulation was performed. A single band was observed on IEF analysis of F1, whereas many bands were seen on IEF analysis of the sera. After the substances in the gel had been transferred to nitrocellulose membranes by capillary blotting, the membranes were made to react with the anti-AEF antiserum. The results suggested that AEF is a high-molecular-weight substance derived from PML and increases in the serum at the time of, or shortly prior to, amyloid deposition in the spleen.

Amyloid↗
PubMed1989

Distribution of spermine in bacilli and lactic acid bacteria.

Obligate moderately thermophilic bacilli and obligate moderately thermoacidophilic bacilli contained spermine as the major polyamine in addition to putrescine and spermidine. The identity of spermine was confirmed by thin-layer chromatography and high-performance liquid chromatography before and after treatment with putrescine oxidase. Using these methods, thermospermine and spermine can be separated; thermospermine was not present in these organisms. On the other hand, various facultative thermophiles and mesophilic strains of the genus Bacillus, including alkalophiles and halophiles, lack spermine and other tetraamines. No spermine was detected in several strains of mesophilic or facultative slightly thermophilic lactic acid bacteria, Lactobacillus and Streptococcus.

Bacillus↗
PubMed1988

Localized amyloidosis of the uterine cervix.

Localized amyloidosis of the uterine cervix was found in a 56-year-old woman. The firm enlarged cervix showed massive tumorous amyloid deposition. In the amyloid deposits there were foci of ossification and calcification. An infiltrate of multinucleated giant cells, histiocytes, lymphocytes, and plasma cells was seen adjacent to the amyloid deposits. Immunohistochemically, the amyloid reacted with antisera against A-lambda, amyloid protein of immunoglobulin lambda light chain origin. This indicated that the amyloid protein was of immunoglobulin origin in this rare case of localized amyloidosis of the uterine cervix.

Amyloidosis↗
PubMed1988

Monoclonal antibody against polyglucosan isolated from the myocardium of a patient with Lafora disease.

Polyglucosan was extracted from the myocardium of a patient with Lafora disease. Gas chromatographic analysis of the isolated polyglucosan revealed glucose as the only sugar component. Monoclonal antibodies (MAb) were raised against the isolated polyglucosan. With the MAb, immunocytochemistry showed positive staining of Lafora bodies, corpora amylacea, basophilic degeneration of the cardiac muscle cells, and inclusion bodies within cardiac muscle cells and the hepatocytes of patients with Lafora disease and type IV glycogenosis (Andersen's disease). These findings indicate that cells of the latter group share antigenicity with Lafora bodies.

Adult↗
PubMed1988

Ultrastructure of kidney from three patients with HBeAg-associated nephropathy with special reference to virus-like particles in the glomerular tufts.

The biopsied kidneys from three patients with hepatitis Be antigen (HBeAg)-associated nephropathy were observed by light microscopy, immunohistochemistry and electron microscopy. By an indirect technique utilizing horseradish peroxidase-conjugated antisera, HBeAg was found to be deposited in a diffuse granular fashion along the glomerular capillary wall. No deposition of hepatitis Bs or hepatitis Bc antigen was detected. The three cases were diagnosed as HBeAg-associated nephropathy. Ultrastructurally, there were finely granular electron-dense deposits in the subendothelial area, basement membrane, mesangial area and subepithelial area of the glomerular tufts. In all three cases, virus-like particles between 30 and 70 nm in diameter were also found in such areas of the glomerular tufts, and rarely in the glomerular capillary lumen and space of Bowman. They occasionally formed clusters in the phagosomes of mesangial cells. In addition, tubulo-reticular structures were noted in the cytoplasm of endothelial cells in the glomerular capillaries. The presence of HBeAg both in the serum and in the kidney and of virus-like particles in the glomerular tufts suggests that HBeAg is causally related to the development of HBeAg-associated nephropathy.

Adult↗
PubMed1987

Foamy cells associated with phagocytosis of glutaraldehyde-treated red blood cells and red cell membranes.

In order to clarify the mechanism for the formation of foamy cells (macrophages with foamy appearance) associated with increased erythrophagocytosis, we tried to reproduce these cells in mice by subcutaneous injection of intact red blood cells (RBCs), OsO4-treated RBCs (Os-RBCs), glutaraldehyde-treated RBCs (G-RBCs), or isolated red cell membranes, and time-course observation was done by light and electron microscopy. Foamy cells were induced by the latter two methods. Within the macrophages, G-RBCs were fragmented into spherules by newly formed small vacuoles, and with time these spherules lost their hemoglobin content transforming into small vacuoles with translucent matrix. In most of these vacuoles, red cell membrane structure was discernible adjacent to the phagocytic vacuole. Such macrophages containing abundant small vacuoles appear foamy in light microscopy. Foamy cells induced by injection of red blood cell membranes were positive for lipid stains and contained abundant laminated membrane structures in electron microscopy. These results suggest that the foamy cells related with increased erythrophagocytosis are heterogeneous with respect to their pathogenesis and cellular inclusions, and proteinaceous constituents resistant to intracellular digestion are also responsible for the occurrence of foamy cells.

Animals↗