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F Uchino

Publications and source records attributed to F Uchino.

At least 19 recordsLinked to original sources
PubMed1999

Delayed postoperative CSF rhinorrhea of intrasellar arachnoid cyst.

CSF rhinorrhea due to a transsphenoidal approach usually follows accidental or intentional arachnoid opening. We report a patient with an intrasellar arachnoid cyst, who developed delayed onset of CSF rhinorrhea. A sixty-two-year-old man presented with bitemporal type visual field defect for the last 3 years. With the diagnosis of arachnoid cyst or Rathke's cleft cyst, based on MRI findings of intra-and supra-sellar cyst with CSF intensity, he successfully underwent transsphenoidal surgery without evidence of intra-operative CSF leakage. He developed CSF rhinorrhea one week later. This needed another operation for sellar floor repair. The pathomechanism of this delayed onset is explained as follows. Incomplete or oneway communication of subarachnoid space to cyst cavity, unrecognized during surgery, might cause delayed onset of CSF rhinorrhea. By using MRI, identification of the residual gland, which was compressed posteriorly, is useful for differentiating an arachnoid cyst from other cystic lesions. In highly suspect cases, even without evidence of intra-operative CSF leakage, peri-operative measures to prevent occurrence of postoperative CSF rhinorrhea are required.

Arachnoid Cysts↗
PubMed1995

Hepatic amyloidosis in Japan: histological and morphometric analysis based on amyloid proteins.

To investigate the relationship between the tissue distribution and the types of amyloid proteins, the detailed histopathologic features of the available liver in 284 cases of amyloidosis were examined. We classified hepatic amyloidosis into three types, namely, the vascular pattern, parenchymal pattern, and stromal pattern according to the topographic distribution pattern of amyloid. Of the 152 amyloid A (AA) cases, all but one exhibited the vascular pattern; the single exception had the parenchymal pattern. Among 117 amyloid light chain (AL) cases, 51.3% exhibited the vascular pattern and 43.6% the parenchymal pattern. The stromal pattern was observed in 5.1% of the cases but was found only in AL amyloidosis. The parenchymal and stromal patterns in the liver seemed to be characteristic morphological distributions of AL amyloidosis. Routine histochemical study is useful to distinguish AL from AA, although some ethnic differences were apparent. Morphometric results showed that the walls of the hepatic arteries with amyloid deposition were significantly thicker than walls in arteries from the control group. The arterial walls in AA amyloidosis, especially, were significantly thicker than walls in AL amyloidosis of any pattern.

Amyloid↗
PubMed1995

Incidence and distribution of isolated atrial amyloid: histologic and immunohistochemical studies of 100 aging hearts.

The incidence and anatomic distribution of isolated atrial amyloid (IAA) in 100 aging hearts were studied histologically and immunohistochemically using antibodies against alpha-human-atrial natriuretic peptide (alpha-ANP), human transthyretin (TTR) and human amyloid P component (AP). Ninety-one of 100 hearts (91%) had amyloid deposits in the atria. Amyloid deposits in all 91 hearts reacted with alpha-ANP and AP antisera, and in four hearts other amyloid deposits that reacted with TTR antiserum were coincidentally seen in the atria. The prevalence of IAA deposition, using a semiquantitative evaluation, was significantly higher in the hearts from patients over 80 years of age, from women, those weighing over 450 g, with a thickened left ventricular wall (> 1.4 cm) and with multiple myocardial scars. IAA deposition showed a significant distribution in the auricle and left atrium; it was located mostly in the interstitium of the subendocardial layer and the subendocardial myocardium. These results indicate that IAA occurs more frequently than previously appreciated in the elderly and in patients with certain cardiac disorders.

Aged↗
PubMed1994

Histochemical and ultrastructural studies of inclusion bodies found in tissues from three siblings with I-cell disease.

Tissues from three siblings with inclusion-cell (I-cell) disease (a 16 month old boy and two fetuses aborted at 20 and 18 weeks) were investigated histologically, histochemically and ultrastructurally. The lymphocytes, fibroblasts, endothelial cells, epithelial cells and histiocytes of various organs were affected. The cells had many intracytoplasmic vacuoles, which showed positive staining with colloidal iron, periodic acid-Schiff (PAS), alcian blue, and Sudan III and IV. Ultrastructurally, the cells contained various inclusion bodies, showing vesicles, granules, flocculent material, amorphous electron-dense globules and myelin structures. The amounts and ultrastructural features of the inclusion bodies differed among the various kinds of cells.

Abortion, Induced↗
PubMed1994

Immunohistochemical classification of 140 autopsy cases with systemic amyloidosis.

One hundred and forty autopsy cases of systemic amyloidosis were examined using the potassium permanganate method for distinction of amyloid A protein from other amyloid proteins and an immunohistochemical technique. Of those cases, amyloid proteins were identified in 121 cases. There were 68 cases of amyloid A-related (AA) amyloidosis and these were the most common type among the cases (56.2%). There were 39 cases of immunoglobulin light chain-related (AL) amyloidosis (32.2%), six cases of beta 2-microglobulin-related (A beta 2M) amyloidosis (5%), and five cases of transthyretin-related (ATTR) amyloidosis (4.1%). Minute areas of amyloid deposits in four cases with AA were resistant to potassium permanganate pretreatment. In A beta 2M amyloidosis amyloid deposits were either resistant or sensitive to potassium permanganate pretreatment, from case to case. The coexistence of two different amyloid proteins was seen in three cases: one case had ATTR and A kappa types, and two cases had A beta 2M and AA types. Some discrepancies were seen between the immunohistochemical typing and clinical classification of amyloidosis referred to in the Annual of the Pathological Autopsy Cases in Japan, for example, one case of AA type in myeloma-associated amyloidosis and one case of AL type in secondary amyloidosis. From the present results, the importance of the immunohistochemical method in classifying amyloidosis is stressed.

Adult↗
PubMed1994

Formation of amyloid-like substance from beta-2-microglobulin in vitro. Role of serum amyloid P component: a preliminary study.

Although the pathogenesis has yet to be fully understood, beta 2-microglobulin (beta 2m) related amyloidosis is a frequent complication in long-term hemodialysis (HD) patients. In an attempt to clarify the association of two potential candidates with amyloidogenesis from beta 2m in HD patients, human urine-derived beta 2m solution alone or combined with glycosaminoglycans: hyaluronic acid, heparan sulfate, or serum amyloid P component (SAP) were dialyzed against physiological buffered solution (pH 7.4) using a microdialyzer in vitro for 72 h at 4 degrees C. This study demonstrates for the first time that SAP can play a crucial role in the formation of amyloid-like fibrils from beta 2m. This occurs by a direct influence on either the processing of a precursor protein, or protein folding, in vitro, by a short-period dialysis against a physiological buffered solution.

Amyloid↗
PubMed1994

Immunohistochemical and pathological characteristics of dystrophic amyloid in surgically excised cardiac valves.

One hundred and thirty-six cardiac valves obtained surgically from 124 patients (aged 15-77 years) were examined. Microdeposition of amyloid was present in sclerotic or sclerocalcific lesions of aortic valves in 38 out of 75 (51%) and mitral valves in 21 out of 61 (34%). Amyloid deposition was not significantly related to the age of the patients. An antiserum raised against a low molecular weight protein extracted from amyloid-laden valvular tissues (about 20 g) reacted positively to amyloid in the cardiac valves. It did not react to amyloid deposition containing fibril proteins including light chain related amyloidosis, reactive amyloidosis, systemic senile amyloidosis, isolated atrial amyloidosis, beta-2-microglobulin related amyloidosis and beta protein related amyloidosis. Further, amyloid in the cardiac valves failed to react immunohistochemically to anti-AA, anti-AL, anti-TTR, anti-ANF, anti-beta 2M and anti-beta protein antibodies. These findings suggest that an unknown amyloid protein is involved in the damaged valves.

Adolescent↗
PubMed1994

[Enhanced regeneration of terminal axons after hyperbaric oxygen therapy in a patient resembling progressive postpoliomyelitis muscular atrophy].

We found an electromyographical proof of reconstruction of the motor nerve terminals following hyperbaric oxygen therapy. A 38-year-old man who had been partially recovered for thirty four months from acute onset paraplegia following a gastrointestinal infection developed progressive muscular atrophy and weakness of the lower limbs, and was first admitted to our hospital. Cerebrospinal fluid examination was normal and nerve conduction studies showed small compound muscle action potentials without an evidence of segmental demyelination. There were ample fibrillation potentials on electromyography. Single fiber electromyography (SFEMG) showed increased fiber density, abnormal jitter and blockings without neurogenic jitter, which were similar to findings in post-poliomyelitis syndrome. He was treated by hyperbaric oxygen consisting of two hour exposures to pressures of two atmospheres breathing 100% oxygen. These exposures continued for a month daily, and thereafter once a week for one year. Clinical improvement of the weakness and a decrease in amount of fibrillation potentials occurred on and after a month after treatment. We found significant changes on SFEMG a year later. There were increased fiber densities and decreased mean values of consecutive differences. These changes indicate diminished degeneration and enhanced regeneration of the terminal axons. We think that hyperbaric oxygen has a beneficial effect on oxygen metabolism of remaining motoneurons which may not be able to maintain excessive metabolic demands of all their sprouting axons.

Adult↗
PubMed1993

Morphological evaluation of amyloid-laden arteries in leptomeninges, cortices and subcortices in cerebral amyloid angiopathy with subcortical hemorrhage.

To investigate the relationship between cerebral amyloid angiopathy and subcortical (lobar) hemorrhage, we examined the severity of amyloid deposition in the leptomeningeal, cortical and subcortical arteries in 28 autopsied elderly patients with cerebral amyloid angiopathy with subcortical hemorrhage, deep cerebral hemorrhage or without hemorrhage. The severity was evaluated in terms of the frequency of amyloid-laden arteries and the degree of amyloid deposition within the arteries. The frequency of amyloid-laden arteries, especially among arteries over 200 microns in diameter, was higher in subcortical hemorrhage group than in the deep hemorrhage group and the non-hemorrhage group, and when the degree of amyloid deposition in the arteries was divided into four grades (none, mild, moderate or severe), the severity was higher in the subcortical hemorrhage group than in the deep cerebral hemorrhage group and the non-hemorrhage group. These results suggest that severe cerebral amyloid angiopathy is related to non-traumatic subcortical hemorrhage in elderly persons.

Aged↗
PubMed1993

Localized amyloidosis in squamous cell carcinoma of uterine cervix: electron microscopic features of nodular and star-like amyloid deposits.

An ultrastructural study of amyloid deposits in four cases of squamous cell carcinoma of uterine cervix was performed. The amyloid deposits reacted with anti-keratin antiserum on frozen sections. Amyloid deposits showed nodular (4 cases) and star-like forms (3 cases). Nodular amyloid deposits were composed of slightly whorled fibrils, measuring 7-10 nm in width. Some of them contained cellular debris and thicker, more electron-dense filaments than amyloid fibrils. In three cases, filamentous tumour cells and filamentous masses were observed together with amyloid. Star-like amyloid deposits were composed of bundles of straight amyloid fibrils. Some of the tumour cells in contact with star-like amyloid deposits had deep cytoplasmic invaginations, where closely packed amyloid fibrils were arrayed in parallel fashion. In addition, a few tumour cells had membrane-bound amyloid fibrils in the cytoplasm. It is suggested that nodular amyloid deposits are derived from the tumour cells through filamentous degeneration. Amyloid fibrils in star-like amyloid deposits are thought to be formed within the cytoplasm or in the vicinity of invaginated cytoplasmic membranes of the tumour cells.

Aged↗
PubMed1992

Farber bodies found in murine phagocytes after injection of ceramides and related sphingolipids.

Mice were injected subcutaneously with a single dose of sphingolipids. The sphingolipids tested were: ceramide with alpha-hydroxy fatty acids, ceramide with non-hydroxy fatty acids, glucocerebroside, sphingomyelin, and galactocerebroside. Lipids without sphingolipids served as a control. The mice were sacrificed 1, 2, 3, 4, 5 and 7 days after injection. Three mice were used for each experiment. The subcutaneous tissue at the injected area, the liver and the spleen were studied histologically. At 1-3 days after injection, numerous cytoplasmic inclusion bodies were observed in the macrophages and fibroblasts in the subcutaneous tissue, but not in the liver or the spleen. Ultrastructural studies of the inclusion bodies indicated that the sphingolipids taken up by the phagocytes retained their respective original shape during the 1-3 day stage. At days 4 and 5, the number of the inclusion bodies decreased, but they contained Farber bodies, i.e. curvilinear bodies 12 to 25 nm wide and up to 120 nm long. The mice with galactocerebroside were an exception, with parallel leaflets structures, but without the Farber bodies.

Animals↗
PubMed1992

An autopsy case of Farber's lipogranulomatosis in a Japanese boy with gastrointestinal involvement.

A boy with Farber's lipogranulomatosis is reported. Excessive ceramide was revealed by thin-layer chromatography of the extracts from the liver. Acid ceramidase activity of the liver was 31.5% of control with exogenous substrate and 33.3% without exogenous substrate. The histological appearance showed granulomatous lesions, composed of spindle or oval-shaped storage cells and proliferation of the connective tissues, in the subcutaneous tissue of the lower lip, periarticular regions and the pericardium. Histochemically the storage cells were revealed to contain lipid and polysaccharide. The foreign body granuloma formed by the surgical suture in the liver was surrounded by a large number of foamy cells. In gastrointestinal mucosa widespread erosion, disappearance of glands and abundant collagen fibers were noted. On electron microscopy, the spindle or oval-shaped cells in the subcutis of the lip had intracytoplasmic inclusions containing granular or fibrillar materials and a smaller number of curvilinear structures, so called "Farber bodies". Our case was a typical clinical and histopathological presentation of Farber's lipogranulomatosis. However, ceramidase activity was higher than in previous descriptions, and severe gastrointestinal lesions and the appearance of a large number of foamy cells around the foreign body granuloma have not been described previously.

Acid Ceramidase↗
PubMed1992

Comparative study of intraneuronal polyglucosan bodies in brains from patients with Lafora disease and aged dogs.

We compared intraneuronal polyglucosan body (PGB) in brains from two patients diagnosed as having Lafora disease and from 18 aged dogs (age range: 10 to 22 years, various breeds). PGBs appeared as various-sized spheroids intensely stained with periodic acid-Schiff (PAS) in both humans and aged dogs. Immunohistochemistry with a monoclonal antibody raised against human polyglucosan showed positive staining of the PGBs. Ultrastructurally, PGBs in both humans and aged dogs were composed of fibril-like structures 4 to 20 nm wide. Electron-dense material formed the central cores of the fibrils, but was also scattered in their peripheral areas. The fibril-like structures were intensely stained upon application of the Thiéry procedure. Immunoelectron microscopy showed that the fibril-like structures were specifically labeled with gold particles. The histological, immunohistochemical and ultrastructural features of the PGBs in humans and aged dogs were quite similar.

Adult↗
PubMed1991

Immunohistochemical and immunoelectron microscopical characterization of cerebrovascular and senile plaque amyloid in aged dogs' brains.

Immunohistochemical and immunoelectron microscopical studies were carried out on 28 aged dogs' brains. Amyloid deposits were seen in the arteries and capillaries in the leptomeninges and in superficial areas of the cortices in 19 (67.9%) of the 28 dogs (10-22 years of age). Immunohistochemically, these amyloid deposits were reactive for anti-beta/A4 antibody. Additionally, a variable number of parenchymal deposits with diffuse beta/A4-immunoreactivity (diffuse plaques) was also noted throughout the cerebral cortex in 24/28 dogs (85.7%). However, these plaque lesions were undetectable in Congo red staining. Electron microscopically, amyloid fibrils, measuring 10 nm in width, were located mainly in the tunica media of the arteries, and in less involved vessels they tended to be present among collagen fibres in the adventitia and smooth muscle cells in the outer layer of the media. The plaque lesions appeared to contain sparse aggregations of amyloid fibrils. In immunoelectron microscopical examinations, all amyloid fibrils in both blood vessels and plaques were selectively labelled by gold particles. These findings indicate that aged dogs can provide a useful experimental model for research into the beta/A4-type of cerebral amyloidosis commonly seen in Alzheimer's disease.

Aging↗
PubMed1991

The significance of cerebrovascular amyloid in the aetiology of superficial (lobar) cerebral haemorrhage and its incidence in the elderly population.

Cerebrovascular amyloid deposition (CVAD), caused by deposition of the beta/A4 protein, has been previously identified as a cause of cerebral haemorrhage, yet its prevalence is uncertain. The presence of vascular amyloid was studied in brains of 169 patients by immunohistochemical and Congo red staining. Fifty patients had cerebral haemorrhage (CH), 56 had cerebral infarction (CI), and 63 had neither haemorrhage nor infarction (control group). CVAD was found in 38 per cent of the CH group, 25 per cent of the CI group, and 32 per cent of the control group. The incidence of CVAD increased with age in each group. Immunohistochemical staining with an antibody to beta/A4 protein was more sensitive than Congo red staining the demonstrating the extent of vascular amyloid. Within the CH group, CVAD was present in the vessels at the site of haemorrhage in 6/8 (75 per cent) of pure superficial (lobar) cerebral haemorrhages. While amyloid was detected in vessels in the brain of 10/37 (27 per cent) of pure deep cerebral haemorrhages, none was present in vessels at the site of haemorrhage. CVAD is a common pathological finding in the elderly and has a significant association with pure superficial (lobar) cerebral haemorrhages.

Aged↗
PubMed1991

Amyloid enhancing factor (AEF). Isolation and biochemical and pathological characteristics.

Neutrophils and spleens were prepared from mice after treatment to induce amyloid deposition. The deposition of amyloid was accelerated in normal recipients by intravenous injection of more than 2 x 10(4) neutrophils, and intraperitoneal injection of supernatants obtained by homogenization and centrifugation of the neutrophils and spleens. The supernatants were subjected individually to DEAE ion-exchange chromatography. Amyloid enhancing factor (AEF) activity was present in peaks eluted at an NaCl concentration of 0.17 M. The fractions containing AEF were subjected to high-performance liquid chromatography (HPLC), and AEF was eluted at a position corresponding to about 15 KDa. Purified AEF was analyzed by amino acid sequencing and gas chromatography. The N-terminal amino acid was blocked, and AEF contained some saccharides including glucose, mannose, galactosamine and sialic acid, and an undefined substance (probably derived from certain proteins). Immunoelectron microscopy by the pre-embedding method using an anti-AEF antiserum demonstrated that the cytosol, but not primary and specific granules in neutrophils from the spleen of amyloid-laden mice, reacted with the antiserum. These findings suggest that AEF is a glycoprotein associated with neutrophils.

Amino Acid Sequence↗