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T Gondo

Publications and source records attributed to T Gondo.

At least 37 records · Page 2Linked to original sources
PubMed1997

CYFRA 21-1 is a useful marker for esophageal squamous cell carcinoma.

BACKGROUND: CYFRA 21-1 measures soluble cytokeratin-19 fragments in serum and is a useful marker for lung carcinoma, especially squamous cell carcinoma (SCC). The authors conducted this study to determine the significance of CYFRA 21-1 in patients with esophageal SCC. METHODS: Expression and production of cytokeratin-19 in the authors' six established esophageal SCC cell lines were determined by immunocytochemical staining and enzyme-linked immunoadsorbent assay, respectively. The correlation between serum CYFRA 21-1 levels and expression of cytokeratin-19 in human tumors was investigated by immunohistochemical staining. The correlation between serum CYFRA 21-1 levels and clinicopathologic factors was examined in 48 patients with esophageal SCC, as were SCC antigen and carcinoembryonic antigen (CEA). RESULTS: Of the 6 cell lines, 5 lines expressed cytokeratin-19 in their cytoplasm and produced soluble cytokeratin-19 fragments. Twenty-three of 48 patients had elevated CYFRA 21-1 levels (>3.5 ng/mL), whereas none of the reference group (consisting of healthy volunteers or patients with benign disease) showed positive levels. The specificity, sensitivity, and accuracy of CYFRA 21-1 were 100%, 47.9%, and 66.7%, respectively. CYFRA 21-1 showed significantly higher sensitivity and accuracy than SCC antigen or CEA (P < 0.05). Univariate analysis revealed that CYFRA 21-1 levels correlated with disease progression (including tumor size, tumor depth, and pTNM stage), resectability, and curability. There was a significant association between the level of CYFRA 21-1 and its intensity of immunohistochemical staining in vitro as well as in vivo. CONCLUSIONS: CYFRA 21-1 appears to be a useful marker for human squamous cell carcinoma of the esophagus.

Adult↗
PubMed1997

Amyloid A protein amyloidosis induced in apolipoprotein-E-deficient mice.

Apolipoprotein E (apoE) is a constituent of lipoproteins other than low-density lipoprotein, and it principally acts in the transport and metabolism of plasma cholesterol and triglyceride. ApoE is a minor constituent of various kinds of amyloidoses and may play a role as a pathological chaperone for fibrillogenesis of amyloid fibril protein with the amyloid P component and proteoglycans. In this study, we examined the role of apoE in amyloidogenesis in vivo in apoE-deficient mutant mice with amyloid A protein (AA) amyloidosis induced by inflammatory stimulation. Amyloid deposition was seen in six of nine C57BL/6J control mice and in six of eight apoE-deficient mutant mice after the intraperitoneal and subcutaneous injections of the mixture of complete Freund's adjuvant and Mycobacterium butyricum. Moreover, amyloid deposition in apoE-deficient mice as well as C57BL/6J control mice started 48 or 72 hours after injection of amyloid-enhancing factor and silver nitrate, although the amount of amyloid deposit in C57BL/6J control mice was slightly larger than that in apoE-deficient mice. These amyloid deposits reacted with anti-mouse AA antibody were seen in the perifollicular area of the spleen. Immunoreactivity of apoE was seen irregularly in the amyloid deposits of C57BL/6J control mice but not in the amyloid deposit of apoE-deficient mice. From these results, we concluded that apoE is not always necessary for amyloid deposition and that the existence of apoE might slightly accelerate AA amyloid deposition in the earliest phase of AA amyloid deposition.

Amyloidosis↗
PubMed1996

Pancreatoblastoma: case report and review of treatment in the literature.

A case of pancreatoblastoma arising from the body-to-tail of the pancreas in a 5-year-old boy is presented. The patient underwent exploratory laparotomy and, 11 days later, resection of the tumor (partial pancreatectomy, pyloroplasty, and splenectomy). Before resection, cyclophosphamide and vincristine were administered. Because of tumor spillage during resection, a combination of chemotherapy (administration of cyclophosphamide and adriamycin on that day) and postoperative radiotherapy was given. Nine months after resection, partial hepatectomy was performed for liver metastasis and consolidated by a more intensive chemotherapy regimen using cisplatin, adriamycin, vincristine, and cyclophosphamide. After completion of the chemotherapy, the patient had a 14-month uneventful course, and a locally recurrent tumor was treated by the fourth surgery (extirpation of the recurrent tumor, partial hepatectomy, partial colectomy, and partial gastrectomy) and intraoperative radiation. Thereafter, the boy has shown no evidence of disease at 3 years 8 months. The literature of pancreatoblastoma is reviewed from the therapeutic viewpoint.

Child, Preschool↗
PubMed1996

Ultrastructural evidence for colocalization of kappa light chain- and beta 2-microglobulin-derived amyloids using double labelling immunogold electron microscopy.

In systemic amyloidosis, it is essential to decide what type of amyloid protein is deposited in tissues before the therapy can be selected and the prognosis assessed in each patient. We examined tissues affected by amyloid deposition from a patient with multiple myeloma by immunohistochemistry and double labelling immunogold electron microscopy and demonstrated colocalization of kappa light chain- and beta 2-microglobulin-derived amyloids in the same tissue. beta 2-Microglobulin-derived amyloid had ultrastructurally characteristic features that distinguished it from kappa light chain-derived amyloid. This is the first report of the colocalization of two different amyloids by immunoelectron microscopy.

Amyloid↗
PubMed1996

The influence of interleukin-6 on the growth of human esophageal cancer cell lines.

We reported that human esophageal cancer cell lines (ECC) (YES-1, -2, -3, -4, -5, and -6) produced interleukin-6 (IL-6). We, therefore, investigated the growth effects ([3H]thymidine uptake assay and direct cell count) of IL-6 on these ECC. IL-6 receptor (R) and GP-130 mRNA were detected in all the ECC, using reverse transcriptase-polymerase chain reaction (RT-PCR) assay, and IL-6R was detected in one (YES-3) by immunohistochemical staining. IL-6, anti-IL-6 monoclonal antibody (mAb), or anti-IL-6R mAb caused no reproducible enhancement or suppression of [3H]thymidine uptake by all six ECC. Direct cell count also revealed that the growth enhancement or suppression by IL-6, anti-IL-6 mAb, or anti-IL-6R mAb was relatively small. Particularly, there was no significant sensitivity of YES-3 cells, which definitely produce IL-6 and express IL-6R for IL-6, anti-IL-6 mAb, or anti-IL6R mAb. These results suggest that some esophageal cancers may produce IL-6 and express IL-6R. However, no major interactions between IL-6 and the growth of human esophageal cancer cell lines were detected in this study.

Antibodies, Monoclonal↗
PubMed1996

Immunohistochemical study with anti-advanced glycation end-products antibody in murine amyloidosis.

Advanced glycation end-products (AGE) are formed in the late phase of the non-enzymatic glycosylation reaction in conditions such as diabetes mellitus and aging. In amyloidosis, AGE have been found in the A beta 2M amyloid associated with long-term hemodialysis and in the beta-protein in Alzheimer's disease. Murine AApoAII and AA amyloidosis were examined immunohistochemically using anti-AGE monoclonal antibody, 6D12. AApoAII amyloid deposits studied in one senescence-accelerated mouse P1 (SAMP1), congenic mice that have the amyloidogenic apolipoprotein A-II of SAMP1 mice, and AKR mice all reacted with biotinylated 6D12 by formic acid pretreatment, whereas AA amyloid deposits did not react with the antibody. The immunoreaction with anti-apolipoprotein A-II for amyloid deposits in senile mice was approximately homogeneous in intensity; on the other hand the reaction with biotinylated 6D12 was irregular in distribution and intensity over the amyloid deposits. These findings suggest that amyloid precursor proteins are not associated uniformly with AGE modification before deposition as amyloid; it is more likely that the AGE modification progresses gradually and unevenly after amyloid deposition. Murine amyloidosis may be a useful model to elucidate the role of AGE in amyloidosis.

Amyloidosis↗
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

Polysialogangliosides expressed by amelanotic melanoma: a possible explanation for the poor response to anti-monosialoganglioside antibody 202 in a patient with melanoma.

A 52-year-old Japanese woman developed numerous amelanotic metastatic melanomas on the skin and in various organs three years after a surgical operation for primary melanoma on the right axilla. The patient was treated with monosialoganglioside specific monoclonal antibody 202; however, no apparent clinical effects were observed. Ganglioside analysis of a metastatic tumor demonstrated that it expressed GM3, GM2, GD3, GD2, and polysialogangliosides. Since polysialogangliosides rarely appear in melanomas, their expression may explain the patient's poor response to MAb 202. The relationship between ganglioside composition and the effect of anti-ganglioside monoclonal antibody is discussed.

Antibodies, Monoclonal↗
PubMed1995

Angiomyxoid tumour in the renal peripelvic tissues with features of aggressive angiomyxoma.

A case of angiomyxoid tumour in the renal peripelvic soft tissue of a 45 year old woman is reported. The encapsulated tumour, measuring 12 x 9 x 6 cm, was solid and firm. The cut surface revealed a yellowish-white, gelatinous, and glistening tumour. Histologically, the tumour was composed of loosely textured spindle and stellate cells with prominent blood vessels of variable calibre. The tumour cells stained strongly for vimentin. These findings strongly resemble those associated with aggressive angiomyxoma in the vulva and perineum.

Female↗
PubMed1995

[Amyloidosis].

Explore the source record for details and available documents.

Amyloidosis↗
PubMed1994

Intervertebral disc amyloidosis: histochemical, immunohistochemical and ultrastructural observations.

Intervertebral discs selected at random from autopsies and surgical operations on herniated discs were examined for evidence of amyloid deposition. Amyloid deposits were detected in 53 (81.5%) of 65 autopsy cases. Discs from subjects over 50 years of age revealed a significantly high incidence of amyloid deposition. Among herniated discs, amyloid deposits were documented in 49 (75.4%) of 65 surgical specimens. The incidence of amyloid deposition in intervertebral discs increased with advancing age. Intervertebral disc amyloidosis consisted of amyloid deposits of three morphological types: linear amyloid deposits around the degenerating chondrocytes (perichondrocyte type), and nodular or band-like deposits in the annulus fibrosus (annulus fibrosus type) and nucleus pulposus (nucleus pulposus type). We suspect that the precursor protein of perichondrocyte type amyloid is derived from chondrocytes, and those of annulus fibrosus type and nucleus pulposus types are derived from the blood. The amyloid deposits were resistant to treatment with potassium permanganate. Immunohistochemically, the amyloid deposits reacted with antibody against amyloid P-component, but not with antibodies against AA, A kappa, A lambda, transthyretin or beta 2-microglobulin. Ultrastructurally, the amyloid deposits were composed of 10 nm-wide nonbranching fibrils. The amyloid in herniated discs had the same biochemical and immunohistochemical properties as those found in autopsy cases. The immunohistochemical characteristics of the amyloid deposits suggest that it derives from an, as yet, unknown precursor protein.

Adolescent↗
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↗
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↗
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 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↗