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Biomedical subjects

H Toshimori

Publications and source records attributed to H Toshimori.

At least 19 recordsLinked to original sources
PubMed2000

[Evaluation of technetium-99m-MIBI scintigraphy in metastatic differentiated thyroid cancer--comparison study with 131I and 201Tl].

Detectability of metastasis in differentiated thyroid cancer using technetium-99m-methoxyisobutyl isonitrile (99mTc-MIBI) was compared with that of 131I and 201Tl. Forty patients after total thyroidectomy were evaluated. The scan results were compared with those of 131I and 201Tl whole body scintigraphy per patient. The positive rate was 68% in 99mTc-MIBI, 84% in 131I, 60% in 201Tl respectively. As to the lymph node metastasis, the positive rates were 56% in 99mTc-MIBI, 78% in 131I, 39% in 201Tl. In lung metastasis, the positive rate was 46% in 99mTc-MIBI, 82% in 131I and 55% in 201Tl. Serum thyroglobulin (Tg) was significantly higher in 201Tl and/or 99mTc-MIBI positive group compared to that of negative group independent of 131I scan results. Although the detectability of both 99mTc-MIBI and 201Tl were inferior to that of 131I, 9 to 22% of metastasis were detected only by these radiopharmaceuticals. Both 99mTc-MIBI and 201Tl, therefore, should be used in cases with high serum Tg even with negative 131I uptake. Basing on the fact there was no prominent difference between 99mTc-MIBI and 201Tl in the detectability of metastasis, 99mTc-MIBI might be more suitable tracer because of better quality image.

Adult↗
PubMed1998

Identification of a novel splicing mutation and 1-bp deletion in the 17alpha-hydroxylase gene of Japanese patients with 17alpha-hydroxylase deficiency.

We report studies of two unrelated Japanese patients with 17alpha-hydroxylase deficiency caused by mutations of the 17alpha-hydroxylase (CYP17) gene. We amplified all eight exons of the CYP17 gene, including the exon-intron boundaries, by the polymerase chain reaction and determined their nucleotide sequences. Patient 1 had novel, compound heterozygous mutations of the CYP17 gene. One mutant allele had a guanine to thymine transversion at position +5 in the splice donor site of intron 2. This splice-site mutation caused exon 2 skipping, as shown by in vitro minigene expression analysis of an allelic construct, resulting in a frameshift and introducing a premature stop codon (TAG) 60 bp downstream from the exon 1-3 boundary. The other allele had a missense mutation of His (CAC) to Leu (CTC) at codon 373 in exon 6. These two mutations abolished the 17alpha-hydroxylase and 17,20-lyase activities. Restriction fragment length polymorphism (RFLP) analysis with a mismatch oligonucleotide showed that the patient's mother and brother carried the splice-site mutation, but not the missense mutation. Patient 2 was homozygous for a novel 1-bp deletion (cytosine) at codon 131 in exon 2. This 1-bp deletion produces a frameshift in translation and introduces a premature stop codon (TAG) proximal to the highly conserved heme iron-binding cysteine at codon 442 in microsomal cytochrome P450 steroid 17alpha-hydroxylase (P450c17). RFLP analysis showed that the mother was heterozygous for the mutation.

Adolescent↗
PubMed1996

Multiple endocrine neoplasia type 1 associated with malignant lymphoma and other complications.

A 49-year-old female with multiple endocrine neoplasia (MEN) type 1 associated with malignant lymphoma, lipoma, functioning adenomatous goiter, non-functioning adrenal tumor, polyneuropathy, postoperative primary hyperparathyroidism, and hepatitis B virus was a human T lymphotropic virus type 1 (HTLV-1) carrier. She underwent parathyroidectomy for primary hyperparathyroidism at age 44. At age 49, examinations of the enlarged para-aortic lymph nodes revealed diffuse small non-cleaved B cell lymphoma in stage II, and other various complications were also found. Multiple tumorigenetic factors were considered to be involved in the present case.

Adrenal Gland Neoplasms↗
PubMed1995

Thyroid anaplastic carcinoma producing granulocyte-colony-stimulating factor and parathyroid hormone-related protein.

A 65-year-old woman noticed a rapidly enlarging neck mass with tenderness and complained of dyspnea. She was diagnosed as having anaplastic thyroid carcinoma. She died of respiratory failure 14 days after admission. Marked leukocytosis and hypercalcemia were observed in the clinical course. Both serum granulocyte-colony-stimulating factor and parathyroid hormone-related protein levels were elevated. The cancerous tissue was also immunohistochemically stained for both peptides. We conclude that the leukocytosis and hypercalcemia of this patient were induced by these two factors produced by the tumor.

Aged↗
PubMed1994

Localization of human neutrophil peptide (HNP) and its messenger RNA in neutrophil series.

Human neutrophil peptides (HNPs) 1,2 and 3, also called defensins, have high antimicrobial activity and are cytotoxic to both normal and transformed human cells. The localization of HNPs 1-3 and their mRNAs in cells of normal human bone marrow and peripheral blood was investigated. Immunoreactivity for HNPs 1-3 appeared in the promyelocyte stage and increased with the maturation of the neutrophil series. HNPs 1-3 were absent from such mononuclear phagocyte systems as peripheral monocytes, alveolar macrophages, and Kupffer cells in the liver. HNP 1-3 mRNAs were detected in bone marrow cells by Northern blot analysis and in peripheral leukocytes by the reverse transcription-polymerase chain reaction (RT-PCR). HNPs 1-3 are restricted to cells of neutrophil lineage and seem to function as microbicidal agents in the neutrophil-mediated defense system.

Adolescent↗
PubMed1993

Measurement of anti-thyroglobulin IgG in urine of patients with autoimmune thyroid diseases by sensitive enzyme immunoassay (immune complex transfer enzyme immunoassay).

Anti-thyroglobulin IgG in urine of patients with Graves' disease and chronic thyroiditis and healthy subjects was measured by a sensitive enzyme immunoassay (immune complex transfer enzyme immunoassay). Anti-thyroglobulin IgG in dialyzed urine was reacted simultaneously with 2,4-dinitrophenylated thyroglobulin and thyroglobulin-beta-D-galactosidase conjugate. The immune complex formed consisting of the three components was trapped onto polystyrene balls coated with (anti-2,4-dinitrophenyl group) IgG, eluted with epsilon N-2,4-dinitrophenyl-L-lysine, and transferred onto polystyrene balls coated with (anti-human IgG gamma-chain) IgG. beta-D-Galactosidase activity bound to the last polystyrene balls was assayed by fluorometry. Anti-thyroglobulin IgG was detected in most of the patients, but not in most of the healthy subjects; levels of anti-thyroglobulin IgG in urine of the patients were well correlated to those in serum of the same patients. The measurement of anti-thyroglobulin IgG in urine by the immune complex transfer enzyme immunoassay was suggested to be useful as a diagnostic aid for autoimmune thyroid diseases. The conventional standard ELISA was not sufficiently sensitive for measuring anti-thyroglobulin IgG in urine.

Adolescent↗
PubMed1993

Improved measurement of anti-thyroglobulin IgG in urine of patients with autoimmune thyroid diseases by sensitive enzyme immunoassay (immune complex transfer enzyme immunoassay.

Previously, antithyroglobulin IgG was assayed in dialyzed urine from patients with autoimmune thyroid diseases by a sensitive enzyme immunoassay (immune complex transfer enzyme immunoassay), and most of the assay results were useful as a diagnostic aid for autoimmune thyroid diseases. However, dialysis of urine was laborious and time-consuming, and some results were less reliable due to low levels of anti-thyroglobulin IgG in urine. This paper describes some improvements of the assay. Useful assay results could be obtained for most of urine samples without dialysis, although some interfering substance(s) was suggested to be present in some urine samples before dialysis. Accurate assay results with no interference could be obtained after gel filtration by only two min centrifugation in place of dialysis. More reliable assay results for urine samples containing low levels of antithyroglobulin IgG were obtained after concentration using a molecular sieve.

Animals↗
PubMed1992

Islet amyloid polypeptide (IAPP) and pancreatic islet amyloid deposition in diabetic and non-diabetic patients.

Twenty pancreata of non-diabetic patients and 17 pancreata of diabetic patients, including two patients with insulin-dependent diabetes mellitus, were immunohistochemically studied using antiserum against human islet amyloid polypeptide (IAPP). The islet beta cells in non-diabetic patients were immunoreactive for both IAPP and insulin. Amyloid deposition immunoreactive for IAPP was detected in six of 20 pancreata of non-diabetic patients. The plasma glucose level of three of these six patients was elevated to more than 200 mg/dl, and that of the other three ranged from 143 to 162 mg/dl; all six were receiving intravenous hyper-alimentation and had no history of diabetes prior to treatment. Amyloid deposition was present in all patients with non-insulin-dependent diabetes mellitus (NIDDM). The deposition was absent in the pancreata of two secondary diabetic patients, one of whom had received steroid hormone for bronchial asthma and the other of whom had liver cirrhosis with hepatocellular carcinoma; deposition was also absent in the pancreas of a patient with impaired glucose tolerance diagnosed on a 75-g oral glucose load. Heterogeneous expression of immunoreactivities of beta cells for insulin and for IAPP was present, suggesting independently regulated production and secretion of the peptides. Immunoreactivity of beta cells was more sensitively decreased for IAPP than for insulin in the islets of NIDDM patients. The decreased immunoreactivity for IAPP suggested an initial stage of disturbed beta-cell function, even if the immunoreactivity for insulin was apparently intact or the amyloid deposition in the islets was insignificant. The degree of amyloid deposition immunoreactivity for IAPP did not necessarily reflect the severity of diabetes mellitus. Amyloid deposits were seen at the narrow spaces beneath the insular capsule of connective tissues and the perivascular region or, in some cases, occupying the whole of the islet. The diabetogenic role of IAPP is unclear, but the deposition might be an accelerating factor which disturbs beta-cell function.

Adult↗
PubMed1992

Plasma islet amyloid polypeptide levels in obesity, impaired glucose tolerance and non-insulin-dependent diabetes mellitus.

We examined the response of plasma islet amyloid polypeptide (IAPP) to an oral glucose load in non-obese and obese subjects with normal glucose tolerance or impaired glucose tolerance (IGT), and in non-obese patients with non-insulin-dependent diabetes mellitus (NIDDM). Plasma IAPP response to intravenous glucagon injection in NIDDM patients was also studied. Plasma IAPP concentration was determined by a sensitive and specific radioimmunoassay. Basal levels of plasma IAPP in non-obese subjects with normal glucose tolerance, IGT and NIDDM were not significantly different from each other. Non-obese subjects with IGT showed delayed and higher plasma IAPP response to oral glucose load compared to normal non-obese subjects. In NIDDM patients, IAPP response to glucose was delayed and lower when compared to normal non-obese subjects. Basal levels of plasma IAPP in normal obese subjects and obese subjects with IGT were significantly higher than those in normal non-obese subjects. Plasma IAPP response to glucose load in these obese subjects was higher than that in normal non-obese subjects. Plasma IAPP response was decreased in diabetic patients treated with diet, oral hypoglycemic agents and insulin in that order. We conclude that the secretion of IAPP is reduced with progression of NIDDM, although it appears to be rather augmented in IGT compared to normal non-obese subjects.

Adult↗
PubMed1992

[A case of loxoprofen-induced pulmonary eosinophilia].

A 65-year-old female suffering from lumbago, headache, and hypertension had been treated with nonsteroidal anti-inflammatory drugs (NSAIDs) and antihypertensive drugs. On June 13, 1990, 2 weeks after the commencement of loxoprofen administration, she developed cough and low grade fever. She was treated with antibiotics and NSAIDs without improvement. Laboratory data showed marked eosinophilia (2200/mm3), elevation of IgE (3090 IU/ml), and liver dysfunction. Her chest X-ray revealed no active lesion, but the percentage of eosinophils in BALF was elevated (38%). Because drug-induced eosinophilic pneumonia was suspected, all drugs were discontinued. Her symptoms improved and the abnormalities of laboratory data normalized. The lymphocyte stimulation test was weakly positive with three NSAIDs (loxoprofen, pranoprofen, and alminoprofen). The challenge test by loxoprofen reproduced eosinophilia and liver dysfunction, suggesting that she had loxoprofen-induced eosinophilic pneumonia. To our knowledge, this is the first reported case of loxoprofen-induced lung injury.

Aged↗
PubMed1991

Identification and characterization of islet amyloid polypeptide in mammalian gastrointestinal tract.

We identified and determined the content and molecular form of islet amyloid polypeptide (IAPP/amylin) in the gastrointestinal (GI) tract of human, rat, mouse and cat. IAPP was isolated by anti- IAPP- IgG immunoaffinity chromatography and reverse-phase high performance liquid chromatography coupled with radioimmunoassays for human and rat/mouse IAPPs. Human IAPP [1-37], [17-37] and [24-37] were identified in human stomach with IAPP [1-37] being the major molecular form. In the GI tract of rat, mouse and cat, IAPP [1-37] and IAPP [19-37] were identified with the latter being the major molecular form. IAPP is present from stomach to colon with the highest concentration being observed in pyloric antrum of stomach. IAPP content in rat antrum fell to 69% of control after 4 days of fasting, with the molar ratio of IAPP [19-37] to IAPP [1-37] increasing from 1.4 in controls to 2.9 in fasted rats. Identification of IAPP and characteristic morphology of IAPP- cells in the GI tract indicate a possible biological function of IAPP as a gastrointestinal peptide.

Aged↗
PubMed1991

Islet amyloid polypeptide in insulinoma and in the islets of the pancreas of non-diabetic and diabetic subjects.

Amyloid deposition is a common pathological feature in insulinoma and in the islets of the pancreas in type-2 diabetic patients. The present immunohistochemical study revealed that normal B-cells, insulinoma, and amyloid deposits in insulinoma and diabetic pancreatic islets were commonly immunoreactive with antiserum to C-terminal synthetic tetradecapeptide of human islet amyloid polypeptide (IAPP) (24-37). Amyloid fibrils in insulinoma were also positive to IAPP by immunoelectron microscopy. A high level of IAPP was detected in the plasma and tissue of a insulinoma patient by radioimmunoassay suggesting that amyloid deposition in insulinoma is due to overproduction of IAPP. Amyloid deposits immunoreactive to IAPP were also seen in all diabetic pancreatic islets, but in no non-diabetic islets. There was much amyloid deposition in the islets of severe diabetics, whose B-cells demonstrated decreased immunoreactivities for IAPP and insulin. The IAPP content of the pancreas was 649.0 and 847.7 pg/mg wet weight in each of two diabetic patients, and 1034.6 and 1447.7 pg/mg wet weight in two non-diabetic patients. The present study revealed that IAPP is a bioactive peptide secreted from islet B-cells and are amyloidogenic peptide concerned in diabetogenensis and/or the progression of type-2 diabetes mellitus.

Adult↗
PubMed1990

Islet amyloid polypeptide (IAPP) in the gastrointestinal tract and pancreas of man and rat.

An immunohistochemical study for islet amyloid polypeptide (IAPP) was made on the gastrointestinal (GI) tract and pancreas of man and rat, using antisera raised against a synthetic peptide of C-terminal human IAPP (24-37) and a synthetic peptide of rat IAPP (18-37). A large number of IAPP-immunoreactive cells were found in the pyloric antrum, and a small number in the body of the stomach in both man and rat. Cytoplasmic processes extended out from the bipolar peripheral region of the immunoreactive cells, rather like neuronal processes, and some appeared to make contact with other immunoreactive cells. In addition, small numbers of immunoreactive cells were also seen in the duodenum and rectum, whereas they were absent from the jejunum, ileum and large intestine. An examination was made for evidence of colocalization of IAPP-immunoreactive material with material immunoreactive for gastrin, somatostatin, vasoactive intestinal polypeptide, pancreatic polypeptide, insulin, and glucagon, but none was found. IAPP-immunoreactive cells were also found in the pancreas of non-diabetic and non-insulin-dependent diabetic patients, but they were completely absent from a patient with insulin-dependent diabetes mellitus despite the presence of IAPP in the plasma. The results of these studies suggest that the peptide may have a biological role in situ in the GI tract and, in addition to the pancreas, may be a possible source of plasma IAPP.

Adult↗
PubMed1990

Chicken atrial natriuretic peptide (chANP) and its secretion.

An immunohistochemical study using antiserum raised against synthetic chicken natriuretic polypeptide was used to investigate the distribution of this peptide in the chicken heart. Immunoreactive cells, both in the atrial and ventricular walls, were identified by electron microscopy, and electron-dense granules in the atrial and ventricular cardiocytes were revealed to be storage sites of the peptide. The electron-dense material, thought to be the peptide, was found in the sarcoplasmic reticulum, and it is suggested that a secretory pathway of the peptide through the latter to extracellular space, may be present, in addition to an exocytotic one.

Aging↗
PubMed1988

Distribution of atrial natriuretic polypeptide (ANP)-containing cells in the rat heart and pulmonary vein. Immunohistochemical study and radioimmunoassay.

The distribution of atrial natriuretic polypeptide (ANP) was immunohistochemically surveyed in the rat heart and lung using an antiserum raised against alpha-human ANP. The ANP-immunoreactive cells were seen to be distributed in the atrial walls and proximal portions of the pulmonary vein and venae cavae, but were absent from the aorta, pulmonary arteries, trachea, bronchus, and alveolar cells. The immunoreactive cells were present in a narrow region just beneath the endothelium of the pulmonary vein and vena cavae, and, ultrastructurally and immunocytochemically, were seen to be striated muscle cells with ANP-containing specific granules similar to those seen in atrial cardiocytes. A radioimmunoassay for ANP revealed a content of 604 +/- 51 pg/mg wet weight in the pulmonary vein, and 3343 +/- 1620 pg/mg wet weight in the venae cavae. In addition to the atrial wall, the proximal portion of both the pulmonary vein and venae cavae are suggested to be constituents of an ANP-producing organ.

Animals↗
PubMed1988

Atrial-specific granules in the hearts of normal and water-deprived rats.

The morphology of atrial-specific granules, which contain atrial natriuretic polypeptide (ANP), was studied in the cardiac tissue of untreated controls and water-deprived rats by means of conventional and immunoelectron microscopy. Immature secretory vesicles or granules appeared to become buded off from the Golgi cisternae and then fused to form specific A-granules. An electron-dense plate with a fuzzy coat was frequently found on the limiting membrane at the end of such fusion. Pale specific B-granules, which were less electron-dense, larger, and more granular than A-granules, were found in small numbers in the left atrial cardiocytes, but rarely in the right ones. Very pale granules with a less granular matrix, considered to be B-type granules which had lost their electron-density, and which had less immunoreactivity for ANP, were numerous in the cardiac tissue after water deprivation. This morphological change, which is interpreted as an indication of granule degradation, was in agreement with the noted increase of natriuretic activity in the atrial tissue of water-deprived specimens.

Animals↗