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Biomedical subjects

M Sone

Publications and source records attributed to M Sone.

At least 73 records · Page 4Linked to original sources
PubMed1998

[Report management system using Web server and search engine].

PURPOSE: To develop a management system of written reports using a Web server and search engine. METHODS: All the reports written through word processing software in the local area network in the radiology department were automatically transferred to one of the PC servers, in which a Web server and search engine were in operation. Previous reports, approximately eighty thousand, were also registered. Using Web browsers and the program developed by hypertext mark-up language and JavaScript, all the reports were readily accessible by keywords, or by any words within reports. RESULTS: Over 100, 000 reports were easily accessible using Web browsers, based on our one-year experience. Maintaining the Web server and search engine, and upgrading the program were easily managed in our daily practice. CONCLUSION: The report management system we developed is flexible, scalable, and easy to maintain. It is an effective way to manage a large volume of radiology reports written through word processing software.

Computer Communication Networks↗
PubMed1998

Mesothelial cell proliferation in the scala tympani: a reaction to the rupture of the round window membrane.

The inner layer of the round window membrane is composed of mesothelial cells and this mesothelial cell layer extends to the scala tympani. This study describes the histopathologic findings of temporal bone analysis from a patient with bilateral perilymphatic fistula of the round window membrane. The left ear showed proliferation of mesothelial cells in the scala tympani of the basal turn adjoining the round window membrane. This cell proliferation is thought to be a reaction to the rupture of the round window membrane.

Cell Division↗
PubMed1997

Regulation and immunohistochemical analysis of stress protein heme oxygenase-1 in rat kidney with myoglobinuric acute renal failure.

Intramuscular injection of hypertonic glycerol solution to rats results in acute renal injury. In this model, the proximal tubules are characteristically damaged. After glycerol injection renal glutathione (GSH) levels drastically decreased. On the other hand, stress protein heme oxygenase-1 (HO-1) was induced. When N-acetyl cysteine was administered to rats before 1 h glycerol injection, renal function was obviously improved. In this condition, the renal GSH content were sustained in the normal levels and HO-1 protein levels were decreased compared with those of glycerol-treated rats. Induction of HO-1 was accompanied by reduced renal GSH content. In addition, to investigate whether the location of HO-1 protein induced by glycerol injection is restricted to injured region or not in the kidney, we determined the localization of HO-1 protein using immunohistochemical staining. HO-1 protein was identified in the epithelia of the distal tubules, Henle's loop and collecting ducts, but not in the injured proximal tubules.

Acetylcysteine↗
PubMed1997

Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells.

DsbA, the disulfide bond catalyst of Escherichia coli, is a periplasmic protein having a thioredoxin-like Cys-30-Xaa-Xaa-Cys-33 motif. The Cys-30-Cys-33 disulfide is donated to a pair of cysteines on the target proteins. Although DsbA, having high oxidizing potential, is prone to reduction, it is maintained essentially all oxidized in vivo. DsbB, an integral membrane protein having two pairs of essential cysteines, reoxidizes DsbA that has been reduced upon functioning. It is not known, however, what might provide the overall oxidizing power to the DsbA-DsbB disulfide bond formation system. We now report that E. coli mutants defective in the hemA gene or in the ubiA-menA genes markedly accumulate the reduced form of DsbA during growth under the conditions of protoheme deprivation as well as ubiquinone/menaquinone deprivation. Disulfide bond formation of beta-lactamase was impaired under these conditions. Intracellular state of DsbB was found to be affected by deprivation of quinones, such that it accumulates first as a reduced form and then as a form of a disulfide-linked complex with DsbA. This is followed by reduction of the bulk of DsbA molecules. These results suggest that the respiratory electron transfer chain participates in the oxidation of DsbA, by acting primarily on DsbB. It is remarkable that a cellular catalyst of protein folding is connected to the respiratory chain.

Aerobiosis↗
PubMed1997

Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds.

Several Escherichia coli proteins participate in protein disulfide bond formation. Among them, DsbA is the primary factor that oxidizes target cysteines. Biochemical evidence indicates that DsbC has disulfide isomerization activity. To study intracellular functions of DsbA and DsbC, we used an alkaline phosphatase mutant, PhoA[SCCC], with the most amino-terminal cysteine replaced by serine. It was found that the remaining 3 cysteines in PhoA[SCCC] form a disulfide bond of incorrect as well as correct combinations. An aberrant disulfide bond was preferentially formed in wild-type cells, which was converted slowly to the normal disulfide bond. This conversion did not occur in the dsbC-disrupted cells. Overproduction of DsbC stimulated the formation of the correct disulfide bond. In contrast, the inefficiently formed disulfide bonds in the dsbA-disrupted cells, and the more efficiently formed disulfide bonds in the same strain in the presence of oxidized glutathione were mostly in the correct form. These results suggest that the DsbA-catalyzed reaction can be too rapid for some proteins. DsbA may simply oxidize available pairs of cysteines, which happen to be in an incorrect combination in the case of PhoA[SCCC]. In contrast, DsbC stimulates the formation of correct disulfide bonds and corrects previously introduced aberrant ones. Thus, DsbC acts to isomerize disulfide bonds in vivo.

Alkaline Phosphatase↗
PubMed1997

Roles of disulfide bonds in bacterial alkaline phosphatase.

Alkaline phosphatase of Escherichia coli (a homodimeric protein found in the periplasmic space) contains two intramolecular disulfide bonds (Cys-168-Cys-178 and Cys-286-Cys-336) that are formed after export to the periplasmic space. The location-specific folding character of this enzyme allowed its wide usage as a reporter of protein localization in prokaryotic cells. To study the roles of disulfide bonds in alkaline phosphatase, we eliminated each of them by Cys to Ser mutations. Intracellular stability of alkaline phosphatase decreased in the absence of either one or both of the disulfide bonds. The mutant proteins were stabilized in a DegP protease-deficient strain, allowing accumulation at significant levels and subsequent characterization. A mutant protein that lacked the N-terminally located disulfide bond (Cys-168-Cys-178) was found to have Cys-286 and Cys-336 residues disulfide-bonded, to have a dimeric structure, and to have almost full enzymatic activity. Nevertheless, the mutant protein lost the trypsin-resistant conformation that is characteristically observed for the wild-type enzyme. In contrast, mutants lacking Cys-286 and Cys-336 were monomeric and inactive. These results indicate that the Cys-286-Cys-336 disulfide bond is required and is sufficient for correctly positioning the active site region of this enzyme, but such an active conformation is still insufficient for the conformational stability of the enzyme. Thus, a fully active state of this enzyme can be formed without full protein stability, and the two disulfide bonds differentially contribute to these properties.

Alkaline Phosphatase↗
PubMed1997

Still life, a protein in synaptic terminals of Drosophila homologous to GDP-GTP exchangers.

The morphology of axon terminals changes with differentiation into mature synapses. A molecule that might regulate this process was identified by a screen of Drosophila mutants for abnormal motor activities. The still life (sif) gene encodes a protein homologous to guanine nucleotide exchange factors, which convert Rho-like guanosine triphosphatases (GTPases) from a guanosine diphosphate-bound inactive state to a guanosine triphosphate-bound active state. The SIF proteins are found adjacent to the plasma membrane of synaptic terminals. Expression of a truncated SIF protein resulted in defects in neuronal morphology and induced membrane ruffling with altered actin localization in human KB cells. Thus, SIF proteins may regulate synaptic differentiation through the organization of the actin cytoskeleton by activating Rho-like GTPases.

Actins↗
PubMed1997

Presence of adrenomedullin-like immunoreactivity in the human cerebrospinal fluid.

The presence of adrenomedullin-like immunoreactivity in the cerebrospinal fluid was studied by radioimmunoassay in 13 subjects with various neurological diseases. The concentrations of adrenomedullin-like immunoreactivity in the cerebrospinal fluid were 9.4 +/- 3.1 pmol/l (mean +/- SD, n = 13). Reverse-phase high performance liquid chromatography of the extract of the pooled cerebrospinal fluid showed that approximately 40% of the adrenomedullin-like immunoreactivity was chromatographically identical to human adrenomedullin (1-52). This is the first report that demonstrates the presence of adrenomedullin-like immunoreactivity in the human cerebrospinal fluid.

Adrenomedullin↗
PubMed1997

Expression of adrenomedullin mRNA in the human brain and pituitary.

We have recently reported the presence of immunoreactive (IR) adrenomedullin (ADM) in the human brain. In the present study, the expression of ADM mRNA was studied by Northern blot analysis in the human brain and pituitary, and the presence of IR-ADM in the human pituitary was studied by radioimmunoassay. ADM mRNA was clearly detected in every region of the brain examined and in the pituitary. High concentrations of IR-ADM were present in the whole pituitary (16.7 +/- 2.0 pmol/g wet weight, mean +/- SEM, n = 4). Reverse phase high performance liquid chromatography of the pituitary showed a peak eluting in the position of human ADM(1-52). These findings suggest that ADM acts as a neuromodulator or a neurotransmitter in the brain, and as an autocrine factor, a paracrine factor, or a neurohormone in the pituitary.

Adrenomedullin↗
PubMed1997

Specific adrenomedullin binding sites in the human brain.

Binding sites for adrenomedullin in human brain were investigated and characterized by radioligand binding. Specific binding sites for adrenomedullin were present in every region of human brain (cerebral cortex, cerebellum, thalamus, hypothalamus, pons and medulla oblongata) obtained at autopsy. Despite the homology with calcitonin gene-related peptide (CGRP), CGRP was a poor inhibitor of [125I]adrenomedullin binding (IC50 > 1 microM) compared with adrenomedullin(1-52) (IC50 = 1.2 +/- 0.5 nM, mean +/- SEM, n = 3). Three adrenomedullin fragments, adrenomedullin(1-12), adrenomedullin(22-52), and adrenomedullin(13-52), were also poor inhibitors of the binding (IC50 = 0.3 microM), suggesting that the whole molecule of adrenomedullin(1-52) is required for binding to the receptor. Scatchard plots of [125I]adrenomedullin binding in human brain (cerebral cortex) gave a dissociation constant of 0.17 +/- 0.03 nM and maximal binding of 99.3 +/- 1.9 fmol/mg protein (n = 5). These findings suggest that specific adrenomedullin binding sites that differ from the CGRP receptors exist in human brain. This indicates a possible novel neurotransmitter/neuromodulator role for adrenomedullin in human brain.

Adrenomedullin↗
PubMed1997

Production and secretion of adrenomedullin from glial cell tumors and its effects on cAMP production.

The expression of adrenomedullin (ADM) and its mRNA was studied in human glial cell tumors and cultured glioblastoma cell lines, T98G and A172. Northern blot analysis showed that ADM mRNA was expressed in all brain tumors examined (three anaplastic astrocytomas and two glioblastomas multiforme) and in the glioblastoma cell lines. Immunoreactive (IR-) ADM was detectable in these brain tumors by radioimmunoassay (0.31-2.0 pmol/g wet weight), except for one anaplastic astrocytoma. Reverse phase high performance liquid chromatography of the tumor extracts showed a single peak eluting in the position of ADM-(1-52). IR-ADM concentrations in the cultured media of T98G cells were 205.5 +/- 8.4 fmol/10(5) cells/24 h (mean +/- SEM, n = 5). Treatment of T98G cells with interferon gamma or interleukin 1 beta increased the expression levels of ADM mRNA and the IR-ADM concentrations in the cultured media, whereas tumor necrosis factor alpha decreased them in a dose-dependent manner. Treatment with synthetic ADM-(1-52) (10(-8) or 10(-7) mol/l) increased the cAMP concentrations in the cultured media of T98G cells. These findings suggest that ADM is secreted from glial cell tumors and is related to the pathophysiology of these tumors.

Adrenomedullin↗
PubMed1997

A case of pleomorphic adenoma of the epiglottis. Bilateral vocal-cord paralysis after YAG laser surgery.

Pleomorphic adenoma of the larynx is a rare disorder, and until recently has been treated mainly by approaches involving pharyngotomy. We encountered a case of pleomorphic adenoma originating from the laryngeal surface of the epiglottis and removed it using a YAG laser through a suspension laryngoscope. This case was complicated by delayed-onset bilateral vocal-cord paralysis, the causes of which are also discussed.

Adenoma, Pleomorphic↗
PubMed1997

Molecular cloning of rat p38 mitogen-activated protein kinase and it's osmotic regulation in rat kidney.

Rat p38 mitogen-activated protein (MAP) kinase cDNA was isolated from rat kidney cDNA library using a PCR cloning strategy. The deduced amino acid sequence consists of 360 amino acids and shares 95.3% similarity with human p38 MAP kinase. The message for rat p38 MAP kinase was about 3.4 kilobases and was highly expressed in the kidney. In water-deprived rat kidneys, the steady-state levels of p38 MAP kinase mRNA increased about 2.7-fold as compared with those of control rats. This result suggests that p38 MAP kinase may play an important role in the osmoregulation in the kidney.

Amino Acid Sequence↗
PubMed1997

Cerebellin and cerebellin mRNA in the human brain, adrenal glands and the tumour tissues of adrenal tumour, ganglioneuroblastoma and neuroblastoma.

The expression of cerebellin and cerebellin mRNA was studied by radioimmunoassay and Northern blot analysis in the human brain, adrenal gland and the tumour tissues of adrenal tumour, ganglioneuroblastoma and neuroblastoma. Immunoreactive cerebellin was detected in every region of brain studied, with the highest concentrations found in the hemisphere of the cerebellum (424.2 +/- 12.6 pmol/g wet weight, n = 6, mean +/- S.E.M.) and the vermis of the cerebellum (256.8 +/- 30.5 pmol/g wet weight). Immunoreactive cerebellin was also detected in the pituitary (8.2 +/- 1.8 pmol/g wet weight), the spinal cord (3.3 +/- 0.3 pmol/g wet weight) and the normal parts of adrenal glands (2.98 +/- 0.37 pmol/g wet weight, n = 9) and some tumour tissues, such as phaeochromocytomas, cortisol-producing adrenocortical adenomas, ganglioneuroblastomas and neuroblastomas. Northern blot analysis showed that cerebellin mRNA was highly expressed in the hemisphere and vermis of the cerebellum. Cerebellin mRNA was also expressed in other regions of the brain and the tumour tissues of phaeochromocytoma, cortisol-producing adrenocortical adenoma, ganglioneuroblastoma and neuroblastoma. Immunocytochemistry of the normal adrenal gland showed that immunoreactive cerebellin was localized in the adrenal medulla. The present study has shown the expression of cerebellin and cerebellin mRNA, not only in the cerebellum but also in other regions of the brain and some tumours, such as cortisol-producing adrenocortical adenoma, phaeochromocytoma and neuroblastoma. These findings suggest possible pathophysiological roles of cerebellin peptides, not only in the cerebellum, but also in the extra-cerebellar tissues.

Adenoma↗
PubMed1997

Immunoreactive adrenomedullin in human adrenal glands and adrenal tumors.

Adrenomedullin is a potent vasodilator peptide that was isolated from human pheochromocytoma. We developed a sensitive and specific radioimmunoassay for adrenomedullin and studied the presence of adrenomedullin in human adrenal glands and adrenal tumors, including pheochromocytoma. High concentrations of immunoreactive adrenomedullin were found in normal parts of adrenal glands (cortex and medulla) (12.6 +/- 1.0 pmol/g wet wt, N = 7, mean +/- SEM). High concentrations of immunoreactive adrenomedullin were also present in the tumor tissues of pheochromocytoma (4.5 +/- 1.5 pmol/g wet wt, N = 11). Immunoreactive adrenomedullin was detected in some adrenocortical tumors, but these concentrations were much lower than those in the normal adrenal glands and pheochromocytomas. Reverse phase high-performance liquid chromatography of the normal adrenal gland and pheochromocytoma showed a peak eluting in the position of synthetic adrenomedullin 1-52. The present study has shown the presence of high concentrations of immunoreactive adrenomedullin in the normal adrenal glands and pheochromocytomas.

Adenocarcinoma↗
PubMed1997

[Radiology information system using HTML, JavaScript, and Web server].

We have developed a radiology information system using intranet techniques, including hypertext markup language, JavaScript, and Web server. JavaScript made it possible to develop an easy-to-use application, as well as to reduce network traffic and load on the server. The system we have developed is inexpensive and flexible, and its development and maintenance are much easier than with the previous system.

Local Area Networks↗