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T Sugimoto

Publications and source records attributed to T Sugimoto.

At least 451 records · Page 25Linked to original sources

Right ventricular ejection fraction in the preoperative risk evaluation of candidates for pulmonary resection.

The major determinants of postoperative morbidity and mortality after lung resection are the physiologic and functional statuses of the pulmonary and cardiac systems. In our previous study, serial measurements of right ventricular performance after pulmonary resection demonstrated significant right ventricular dysfunction in the postoperative period. This study evaluates the preoperative measurement of right ventricular ejection fraction as a predictor of postoperative complications. In addition to conventional cardiopulmonary functional tests, right ventricular function was assessed with a thermodilution technique at rest and during exercise in 18 patients before and 3 weeks after lobectomy or pneumonectomy. The patients were grouped according to severity of right ventricular functional defect: right ventricular ejection fraction of at least 45% (group Ia, n = 8), right ventricular ejection fraction less than 45% (group Ib, n = 10), exercise-induced increases in right ventricular ejection fraction (group IIa, n = 8), and exercise-induced decreases in right ventricular ejection fraction (group IIb, n = 10). Postoperative cardiopulmonary morbidity was recorded for two patients (25%) in group Ia, three patients (30%) in group Ib, no patients (0%) in group IIa, and five patients (50%) in group IIb. Postoperative hospital stay was 28.9 +/- 8.5 days in group Ia, 29.9 +/- 20.2 days in group Ib, 19.4 +/- 8.0 days in group IIa, and 37.5 +/- 15.9 days in group IIb (p < 0.05, group IIa vs group IIb). Although resection-induced changes in forced expiratory volume in 1 second did not differ significantly between group Ia and group Ib, these values appeared to be increased in groups IIa (not statistically significant) and IIb (significantly, p < 0.05). The measured postoperative values of forced expiratory volume in 1 second and vital capacity were significantly higher than the predicted postoperative values (p < 0.05) in group IIa, but not in groups Ia, Ib, and IIb. We conclude that evaluation of right ventricular performance is useful in determining which patients are at increased risk for medical complications after lung resection. Exercise-induced change in right ventricular ejection fraction may be a better indicator of high risk among candidates for pulmonary resection than the absolute value of this parameter.

Aged↗

Functional role of ventral respiratory group expiratory neurons during vocalization.

The activities of expiratory neurons of the caudal ventral respiratory group (cVRG) (n = 31) were recorded extracellularly during vocalization in unanesthetized, decerebrate cats. Vocalization was induced by electrical stimulation (0.2 ms, 20-80 microA, 100 Hz, lasting for 2-5 s) of the periaqueductal gray (PAG). The firing rates of more than two-thirds of the neurons (24/31) increased during periods of vocalization induced by stimulation of the PAG, with an increase in abdominal muscle activities. The axons of most of these neurons (19/24) projected to the contralateral lumbar spinal cord, and one-third of the bulbospinal neurons (6/19) were orthodromically activated by stimulation of the PAG. Even after sectioning of the axons of bulbospinal cVRG neurons by midsagittal lesion between the obex and the C1 spinal cord, stimulation of the PAG still induced adduction of the vocal cords and vocalization. However, activities of abdominal muscles during vocalization were abolished. These results indicate that the efferent signals for vocalization from the PAG may be relayed at the cVRG neurons and converted into adequate activation of these neurons, contributing to the activation of the abdominal muscles for vocalization.

Abdominal Muscles↗

Voltage-gated ionic channels in cultured rabbit articular chondrocytes.

The membrane properties of cultured cells of rabbit articular chondrocytes were studied using the whole-cell patch clamp technique. The average cell capacitance was 37.9 +/- 9.0 pF (n = 13), and the cell resting potential was -41.0 +/- 7.0 mV (n = 11). We were unable to induce an action potential by applying a depolarizing current. Upon step depolarization, under voltage clamp conditions, one kind of inward and two kinds of outward currents were elicited. The inward current was initially observed at around -30 mV, peaked at 0 mV, and reversed at around +90 mV. Tetrodotoxin (TTX; 1 microM) was shown to completely block this inward current. At steady state, the inward current was half-inactivated at -51 mV, with a slope factor of 6.3 mV. Two outward currents were determined from measurements of activation threshold, reversal potential, and pharmacological responses. One was observed at around -30 mV, and its amplitude increased with membrane depolarization. Extracellularly applied 4-aminopyridine (4 AP) (1 mM) and tetraethyl ammonium chloride (TEA) (5 mM) blocked this current. The other outward current was observed at around +10 mV, and its direction reversed at a potential close to that predicted by the Nernst equation for a Cl- selective channel. This current fluctuated markedly, and the fluctuation did not decline throughout the 100 ms of the step pulse. Extracellularly applied 4-acetamido-4'-isothiocyanostilbenezene-2,2-disulfonic acid (SITS) (0.25 mM) blocked this current, but the same dose of 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS) had little effect. These results suggest the presence of TTX-sensitive Na+, 4-AP- and TEA-sensitive K+, and SITS-sensitive Cl- channels in rabbit articular chondrocyte membrane. The functional significance of these channels is discussed.

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid↗

Differential inhibition of mesangial MAP kinase cascade by cyclic nucleotides.

The agents which increase intracellular cyclic AMP (cAMP) or cyclic GMP (cGMP) have been found to counteract the effects of the vasoconstrictive agents such as endothelin-1 (ET-1). To clarify the mechanism of this interaction, we evaluated the activities of mitogen-activated protein kinase (MAPK) cascade, one of the important signal transduction system of ET-1. Beraprost sodium, an analogue of PGI2, and adrenomedullin, a cAMP-raising agent, inhibited ET-1-induced activation of MAPK. Dibutyryl cAMP (Bt2-cAMP) and 8-bromo-cGMP (8-Br-cGMP), cell permeable analogues of cAMP and cGMP, were also able to inhibit the activation of MAPK and MAPK kinase (MAPKK) by ET-1 without interfering basal activities. In contrast, phorbol 12, 13-dibutylate (PDBu)-induced activation of MAPK and MAPKK was inhibited by Bt2-cAMP but not by 8-Br-cGMP. Interestingly, atrial natriuretic peptide (ANP) partially inhibited PDBu-induced activation of MAPK and MAPKK. These results indicate that cAMP and cGMP inhibit ET-1-induced activation of MAPK in cultured mesangial cells at different steps; the former might inhibit at a step downstream of PKC and the latter prior to PKC. The data also suggest that ANP might have cGMP-independent effect on MAPK.

Adrenomedullin↗

Emergence of proteases in germinating cucumber cotyledons and their roles in the two-step degradation of storage protein.

The degradation of storage protein in germinating cucumber seeds was shown to proceed via two distinct steps. First, several proteases with acidic isoelectric points (pIs) were involved in solubilization and partial degradation of 11S globulin. Treatment of seedlings with cycloheximide inhibited this step and the expression of these proteases. Thus, the first step appeared to be governed by these proteases, which were synthesized de novo after imbibition. The first step was observed in dark-grown cotyledons, but the complete degradation of 11S globulin did not occur in the absence of illumination. An additional protease, with a pI of 4.5, was induced by illumination, and it was involved in the further cleavage of the partially degraded products of 11S globulin. Thus, the complete degradation of the storage protein proceeded via a two-step process in illuminated germinating seedlings. Light is needed to induce the second step in the degradation of 11S globulin that supplies the nitrogen required for development of the photosynthetic apparatus in the greening cotyledon.

Amino Acid Sequence↗

Expression of bone marrow stromal cell specific antigen during murine development: its expression in embryonic hematopoietic tissues as well as in other developing tissues.

Monoclonal antibody R4-A9 demonstrated specificity for a cell surface antigen of stromal cells in murine bone marrow and spleen. In order to identify patterns of expression that may elucidate the potential role of R4-A9 antigen, the developmental expression of this antigen in mouse embryos from 8 days post-coitum to 5 days post-partum was investigated by immunohistochemistry. At an early developmental stage, weak staining for R4-A9 antigen could be detected in the yolk sac. At later stages, strong staining of this antigen was detected predominantly in the embryonic liver, the main site of embryonic hematopoiesis. However, concomitant with the decreased staining in the liver, increased expression of this antigen was observed in bone marrow and spleen. Therefore, the changes in expression in those hematopoietic tissues suggest that its expression is coordinately regulated during the developmental stage of the sites of embryonic hematopoiesis. Compared with the distribution of R4-A9 antigen in adult tissues as previously reported, the expression of this antigen in fetal tissues was more widespread during the period of organogenesis, and was most abundant in other developing tissues, including the heart, skin, and lung. In contrast, fetal expression detected in hematopoietic and other developing tissues was lost after birth. These results taken together show a marked gradient of R4-A9 antigen expression, with the highest level at the peak of organ development, raising the possibility that this molecule may act as a growth/differentiation factor both in hematopoietic and other developing tissues in a fetus.

ADP-ribosyl Cyclase↗

Valproate metabolites in high-dose valproate plus phenytoin therapy.

PURPOSE: We wished to determine the relation between liver function, beta-, and omega-, and omega-1-oxidation metabolites and 4-en-valproate (VPA). METHODS: We measured the serum levels of VPA and its metabolites in children and adolescent receiving high-dose VPA plus phenytoin (PHT) therapy using gas chromatography-mass spectrometry with selected ion monitoring (GC/MS/ SIM). RESULTS: In high-dose VPA plus PHT polytherapy, the total VPA serum concentration was distinctly low, the concentrations of total beta-oxidation metabolites were decreased, the percentage values of VPA (percent of VPA) of total beta-oxidation metabolites were increased, and the E-2-en-VPA/3-keto-VPA ratios were decreased, as compared with those in high-dose VPA monotherapy. In high-dose VPA plus PHT polytherapy, 4-en-VPA (microM) was decreased and the concentrations of [omega + (omega-1)]-oxidation metabolites (microM) were decreased as compared with those in high-dose VPA monotherapy. In high-dose VPA plus PHT, serum glutamic-oxaloacetic transaminase (GOT), glutamic-pyruvic transaminase (GPT) and lactic dehydrogenase (LDH) did not correlate significantly with the ¿beta/omega + (omega-1)¿ metabolites ratio and 4-en-VPA levels, but serum GOT, GPT, and LDH were increased as compared with those in high-dose VPA therapy. We were not able to establish a significant relation between the formation of metabolites of VPA metabolites and liver dysfunction in patients receiving high-dose VPA and PHT concurrently. CONCLUSIONS: Metabolic levels do not appear to be a reliable predictor of hepatotoxicity in children receiving pharmacological antiepileptic drug (AED) therapy.

Adolescent↗

Effect of L-carnitine supplementation on acute valproate intoxication.

We analyzed urinary valproate (VPA) metabolites and carnitine concentrations in a child who accidentally ingested 400 mg/kg VPA. The concentration of 4-en VPA, the presumed major factor in VPA-induced hepatotoxicity, was markedly increased, without liver dysfunction or hyperammonemia. The other major abnormality was decreased beta-oxidation and markedly increased omega-oxidation. After L-carnitine supplementation, VPA metabolism returned to normal. The level of valproylcarnitine was not increased and therefore was not affected by L-carnitine. L-Carnitine may be useful in treating patients with coma after VPA overdose.

Ammonia↗

Latex agglutination test for canine parvovirus.

Canine parvovirus (CPV) was detected in faeces from dogs with diarrhoea by a specific slide agglutination test using latex particles coated with anti-CPV monoclonal antibody (LA-anti-CPV). The agglutination of LA-anti-CPV with CPV on a glass slide was evident macroscopically within 2 min. The sensitivity of the latex agglutination (LA) test was similar to that of the hemagglutination test. The LA test is available for the rapid diagnosis of CPV infection at an animal hospital.

Animals↗

Hormonal regulation of prostaglandin F2 alpha receptor gene expression in mouse ovary.

In this study we examined regulation by pituitary gonadotropins of the prostaglandin F2 alpha (PGF2 alpha) receptor gene expression in the mouse ovary. Administration of pregnant mare serum gonadotropin (PMSG) to 35-day-old mice in the diestrus phase stimulated the ovary and enhanced the production of progesterone at 1 h PMSG also increased the ovarian PGF2 alpha receptor mRNA level in a time-dependent manner, reaching a sixfold maximum at 1 h. These actions of PMSG were mimicked by human chorionic gonadotropin (hCG), follicle-stimulating hormone (FSH), and cholera toxin, all of which elevate intracellular adenosine 3',5'-cyclic monophosphate (cAMP). In situ hybridization revealed that PGF2 alpha receptor mRNA was localized to the corpus luteum, but the intensity of staining varied among corpora lutea in the same ovary. Exogenous PGF2 alpha inhibited the PMSG-stimulated progesterone production. These results demonstrate that gonadotropins may induce the expression of the PGF2 alpha receptor gene in luteal cells of the corpus luteum, probably by acting through a cAMP-mediated pathway, and that expression of the PGF2 alpha receptor may be functionally associated with the decrease in serum progesterone level.

Animals↗

Acute myelomonocytic leukaemia with 11q23 abnormality during multiple myeloma: is this related to anthracycline?

The clinical course of a 66-year-old man diagnosed with multiple myeloma is described. Chemotherapy including alkylating agents had no effect, and so he was treated with vincristine, doxorubicin, and dexamethasone. His bone tumor was treated with localized radiation after two courses of chemotherapy. After these treatments, monocytosis was found and dysplastic changes were noted in the bone marrow. A cytogenetic study revealed t(9;11)(p22;q23), an abnormality which had previously been absent. A diagnosis of myelodysplastic syndrome (MDS) was newly established, and transformation to acute non-lymphocytic leukaemia (ANLL) was observed 6 months later. The cumulative doses of melphalan, cyclophosphamide, doxorubicin, and radiation therapy were 432 mg, 4,200 mg, 120 mg, and 4,000 cGy, respectively. The cytogenetic abnormality suggested that this patient's MDS/ANLL was related to doxorubicin and not talk to alkylating agents, although the dose of doxorubicin administered was quite low.

Aged↗

Surgical treatment of refractory venous stasis ulcer due to a severe impairment of calf muscle pump function: evaluation by air plethysmography. A case report.

The authors encountered a forty-nine-year-old man with a lower limb ulcer refractory to intensive conservative therapy. No varicose vein was found anywhere, and the usual phlebographies and foot venous pressure measurement failed to diagnose it as a venous stasis ulcer. A direct phlebography method developed by the authors, in which a thin catheter is inserted into the deep vein, disclosed a reflux of the popliteal vein or a deep muscle branch from which an incompetent perforator arose toward the superficial vein above the ulcer. Air plethysmography (APG) showed a severe impairment of the calf muscle pump function. He underwent a subfascial ligation of two incompetent perforators together with a stripping of the great saphenous vein passing under the ulcer. Postoperatively, this ulcer was cured in an early phase, and the calf muscle pump function showed improvement in the APG.

Hemodynamics↗

Stimulatory effect of growth hormone on bone resorption and osteoclast differentiation.

Although the actions of GH on osteoblasts have been extensively investigated, its effects on osteoclasts remain unknown. In the present study, the effects of GH on bone resorption and osteoclast differentiation were examined in vitro. Bovine GH (bGH; 1-100 ng/ml) significantly stimulated bone resorption by preexistent osteoclasts in stromal cell-containing mouse bone cell cultures, whereas it did not affect the bone-resorbing activity of isolated rabbit osteoclasts. When bGH was added to unfractionated bone cells after degeneration of preexistent osteoclasts, it concentration dependently stimulated osteoclast-like cell formation. GH also enhanced 1,25-dihydroxyvitamin D3-induced osteoclast-like cell formation. Moreover, osteoclast-like cells newly formed from unfractionated bone cells in the presence of bGH possessed the ability to form pits on dentine slices. The conditioned medium from osteoblastic MC3T3-E1 cells or MC3T3-G2/PA-6 stromal cells pretreated with bGH stimulated osteoclast-like cell formation from mouse hemopoietic blast cells supported by granulocyte-macrophage colony-stimulating factor. On the other hand, the PCR products corresponding in size to the mouse GH receptor were detected in mouse hemopoietic blast cells as well as liver. GH concentration dependently stimulated osteoclast-like cell formation from these hemopoietic blast cells in the absence of stromal cells, and these osteoclast-like cells formed pits on dentine slices in the presence of MC3T3-G2/PA-6 stromal cells. The present study indicated for the first time that GH stimulates osteoclastic bone resorption through both its direct and indirect actions on osteoclast differentiation and through its indirect activation of mature osteoclasts, possibly via stromal cells, including osteoblasts.

Animals↗

Estrogen blocks parathyroid hormone (PTH)-stimulated osteoclast-like cell formation by selectively affecting PTH-responsive cyclic adenosine monophosphate pathway.

Several lines of evidence have previously indicated that estrogen inhibits PTH-induced bone resorption in vivo and in vitro. However, its mechanism remains unknown. Therefore, the present study was performed to investigate the effect of estrogen on PTH-stimulated osteoclast-like cell formation and clarify its mechanism. 17 beta-estradiol (17 beta-E2) significantly antagonized osteoclast-like cell formation stimulated by 10(-8) M human (h) PTH-(1-34) as well as 10(-8) M hPTH-related peptide (PTHrP)-(1-34)in osteoblast-containing mouse bone cell cultures. The conditioned medium derived from osteoblastic SaOS-2 cells or MC3T3-E1 cells pretreated with both PTH-(1-34) (10(-8)M) and 17 beta-E2(10(-8)M) stimulated osteoclast-like cell formation from hemopoietic blast cells more weakly than conditioned medium from cells pretreated with PTH-(1-34) alone. Moreover, 10(-8) M 17 beta-E2 significantly blocked the formation of osteoclast-like cells stimulated by 10(-8) M hPTH-(1-34) in spleen cell cultures derived from 5-fluorouracil-pretreated mice. On the other hand, 10(-8) M 17 beta-E2 significantly inhibited osteoclast-like cell formation stimulated by dbcAMP (10(-4)M) and Sp-cAMPS (10(-4)M), as well as forskolin (10(-5)M) in mouse bone cell cultures. In contrast, 10(-8)M 17 beta-E2 did not affect PMA (10(-7)M)-, A23187 (10(-7)M)-, or BAYK-8644 (5 x 10(-6) M)-stimulated osteoclast-like cell formation. In conclusion, the present study demonstrated that estrogen inhibits PTH-stimulated osteoclast-like cell formation by directly acting on hemopoietic blast cells as well as by indirectly acting on them via osteoblasts. The inhibitory effects of estrogen on PTH-stimulated osteoclast-like cell formation seemed to be mediated through blocking the cAMP-dependent protein kinase pathway but not by blocking calcium/protein kinase C.

Animals↗

Pericardiectomy and coronary artery bypass grafting for constrictive pericarditis after heart surgery.

A 63-year-old male was operated on for chronic heart failure due to myocardial ischemia and constrictive pericarditis after heart surgery. He was in New York Heart Association (NYHA) class III under a large dose of diuretics. He underwent a pericardiectomy and coronary bypass surgery without cardiopulmonary bypass. His cardiac function improved with a patent graft. He is now, 1 year after surgery, in NYHA class I under a tapering dose of diuretics.

Cardiac Output, Low↗

Purification and characterization of thermostable maltooligosyl trehalose synthase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius.

A thermostable maltooligosyl trehalose synthase was purified from a cell-free extract of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius ATCC 33909 to an electrophoretically homogeneous state by successive column chromatography on Sepabeads FP-DA13, Butyl-Toyopearl 650M, DEAE-Toyopearl 650S, Ultrogel AcA44, and Mono Q. The enzyme had a molecular mass of 74,000 by SDS-polyacrylamide gel electrophoresis and a pI of 5.9 by gel isoelectrofocusing. The N-terminal amino acid of the enzyme was methionine. The enzyme showed the highest activity from pH 5.0 to 5.5 and at 75 degrees C, and was stable from pH 4.5 to 9.5 and up to 85 degrees C. The enzyme activity was inhibited by Hg2+ and Cu2+. The Kms of the enzyme for maltotetraose, maltopentaose, maltohexaose, maltoheptaose, and short chain amylose (DP 18) were 41.5 mM, 7.1 mM, 5.7 mM, 1.4 mM, and 0.6 mM, respectively.

Amino Acid Sequence↗

Purification and characterization of thermostable maltooligosyl trehalose trehalohydrolase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius.

A thermostable maltooligosyl trehalose trehalohydrolase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius ATCC 33909 was purified from a cell-free extract to an electrophoretically pure state by successive column chromatographies on Sepabeads FP-DA13, Butyl-Toyopearl 650M, DEAE-Toyopearl 650S, Toyopearl HW-55S and Ultrogel AcA44. The enzyme had a molecular mass of 59,000 by SDS-polyacrylamide gel electrophoresis and a pI of 6.1 by gel isoelectrofocusing. The N-terminal amino acid of the enzyme was methionine. The enzyme showed the highest activity from pH 5.5 to 6.0 and at 75 degrees C, and was stable from pH 5.5 to 9.5 and up to 85 degrees C. The activity was inhibited by Hg2+, Cu2+, Fe2+, Pb2+, and Zn2+. The Km values of the enzyme for maltosyl trehalose, maltotriosyl trehalose, maltotetraosyl trehalose, and maltopentaosyl trehalose were 16.7 mM, 2.7 mM, 3.7 mM, and 4.9 mM, respectively.

Chemical Phenomena↗

Purification and properties of a novel enzyme, trehalose synthase, from Pimelobacter sp. R48.

A novel enzyme, trehalose synthase, was purified from a cell-free extract of Pimelobacter sp. R48 to an electrophoretically homogeneous state by successive chromatographies on DEAE-Toyopearl 650, Butyl-Toyopearl 650, and Mono Q HR5/5 columns. The molecular weight of the enzyme was estimated to be 62,000 by SDS-polyacrylamide gel electrophoresis, and the enzyme had a pI of 4.6 by gel isoelectrofocusing. The enzyme catalyzed the conversion of maltose into trehalose by intramolecular transglucosylation. The enzyme also converted into maltose but was inactive on other saccharides. The N-terminal amino acid of the enzyme was serine. The optimum pH and temperature were pH7.5 and 20 degrees C, respectively. The enzyme was stable in the range of pH 6.0-9.0 and up to 30 degrees C for 60 min. The rate of conversion of maltose into trehalose was independent of the maltose concentration. The maximum yield of trehalose from maltose were 81.8%, 80.9%, and 76.7% at 5, 15, and 25 degrees C, respectively. The activity was inhibited by Cu2+, Hg2+, Ni2+, Zn2+, and Tris.

Amino Acid Sequence↗