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Biomedical subjects

K Fukuyama

Publications and source records attributed to K Fukuyama.

At least 37 records · Page 2Linked to original sources
PubMed2000

[Clinical study of cerebral blood flow in unilateral chronic subdural hematoma measured by 99mTc-HMPAO SPECT].

Cerebral blood flow (CBF) measured by 99mTc-HMPAO SPECT before operation was studied in 60 patients with unilateral chronic subdural hematoma. The regional CBF was measured in 26 regions of the fronto-occipital 10 cortices, putamen, thalamus and cerebellar hemisphere on both sides. Sixty cases with unilateral chronic subdural hematoma were classified into four groups on the basis of clinical symptoms: 17 cases with headache (headache group), 34 cases with hemiparesis (hemiparesis group) and 9 cases with consciousness disturbance or dementia (consciousness disturbance group), and into three groups on the basis of the degree of midline brain shift on MRI: 7 cases of mild shift group, 24 cases of moderate shift group and 29 cases of severe shift group. The average CBF in 60 patients in each region indicated that the regional CBF was reduced in frontal, occipital cortices and cerebellum on the non-hematoma side, and in putamen and thalamus on the hematoma side. In the headache group, the regional CBF reduction on the non-hematoma side was found in only frontal and occipital cortices compared with the corresponding regions on the hematoma side. In the hemiparesis group, the regional CBF was reduced in frontal and occipital cortices on the non-hematoma side and in putamen and thalamus on the hematoma side. The part of CBF reduction in both hemispheres was also noted in the hemiparesis group. In the consciousness disturbance group, the CBF reduction was markedly noted in whole brain. The CBF reductions in frontal and occipital cortices on the non-hematoma side and in putamen, thalamus and cerebellum on the hematoma side was not mutually related with the degree of midline brain shift. We concluded that the disturbance of CBF in chronic subdural hematoma was started from frontal and occipital cortices on the non-hematoma side observed in the headache group, and which was extended to putamen and thalamus on the hematoma side and a part of both hemispheres observed in the hemiparesis group. And such disturbance was finally observed as the CBF reductions in whole brain in the consciousness disturbance group.

Adolescent↗
PubMed2000

[Clinical study of cerebral blood flow in bilateral chronic subdural hematoma measured by 99mTc-HMPAO SPECT].

Cerebral blood flow(CBF) in 34 patients with bilateral chronic subdural hematoma was measured by 99mTc-HMPAO SPECT before operation. The regional CBF was measured in 26 regions of the 10 cortical regions, putamen, thalamus and cerebellar hemisphere on both sides. According to the thickness of subdural hematoma, the thicker hematoma side was measured and examined as the thick hematoma side, and the other side as the thin hematoma side. Thirty four cases with bilateral chronic subdural hematoma were classified into four groups on the basis of clinical symptoms: 13 cases with headache(headache group), 10 cases with hemiparesis(hemiparesis group), 5 cases with tetraparesis(tetraparesis group) and 6 cases with consciousness disturbance or dementia(consciousness disturbance group), and into two groups according to the degree of midline brain shift on MRI: 14 cases of non-shifted group and 20 cases of shifted group. The average CBF of 34 patients in each region indicated a regional CBF reduction in the frontal, parietal and occipital cortices on the thin hematoma side, and in the putamen on the thick hematoma side. In the headache group, the regional CBF reduction on the thin hematoma side was found in the frontal, parietal and occipital cortices compared with the corresponding regions on the thick hematoma side, and in thalamus on the thick hematoma side. In the hemiparesis and tetraparesis groups, there was no statistically significant CBF reduction between the thick and thin hematoma sides. In the consciousness disturbance group, the CBF reduction in whole brain was remarkably significant. By the degree of the midline brain shift, the CBF reductions between the thick and thin hematoma sides were observed. Namely, in the shifted group, the CBF reductions were noted in the frontal, parietal and occipital cortices in the thin hematoma side, and in the putamen in the thick hematoma side. We concluded that the CBF reduction of bilateral chronic subdural hematoma was bilaterally found in the hemiparesis and tetraparesis groups, and which was finally observed in whole brain in the consciousness disturbance group.

Adult↗
PubMed2000

[Simple antireflux measures for management of gastroesophageal reflux disease].

It is widely accepted that proton pump inhibitors are the most effective therapy for management of gastroesophageal reflux disease. H2-receptor antagonists, prokinetic agents, and antacids are used in treatment of gastroesophageal reflux disease. In addition to these medical treatments, beneficial effects of simple anti-reflux measures on management of gastroesophageal disease are evaluated. Simple anti-reflux measures include elevation of the head of the bed, weight loss, reduced food intake, and the avoidance of precipitating foods and drugs. In this chapter, we summarized the utility of these simple anti-reflux measures for management of gastroesophageal reflux disease.

Diet↗
PubMed1999

Binding of salicylhydroxamic acid and several aromatic donor molecules to Arthromyces ramosus peroxidase, investigated by X-ray crystallography, optical difference spectroscopy, NMR relaxation, molecular dynamics, and kinetics.

The X-ray crystal structure of the complex of salicylhydroxamic acid (SHA) with Arthromyces ramosus peroxidase (ARP) has been determined at 1.9 A resolution. The position of SHA in the active site of ARP is similar to that of the complex of benzhydroxamic acid (BHA) with ARP [Itakura, H., et al. (1997) FEBS Lett. 412, 107-110]. The aromatic ring of SHA binds to a hydrophobic region at the opening of the distal pocket, and the hydroxamic acid moiety forms hydrogen bonds with the His56, Arg52, and Pro154 residues but is not asscoiated with the heme iron. X-ray analyses of ARP-resorcinol and ARP-p-cresol complexes failed to identify the aromatic donor molecules, most likely due to the very low affinities of these aromatic donors for ARP. Therefore, we examined the locations of these and other aromatic donors on ARP by the molecular dynamics method and found that the benzene rings are trapped similarly by hydrophobic interactions with the Ala92, Pro156, Leu192, and Phe230 residues at the entrance of the heme pocket, but the dihedral angles between the benzene rings and the heme plane vary from donor to donor. The distances between the heme iron and protons of SHA and resorcinol are similar to those obtained by NMR relaxation. Although SHA and BHA are usually considered potent inhibitors for peroxidase, they were found to reduce compound I and compound II of ARP and horseradish peroxidase C in the same manner as p-cresol and resorcinol. The aforementioned spatial relationships of these aromatic donors to the heme iron in ARP are discussed with respect to the quantum chemical mechanism of electron transfer in peroxidase reactions.

Binding Sites↗
PubMed1999

Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair.

In the nucleotide excision repair system, UvrB plays a central role in damage recognition and DNA incision by interacting with UvrA and UvrC. We have determined the crystal structure of Thermus thermophilus HB8 UvrB at 1.9 A resolution. UvrB comprises four domains, two of which have an alpha/beta structure resembling the core domains of DNA and RNA helicases. Additionally, UvrB has an alpha-helical domain and a domain consisting of antiparallel beta-sheets (beta-domain). The sequence similarity suggests that the beta-domain interacts with UvrA. Based on the distribution of the conserved regions and the structure of the PcrA-DNA complex, a model for the UvrB-DNA complex is proposed.

Bacterial Proteins↗
PubMed1999

Crystallization and preliminary X-ray diffraction studies of a DNA excision repair enzyme, UvrB, from Thermus thermophilus HB8.

A DNA excision repair enzyme, UvrB, from Thermus thermophilus HB8 was crystallized by the vapor-diffusion method using lithium sulfate as the precipitant and beta-octylglucoside as an additive. The crystals belong to the trigonal space group P3121 or P3221, with unit-cell dimensions of a = b = 136.0 and c = 108.1 A. The crystal is most likely to contain one UvrB protein in an asymmetric unit with the Vm value of 3.8 A3 Da-1. The crystals diffracted X-rays beyond 2.9 A resolution. Although the crystals were sensitive to X-ray irradiation at room temperature, the frozen crystals at 100 K showed no apparent decay during the intensity measurement.

Bacterial Proteins↗
PubMed1999

Mitral valve thrombus attached to the intact mitral valve associated with distal embolism.

A 61-year-old man was referred for cardiac investigation because embolism was suspected to be the cause of the sudden onset of severe pain in his right leg after a surgical procedure. The electrocardiogram revealed no atrial fibrillation. Transthoracic echocardiography demonstrated a tumor-like echo at the anterior mitral leaflet, and transesophageal echocardiography documented a mass 13x9mm in size, attached by a stalk to the left atrial side of the anterior mitral leaflet. The other parts of the mitral valve appeared to be intact. At emergency surgery, the mass was located in the center of the left atrial side of the anterior mitral leaflet. It mimicked a myxoma and had a stalk arising from the anterior leaflet. After resection of the mitral valve mass, catheter thrombo-embolectomy was performed and several long pieces of fresh thrombus were removed. On histological examination, the mass consisted of fresh thrombus tissue. No cellular component or myxoma tissue was documented. The distal embolus also consisted of fresh thrombus tissue. This is the first case of a thrombus of the intact mitral valve without atrial fibrillation.

Diagnosis, Differential↗
PubMed1999

Rosai-Dorfman disease presenting multiple intracranial lesions with unique findings on magnetic resonance imaging. Case report.

Rosai-Dorfman disease (RDD) is a rare idiopathic histoproliferative disease affecting the systemic lymph nodes. Although an extranodal lesion has also been recognized, central nervous system involvement is extremely rare. To the authors' knowledge, only 20 cases of intracranial lesions have been reported previously. Intracranial RDD is clinically and radiologically difficult to distinguish from meningioma, and histological examination is essential for a definitive diagnosis. The authors treated a large frontal lobe tumor associated with multiple meningeal nodules in a 67-year-old patient presenting with diplopia and headache. Radiological examination indicated that the mass was an inflammatory lesion rather than a meningioma. Microscopically the lesion consisted of mixed inflammatory infiltrate with marked emperipolesis, which is characteristic of RDD. A review of the literature and a discussion of the differential diagnosis of this rare lesion are also presented.

Aged↗
PubMed1998

Colorimetric determination of citrulline residues in proteins.

A method is described for the direct colorimetric determination of citrulline residues in proteins based on the reaction with diacetylmonoxime in the presence of lower concentrations of sulfuric acid. The reduced sensitivity due to the lower acid concentration was overcome by the addition of ferric chloride which also contributed to the color stabilization. Insoluble proteins or proteins resulting in turbidity can be analyzed following partial hydrolysis of those with enzyme or acid. The molar absorption coefficient (epsilon) for citrulline at 464 nm was 2.8 x 10(4). The method enabled us to determine low levels of protein-bound citrulline which are beyond the limitations of conventional methods using an amino acid analyzer. We determined the citrulline contents in the cornified cells of the epidermis of newborn rats, as well as soybean trypsin inhibitor.

Amino Acids↗
PubMed1998

Domain organization and functional analysis of Thermus thermophilus MutS protein.

MutS protein binds to DNA and specifically recognizes mismatched or small looped out heteroduplex DNA. In order to elucidate its structure-function relationships, the domain structure of Thermus thermophilus MutS protein was studied by performing denaturation experiments and limited proteolysis. The former suggested that T. thermophilus MutS consists of at least three domains with estimated stabilities of 12.3, 22.9 and 30.7 kcal/mol and the latter revealed that it consists of four domains: A1 (N-terminus to residue 130), A2 (131-274), B (275-570) and C (571 to C-terminus). A gel retardation assay indicated that T.thermophilus MutS interacts non-specifically with double-stranded (ds), but not single-stranded DNA. Among the proteolytic fragments, the B domain bound to dsDNA. On the basis of these results we have proposed the domain organization of T. thermophilus MutS and putative roles of these domains.

Adenosine Triphosphatases↗
PubMed1998

Crystallization and preliminary X-ray diffraction studies on the water soluble form of rat heme oxygenase-1 in complex with heme.

The water-soluble portion of rat heme oxygenase-1 which lacks 22 hydrophobic amino-acid residues at the C-terminus was expressed in E. coli and crystallized in the form of a complex with heme by the vapor-diffusion method using polyethylene glycol 4000 as the precipitant. The crystals belong to the tetragonal space group P41212 or P43212, with unit-cell dimensions of a = b = 56.7, c = 186. 7 A. The crystal contains one heme-heme oxygenase-1 complex in an asymmetric unit and diffracts X-rays beyond 3.0 A resolution with a conventional X-ray source.

Animals↗
PubMed1998

Differential activation of two JNK activators, MKK7 and SEK1, by MKN28-derived nonreceptor serine/threonine kinase/mixed lineage kinase 2.

MKN28-derived nonreceptor type of serine/threonine kinase/mixed lineage kinase 2 (MST/MLK2) directly phosphorylates and activates SEK1/MKK4/JNKK1/SKK1 in vitro, thereby acting as a mitogen-activated protein (MAP) kinase kinase kinase in the JNK/SAPK pathway (Hirai, S. -i., Katoh, M., Terada, M., Kyriakis, J. M., Zon, L. I., Rana, A., Avruch, J., and Ohno, S. (1997) J. Biol. Chem. 272, 15167-15173). The in vitro reconstitution system for the kinase cascade allowed us now to identify JNK/SAPK activators involved in the MST/MLK2-dependent activation of JNK/SAPK in vivo. We show that at least two distinct MST/MLK2-dependent JNK/SAPK activators are present in the fractionated COS-1 cell lysate, and that they appear to be SEK1/MKK4/JNKK1/SKK1 and MKK7/JNKK2/SKK4 by Western blot analysis. Notably, a majority of the MST/MLK2-dependent JNK/SAPK-activating activity is found in MKK7-containing fractions, whereas the MEKK1-dependent activity is comparably distributed in SEK1- and MKK7-containing fractions. Moreover, MST/MLK2 activates recombinant MKK7 more effectively than recombinant SEK1, whereas MEKK1 activates both to a similar extent. In addition, the deletion analysis on MST/MLK2 showed that the kinase domain is responsible for the determination of substrate specificity. These results provide a molecular aspect to the differential regulation of the two JNK activators by a variety of cellular stimuli.

Animals↗
PubMed1998

Thrombomodulin expression on dermal cells in normal and psoriatic skin.

The various subsets of dermal cells with a dendritic appearance can be identified by phenotypic differences in cell markers. We report on the morphology and tissue distribution of dermal cells detected with a monoclonal antibody against thrombomodulin in histological sections of normal arm and scalp skin and psoriatic skin. Double staining with antibodies to factor XIIIa, CD34 and CD68 was also employed in scalp biopsies to elucidate the relationship between thrombomodulin+ dermal cells and dermal dendrocytes and macrophages described by others. Thrombomodulin+ dermal cells in normal arm skin had little cytoplasm with fine branched dendrites and tended to be localized just beneath the epidermis. In scalp skin these cells had longer, more numerous dendrites and were distributed in the papillae and perivascular adventitial dermis primarily in the upper and central reticular dermis. In psoriatic skin, thrombomodulin+ dermal cells had an increased cytoplasmic volume with stout, less branched dendrites and appeared in the papillae and among inflammatory cells. Dermal cells detectable by thrombomodulin expression were factor XIIIa-, CD34- and CD68-, and seemed to represent a distinct subset of dermal cells which may function in tissue repair. However, thrombomodulin+ dermal cells and factor XIIIa+ dendrocytes were frequently seen close together and could act cooperatively to regulate extravascular thrombin homeostasis in both normal and pathological dermal environments.

Antigens, CD↗
PubMed1998

Combination therapy of fasudil hydrochloride and ozagrel sodium for cerebral vasospasm following aneurysmal subarachnoid hemorrhage.

Fasudil hydrochloride is a new type of intracellular calcium antagonist, different from the calcium entry blockers that are commonly employed for clinical use. Since September 1995, the combination of fasudil hydrochloride and ozagrel sodium, an inhibitor of thromboxane A2 synthesis, has been used to treat 60 patients at risk of cerebral vasospasm after aneurysmal subarachnoid hemorrhage. The effectiveness of this combination therapy was investigated by comparison with the outcome of 57 patients previously treated with only ozagrel sodium. The combination therapy was significantly more effective (p < 0.01) in reducing the incidence of low density areas on computed tomography scans, and reduced, but not significantly, the occurrence of symptomatic vasospasm. The combination therapy of fasudil hydrochloride and ozagrel sodium has superior effectiveness over only ozagrel sodium in treating patients at risk of vasospasm after aneurysmal subarachnoid hemorrhage.

1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine↗
PubMed1997

Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 A resolution.

The crystal structure of 0.19 alpha-amylase inhibitor (0.19 AI) from wheat kernel was determined by the multiple-isomorphous replacement method coupled with density modification and noncrystallographic symmetry averaging and then refined by simulated annealing using diffraction data to 2.06 A resolution (R = 18.7%, free R = 22.3%). The asymmetric unit has four molecules of 0.19 AI, each comprised of 124 amino acid residues. Electron density for residues 1-4 and 69-77 is absent in all subunits, probably because of the intrinsic flexibility of these segments. Each subunit has four major alpha-helices and one one-turn helix which are arranged in the up-and-down manner, maintaining the favorable packing modes of the alpha-helices. 0.19 AI, however, has two short antiparallel beta-strands. All 10 cysteine residues in 0.19 AI form disulfide bonds (C6-C52, C20-C41, C28-C83, C42-C99, and C54-C115), consistent with the assignments made biochemically for 0.28 AI from wheat kernel and by NMR analysis of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds (RBI). The disulfide bond patterns in these AIs are similar to those in the hydrophobic protein from soybean (HPS), which lack only the bond corresponding to C28-C83 in 0.19 AI. Extensive interactions occurred between particular pairs of 0.19 AI subunits, mainly involving hydrophobic residues. Comparisons of the structures of 0.19 AI, RBI, and HPS showed that the arrangements of the major alpha-helices are similar but the conformations of the remaining residues differ markedly. The present X-ray analysis for 0.19 AI and the NMR analysis for RBI suggest that all the AIs in this family have a common fold. The alpha-amylase binding site is discussed on the basis of the tertiary and quaternary structures of 0.19 AI together with biochemical and spectroscopic data for AIs.

Amino Acid Sequence↗
PubMed1997

Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X-ray crystallographic analysis of the complex at 1.6 A resolution.

The crystal structure of Arthromyces ramosus peroxidase (ARP) in complex with benzhydroxamic acid (BHA) as determined by X-ray analysis at 1.6 A shows unambiguously how BHA binds to ARP. BHA is located in the distal heme pocket. Its functional groups are held by three hydrogen bonds to His56N(epsilon), Arg52N(epsilon), and Pro(154)O, but are too far away to interact with the heme iron. The aromatic ring of BHA is positioned at the entrance of the channel to the heme pocket, approximately parallel to the heme group. Most water molecules at the active site of the native enzyme are replaced by BHA, leaving a ligand, probably a water molecule, at the sixth position of the heme. Results are compared with spectroscopic data.

Binding Sites↗
PubMed1997

Binding of iodide to Arthromyces ramosus peroxidase investigated with X-ray crystallographic analysis, 1H and 127I NMR spectroscopy, and steady-state kinetics.

The site and characteristics of iodide binding to Arthromyces ramosus peroxidase were examined by x-ray crystallographic analysis, 1H and 127I NMR, and kinetic studies. X-ray analysis of an A. ramosus peroxidase crystal soaked in a KI solution at pH 5.5 showed that a single iodide ion is located at the entrance of the access channel to the distal side of the heme and lies between the two peptide segments, Phe90-Pro91-Ala92 and Ser151-Leu152-Ile153, 12.8 A from the heme iron. The distances between the iodide ion and heme peripheral methyl groups were all more than 10 A. The findings agree with the results obtained with 1H NMR in which the chemical shift and intensity of the methyl groups in the hyperfine shift region of A. ramosus peroxidase were hardly affected by the addition of iodide, unlike the case of horseradish peroxidase. Moreover, 127I NMR and steady-state kinetics showed that the binding of iodide depends on protonation of an amino acid residue with a pKa of about 5.3, which presumably is the distal histidine (His56), 7.8 A away from the iodide ion. The mechanism of electron transfer from the iodide ion to the heme iron is discussed on the basis of these findings.

Crystallography, X-Ray↗