[Cerebrospinal fluid neuron-specific enolase as a useful indicator for the early diagnosis of Creutzfeldt-Jakob disease].
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Aged↗
Biomedical subjects
T Jimi
Publications and source records attributed to T Jimi.
Ultrastructural localization of adhalin in normal murine skeletal myofiber.
The ultrastructural localization of adhalin and its relations to dystrophin, beta-dystroglycan, and beta-spectrin were studied in normal murine skeletal myofibers. The C-terminal peptides of adhalin and beta-dystroglycan were synthesized based on their cDNAs, and the affinity-purified antibodies against these peptides were produced. Single-immunolabeling electron microscopy showed that the adhalin was located just inside the muscle plasma membrane or inside the myofiber a short distance from the plasma membrane. The adhalin signal was also noted at the sarcoplasmic side of plasmalemmal invaginations or at vesicular structures in subsarcolemmal areas. Double-immunogold-labeling electron microscopy disclosed a similar localization of dystrophin, beta-dystroglycan, and beta-spectrin. The close association of adhalin with dystrophin or beta-dystroglycan was demonstrated by formation of doublets by signals of antibodies of adhalin with those of dystrophin or beta-dystroglycan and was confirmed by statistical analyses. This study demonstrated that the location of adhalin is close to that of dystrophin and beta-dystroglycan at the muscle plasma membrane.
Animals↗
Electron microscopic observations of triple immunogold labelling for dystrophin, beta-dystroglycan and adhalin in human skeletal myofibers.
Dystrophin is the Duchenne muscular dystrophy gene product and is a membrane cytoskeletal protein present in the network of the plasma membrane undercoat. Adhalin (50 kDa dystrophin-associated glycoprotein) and beta-dystroglycan (43 kDa dystrophin-associated glycoprotein) are the transmembrane components of the normal muscle plasma membrane, and beta-dystroglycan has been demonstrated to bind dystrophin at the inside surface of normal muscle plasma membrane. This investigation was undertaken to test whether the epitopes of dystrophin, beta-dystroglycan and adhalin are closely associated with each other by using triple immunogold labelling electron microscopy on normal human skeletal myofibers. Although closely associated signals of triplet immunogold particles were observed, there were less numerous than expected. However, closely associated signals of two epitopes of dystrophin and beta-dystroglycan, dystrophin and adhalin, or adhalin and beta-dystroglycan were frequently observed. These ultrastructural findings are consistent with biochemical evidence implying that dystrophin, beta-dystroglycan and adhalin are closely associated with each other at the normal muscle plasma membrane.
Cytoskeletal Proteins↗
Altered distribution of beta-dystroglycan in sarcolemma of human dystrophic muscles: an immunohistochemical study.
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Animals↗
Influence of boiling water treatment on surface roughness and surface microstructure of set gypsum (dental stone).
The influence of boiling water treatment on the surface roughness and surface microstructure of set gypsums was investigated. Typical surfaces before and after immersion in boiling water were compared by means of SEM observation, the Knoop hardness test, and a surface roughness test. The surfaces of set gypsums were rougher than that of an acrylic resin plate, and after immersion in boiling water, highly roughened surfaces and thinner crystal bodies were observed on each specimen under SEM. The knoop hardness of set gypsums was considerably lowered after boiling water immersion. That of die stones was the same or lower than set dental stones. The results showed that even brief immersion in boiling water had profound effects on the dental stone cast, resulting in rougher surfaces and lower hardness of set gypsums.
Calcium Sulfate↗
Ultrastructural localization of the C-terminus of the 43-kd dystrophin-associated glycoprotein and its relation to dystrophin in normal murine skeletal myofiber.
We used single and double immunogold labeling electron microscopy to investigate ultrastructural localization of the C terminus of the 43-kd dystrophin-associated glycoprotein (43-DAG) and its relationship to dystrophin in normal murine skeletal myofibers. Single immunolabeling localized the antibody against the C terminus of 43-DAG to the inside surface of the muscle plasma membrane and the sarcoplasmic side of plasma membrane invaginations. Double immunolabeling co-localized antibodies against dystrophin and the C terminus of 43-DAG to the same site noted in the single immunolabeling localization of 43-DAG. In particular, dystrophin and the C-terminal 43-DAG antibody signals were often observed as doublets separated by less than 30 nm. We compared these results with those obtained from double immunogold labeling with anti-dystrophin and anti-beta-spectrin, as well as anti-C-terminal 43-DAG and anti-beta-spectrin antibodies. The antibodies against dystrophin and beta-spectrin, or beta-spectrin and 43-DAG, also co-localized to similar sites in skeletal muscle fibers. Signals of doublet formations were noted but their frequency was significantly lower than the doublet frequency of antidystrophin and anti-43-DAG antibodies. The results support the presence of dystrophin and 43-DAG linkage at the inside surface of the murine skeletal muscle plasma membrane.
Amino Acid Sequence↗
Freeze-fracture analysis of muscle plasma membrane in Becker's muscular dystrophy.
The intramembranous particle (IMP), orthogonal array (OA) and orthogonal array subunit particle (OASP) densities in skeletal muscle plasma membranes from eight patients with Becker's muscular dystrophy (BMD) were analysed by the freeze-fracture technique. The results showed almost normal IMP density with the significant decrease of OA and OASP densities in BMD. The group mean densities +/- SE of IMPs on the protoplasmic faces with and without OASPs, and on extracellular faces/microns 2 were 2137 +/- 207, 1839 +/- 68 and 895 +/- 108, respectively in controls; whereas those of BMD were 1989 +/- 259, 1837 +/- 203 and 900 +/- 239, respectively (P > 0.1 by two-tailed t-test). The group median density of OAs and their pits/microns 2 was 4.89 with mid-ranges (25-75% values of the counts) of 2.66-10.18 in controls; whereas that in BMD was 2.15 with mid-ranges of 1.14-4.31 (P < 0.01 by Wilcoxon rank-sum test). The group mean density +/- SE of OASPs in controls was 15.99 +/- 1.83; whereas that in BMD was 13.47 +/- 1.07 (P < 0.01 by two-tailed t-test). However, the diminution of OA and OASP densities in BMD muscle plasma membranes was not as severe as in Duchenne's muscular dystrophy. There was a relationship between OA density and clinical severity in BMD patients; the decrease of OA density in a severe BMD patient was more marked than that in mildly affected BMD patients. Therefore, it seems that marked depletion of OA density may lead to the severe disability in muscular dystrophies.
Adolescent↗
Immunoelectron microscopic localization of C-terminus of 43-kDa dystrophin-associated glycoprotein in normal human skeletal myofibers.
Ultrastructural localization of the C-terminus of a 43-kDa dystrophin-associated glycoprotein (43-DAG) and its relation to dystrophin were investigated in normal human skeletal myofibers by using single and double immunogold labelling methods. The C-terminal end of 43-DAG antibody was localized ultrastructurally at the inside surface of muscle plasma membrane and the sarcoplasmic side of the plasma membrane invaginations. Double immunolabelling electron microscopy disclosed that signals of the C-terminal end of 43-DAG and dystrophin were often associated with each other and formed a doublet at the inside surface of plasma membranes in normal human skeletal myofibers.
Cytoskeletal Proteins↗
Size and localization of dystrophin molecule: immunoelectron microscopic and freeze etching studies of muscle plasma membranes of murine skeletal myofibers.
The ultrastructure and mode of existence of the dystrophin molecule and its relations to actin filaments were examined in murine skeletal myofibers. Electron microscopy of freeze-etched replicas of gold-labelled dystrophin molecules in quick-freeze, deep-etch, rotary-shadow preparations revealed rod-like structures 108.2 +/- 16.3 nm long and 3.1 +/- 1.5 nm thick. Some dystrophin molecules appeared to link their ends to form anastomosing networks; others were separate from each other. The dystrophin molecules were parallel or nearly parallel to the inner surface of the muscle plasma membrane. Double immuno-labelling transmission electron microscopy using N- and C-terminal dystrophin antibodies showed that the group mean distances of the N- and C-terminal signals from the muscle plasma membrane were 52.7 +/- 8.1 nm and 45.9 +/- 11.3 nm, respectively, which were not significantly different. Histograms of the distribution of the N- and C-terminal distances from the muscle plasma membrane had similar patterns with peaks 10-20 nm from the membrane. This was consistent with the findings of the mode of existence of dystrophin molecules seen in freeze-etched replicas. Finally, the dystrophin molecules were linked with the most peripheral sarcoplasmic actin like filaments, end to side as well as end to end.
Amino Acid Sequence↗
[A case of cough hemiplegia].
We reported a patient with internal carotid artery occlusion (ICAO) who developed cough-induced transient hemiplegia. A 63-year-old man with chronic obstructive pulmonary disease experienced several episodes of cough-induced left hemiplegia during drinking and smoking. Selective cerebral angiography demonstrated right ICAO at the vessel origin, with 50% stenosis of the left internal carotid artery. Collateral circulation from the right external to internal carotid artery branches and through the anterior communicating artery was poorly observed on the angiograms. Right middle cerebral artery branches were well visualized on vertebral angiograms at the late phase through the posterior and anterior pericallosal arteries. Due to this collateral blood supply, the right middle cerebral artery territory formed the most distal part of the cerebral circulation and was vulnerable to a reduction of cerebral blood flow. We considered that systemic hemodynamic disturbances by identical mechanisms to those observed in cough syncope may have brought about transient ischemia in the right middle cerebral artery territory which was manifested in the patient's unusual clinical presentation of ICAO "cough hemiplegia".
Carotid Artery, Internal↗
Mexiletine for treatment of spasticity due to neurological disorders.
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Adult↗
Demonstration of cathepsins B, H and L in xenografts of normal and Duchenne-muscular-dystrophy muscles transplanted into nude mice.
The activities and contents of the lysosomal cysteine proteinases cathepsins B, H and L were examined in xenografts of biopsied muscles transplanted from age-matched normal subjects and Duchenne-muscular-dystrophy (DMD) patients into nude mice. The activity of cathepsin B increased 9-fold and that of B-plus-L increased 24-fold in the first week after transplantation in normal muscle xenografts. By the third week, the activity of cathepsin B increased a total of 20-fold and B-plus-L increased to 36-fold the original level. The activity levels of cathepsin B, B-plus-L, H and D, and acid phosphatase in normal and DMD xenografts were not significantly different when compared 2 weeks after transplantation. However, the protein content of cathepsin B in DMD muscle xenografts was more than 3-fold that of normal xenografts at 2 weeks. The profile of cathepsin H activity in normal muscle xenografts was different than those of cathepsins B and B-plus-L. In the first week, the cathepsin H diminished sharply to about one-third of the biopsied muscle level and then, by 3 weeks after transplantation, it had increased slightly to about half the original level. The amount of endogenous cysteine-proteinase inhibitor changed in parallel with the activity of cathepsins B and B-plus-L. Cathepsins B and H, but not cathepsin L, were found immunohistochemically in regenerating muscle fibres of normal and DMD xenografts 2 weeks after transplantation. Staining of cathepsin B in DMD xenografts was slightly stronger than that in normal subjects. There was no immunostaining in degenerating or necrotic muscle fibres 2 weeks after transplantation. Western-blot analysis revealed that the cathepsin B band at 29 kDa was increased in normal xenografts 2 and 3 weeks after transplantation. Also, 2 weeks after transplantation the staining intensity of this band was slightly stronger in DMD xenografts than in normal xenografts. These results suggest that cathepsin B participates in the regeneration of transplanted muscle, both normal and DMD, and in the DMD muscle fibre-wasting processes, during regeneration.
Acid Phosphatase↗
High levels of nervous system-specific proteins in cerebrospinal fluid in patients with early stage Creutzfeldt-Jakob disease.
Concentrations of several proteins that are characteristic of the nervous system were time-sequentially analyzed by radio- and enzyme-immunoassay in the cerebrospinal fluid (CSF) of patients with Creutzfeldt-Jakob disease (CJD). We found abnormally high levels of several proteins, such as neuron-specific enolase (NSE), S-100b protein, brain-type isozyme of creatine kinase (CK-BB) and alpha subunit of GTP binding protein G0 (G0 alpha) in the early stage of the disease. Generally, these protein levels were far higher in CJD patients than in normal controls and other neurological patients in the early stage before the typical clinical manifestations were evident. These levels increased to maxima when the disease activity was most prominent and returned to normal or mildly elevated levels in the terminal stage. The results imply that these protein levels can serve as biochemical markers for the presence of an active destructive process in CJD brain and provide us with a useful indicator for early diagnosis of CJD.
Brain↗
Strong immunoreactivity of cathepsin L at the site of rimmed vacuoles in diseased muscles.
Skeletal muscle samples from four patients with myopathies showing autophagic vacuole formation were examined by immunohistochemical, biochemical and immunoblot analyses. Immunochemical studies demonstrated strongly positive reactions of cathepsins B and L in and around the rimmed vacuoles and weak reactions in intramyofibral portions of degenerating muscle fibres. Faint staining of cathepsin H was also seen at the sites of rimmed vacuoles. Biochemical analyses showed increased activity of cathepsin B and L in muscle specimens from the patients with rimmed vacuole formation. However, there was no remarkable cathepsin H activity in the muscle specimens from these patients. Cathepsin L immunoblot analysis of muscle extracts showed three bands with molecular masses of 30 kDa, 36 kDa and 39 kDa. The immunostaining of cathepsin L from patients with rimmed vacuole formation was stronger than that of normal controls. Cathepsin B immunoblot analysis showed only faint bands in samples from patients with rimmed vacuole formation and normal controls. This study demonstrated, for the first time, strong immunoreactivity of cathepsin L at the sites of rimmed vacuoles. Possible mechanisms of rimmed vacuole formation are discussed.
Adult↗
[Bezafibrate myopathy in two patients with chronic renal failure].
Case 1, a 60-year-old man and case 2, a 70-year-old man had several year history of chronic renal failure with hypertension and hyperlipidemia due to diabetes mellitus. Treatment of hyperlipidemia was started by oral bezafibrate intake 1,200 mg per day in case 1 and 400 mg per day in case 2 respectively. Three to fourteen days later, both patients noticed symmetrical muscle pain and weakness. Then the symptoms worsened and they were hospitalized. At the time of admission, both patients revealed weakness in the proximal muscles of their upper and lower limbs and the serum creatine kinase and myoglobin levels were remarkably elevated. Myoglobinuria was also noted. Routine light microscopic examination of biopsied quadriceps femoris muscles of two patients showed scattered necrotic muscle fibers, some of which were under phagocytosis. The symptoms of the patients were immediately resolved after the drug was discontinued. Serum concentration of bezafibrate was remarkably elevated during treatment. Thus the diagnosis was established as having bezafibrate induced myopathy and, as far as we know, this is the first report of bezafibrate induced myopathy in Japan. On the basis of the above description, bezafibrate may induce muscle damage if dose is excess over the renal capacity. Extreme caution is warranted when the patient is placed on bezafibrate and has renal dysfunction. Strict dose adjustment is necessary in taking account of renal function to avoid muscle damage including rhabdomyolysis.
Aged↗
[Detection of dystrophin with anti-peptide antibodies].
The analysis of dystrophin in skeletal muscles was performed to identify Duchenne and Becker muscular dystrophy (DMD and BMD) by means of immunohistochemical stain and Western blotting with antisera against synthetic dystrophin peptides. The control muscle specimens derived from normal healthy persons, and patients without DMD and BMD revealed clearly continuous stains of dystrophin at surface membrane. A band with 400 kDa of molecular size by Western blotting was positively stained by anti-dystrophin antibodies. The muscle specimens from eleven DMD patients showed no observation both in the band on Western blotting and in the immunohistochemical staining of dystrophin on frozen-thin sections. BMD muscle specimens showed patchy and faint stains, but no detection of any band on Western blotting except a 380 kDa minor band with anti-peptide IX antibody in one patient muscle. The immunohistochemical procedure was found to be more sensitive than Western blotting for the detection of dystrophin. These results indicate that the dystrophin analysis by both methods is an useful tool for the differential diagnosis of patients with DMD and BMD.
Animals↗
Effect of denervation on regenerating muscle plasma membrane integrity: freeze-fracture and dystrophin immunostaining analyses.
We investigated time sequentially, the densities of intramembranous assembly "orthogonal arrays" of regenerating rat extensor digitorum longus muscle after bupivacaine-induced muscle injury. There was no evidence of orthogonal arrays at the early stage, but the densities of orthogonal arrays increased with the maturation of the innervated regenerating myofibers. In contrast, the orthogonal arrays were scarcely observed at any time point examined in denervated regenerating muscles. Therefore, the neural factor may have an important effect on the appearance of orthogonal arrays. Moreover, we studied the immunostainability of Duchenne muscular dystrophy gene product "dystrophin" in the regenerating muscle at the same time points. Positive immunostaining was observed in both innervated and denervated regenerating myofibers even from the early stage of regeneration. On the basis of these data, the relationship between orthogonal array and dystrophin are discussed.
Animals↗
Immunoreactivity of antibodies raised against synthetic peptide fragments predicted from mid portions of dystrophin cDNA.
We synthesized 3 peptide fragments predicted by residues 2354-2368 (peptide I), 2310-2324 (peptide II) and 2255-2269 (peptide III) on the mid-portion of the human dystrophin cDNA map where the most frequent intragenic deletions occurred in Duchenne muscular dystrophy. Rabbit antibodies against these peptides were raised and cryosections of 47 biopsied muscles were studied immunohistochemically. The 47 biopsied muscles included the quadriceps femoris muscles of 8 Duchenne muscular dystrophy patients, 8 child and 5 adult normal controls, 1 facioscapulohumeral dystrophy, 2 limb girdle dystrophy, 3 myotonic dystrophy, 3 polymyositis, 1 mitochondrial myopathy, 1 nemaline myopathy, 3 amyotrophic lateral sclerosis and the extensor digitorum longus muscles of 6 mdx mice (C57BL/10ScSn-mdx) and 6 normal control mice (C57BL/10ScSn). The peptide I antiserum continuously stained the myofiber surface membranes in 8 child and 5 adult normal control muscles, and in 14 other muscles from various neuromuscular diseases, but failed to stain the surface membranes in normal control mice. The surface membranes of 8 Duchenne muscles were not stained by the peptide I antiserum except for a few myofibers. Although the ELISA titers of peptide I, II and III antibodies were high, immunostaining by peptide II antiserum showed no reaction in the myofibers of any of the biopsied muscles, and immunostaining by peptide III antiserum revealed faint reactions on the myofiber surface membranes of all biopsied muscles, including the mdx control mouse muscles except for the Duchenne and mdx myofibers.
Adult↗