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Biomedical subjects

Akira Harada

Publications and source records attributed to Akira Harada.

22 records · Page 2Linked to original sources

Changes in serum macrophage-related factors in patients with chronic inflammatory demyelinating polyneuropathy caused by intravenous immunoglobulin therapy.

Chronic inflammatory demyelinating polyneuropathy (CIDP) is a slowly progressive or recurrent neuropathy accompanied by infiltration of macrophages in the peripheral nerves. Macrophage colony-stimulating factor (M-CSF) and monocyte chemoattractant protein-1 (MCP-1) are a macrophage-related cytokine and chemokine, respectively. Although, intravenous immunoglobulin (IVIg) infusion therapy has been used for treating CIDP patients, not all CIDP patients have responded to IVIg infusion therapy. To determine the mechanisms of the action of IVIg, we examined serum M-CSF and MCP-1 levels during and after IVIg infusion therapy in 19 CIDP patients treated with IVIg (0.4 g/kg/day for 5 days). Ten of the 19 patients (52.6%) responded to IVIg therapy. Both M-CSF and MCP-1 concentrations in IVIg responders were significantly higher on day 1 postinfusion than those in nonresponders, but decreased to their pretreatment values on day 5 postinfusion. The results suggest that immunomodulation through M-CSF and MCP-1 is involved in the mechanisms underlying the effect of IVIg infusion therapy in CIDP patients.

Adult↗

A death in a stationary vehicle whilst idling: unusual carbon monoxide poisoning by exhaust gases.

In this paper, we describe an autopsy case in which death was due to accidental carbon monoxide poisoning occurring in a stationary vehicle idling in an open space. To investigate the source of the fatal fumes, the death scene situation was reconstructed using the vehicle. Exhaust gases were found to invade the interior through the floor from a defective exhaust system. CO gas was detected while idling and the level in the cabin gradually rose to 1.5% over a 2-h period. Since the 8-year-old motor vehicle seemed to have been defective for some months, it was concluded that stationary idling overnight caused an accumulation of toxic gases in the interior.

Accidents↗

Peroxidation of Pyrogallol by Antibody-Metalloporphyrin Complexes.

Antibody 03-1, which was prepared by immunization with meso-tetrakis(4-carboxyphenyl)porphyrin (TCPP) conjugate, has been found to bind strongly to Mn(III)-TCPP and Fe(III)-TCPP complexes with dissociation constants of 4.1 x 10(-)(7) and 1.5 x 10(-)(7) M, respectively, although other monoclonal antibodies raised against TCPP did not bind to these TCPP-metal complexes. The complexes of antibody 03-1 with Mn(III)-TCPP and Fe(III)-TCPP were found to catalyze oxidation of pyrogallol selectively. A Lineweaver-Burk plot for the oxidation of pyrogallol by the antibody-Fe-TCPP complex showed K(m) = 4.0 mM and k(cat) = 50 min(-)(1). Studies on the effect of the molar ratio of the antibody to metalloporphyrin on the catalytic activity showed that a 1:1 complex was the most effective for the reaction. The effect of salt (NaCl) on the reaction showed that electrostatic interaction between the antibody and the metalloporphyrin was important for the reaction. The antibody-metalloporphyrin complexes are stable enough to show catalytic activity in the presence of an excess amount of H(2)O(2).

Journal Article↗

Supramolecular formation of antibodies with viologen dimers: utilization for amplification of methyl viologen detection signals in surface plasmon resonance sensor.

Monoclonal antibodies for 1-(carboxypentyl)-1'-methyl-4,4'-bipyridinium dichloride have been prepared. The complex formation of one of the antibodies, 10D5, with viologen dimer has been studied by a biosensor technique based on surface plasmon resonance. The dissociation constants of the complex between antibody 10D5 and methyl viologen or viologen dimer are found to be (2.0 +/- 0.2) x 10 (-7) and (1.5 +/- 0.5) x 10 (-7) M, respectively. Enhancement of response signal intensities in SPR is observed by the addition of the antibody solution to the viologen dimer-antibody complex indicating the formation of linear supramolecules between the antibody and viologen dimer. Amplification of methyl viologen sensing processes is realized by the inhibition of the complex formation between antibodies and viologen dimer-antibody complexes by methyl viologen and signal enhancement due to the supramolecular formation of the antibody and viologen dimer. The sensitivity in this system is found to be 2 orders larger than that obtained in the simple addition of methyl viologen to the antibody immobilized to the surface of the sensor chip.

Antibodies, Monoclonal↗