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Masanari Hamazu

Publications and source records attributed to Masanari Hamazu.

4 recordsLinked to original sources

[Examination of attenuation correction using low-dose computed tomography].

Attenuation correction is necessary for the reconstruction of SPECT images. One report has mentioned that attenuation correction by X-ray computed tomography (CT) is effective for a non-uniform attenuation body. We examined the effect of attenuation correction on SPECT images by changing the scanning conditions of CT, and evaluated the possibility of attenuation correction by low-dose CT. The phantom was scanned under several X-ray tube conditions varying from 80 kV to 135 kV and from 7.5 mAs to 200 mAs. We obtained equations of attenuation correction based on the Hounsfield Unit (HU) units of each pixel and compared the effects of attenuation correction. The results showed that the equation for attenuation correction under each condition did not vary significantly, and the effects of attenuation correction by the equations did not vary significantly between CT of low dose and that of clinical dose. This result suggest that the attenuation correction obtained by low-dose CT was equal to that obtained by the clinical dose. In conclusion, it seemed that the equation and map of attenuation correction matched with each radionuclide yielded more adequate attenuation correction than conventional methods.

Image Processing, Computer-Assisted↗

Antibody to immunoglobulin G and polyethylene glycol augment cyclic adenosine monophosphate production by TSH receptor antibody bound to porcine thyroid cells.

Anti-immunoglobulin G (IgG) augments cyclic adenosine monophosphate (cAMP) production by thyroid-blocking antibody (TBAb) bound to porcine thyroid cells (PTC). This is described as a conversion phenomenon. We reported the effect of polyethylene glycol (PEG) to augment thyroid-stimulating antibody (TSAb) activity in a PTC assay. In the present experiment we examined the effect of anti-immunoglobulin G (IgG) and PEG on cAMP production from TBAb or TSAb bound to PTC. TBAb bound to PTC was separated from unbound TBAb by centrifugation after a first incubation (0.5 hour at 37 degrees C) of TBAb-IgG with PTC. TBAb bound to PTC were incubated with anti-human (h)IgG or hIgG fragments [F(ab')(2), Fc, Fd, H chain or L-chain] for 4 hours at 37 degrees C in the second incubation. Anti-IgG or anti-IgG fragments increased cAMP production. No conversion was caused by protein A, protein L, or PEG (5%). PEG did not augment cAMP production by these IgG antibodies. PEG augmented cAMP production during incubation of TSAb-IgG bound to PTC, but anti-IgG did not. PEG significantly augmented cAMP production by coincubation of TSAb-IgG bound to PTC and the unbound TSAb-IgG (obtained from the first incubation). A similar augmentative effect of PEG was also observed in experiments using TSAb-F(ab')(2) and TSAb-Fab. cAMP production by PTC bound by both TBAb- and TSAb-IgG was increased by co-incubation with anti-IgG, but was not increased by PEG. In conclusion, anti-IgG specifically increased cAMP production from TBAb bound to PTC (conversion phenomenon) and PEG specifically increased cAMP production by TSAb bound to PTC. Different mechanisms enhance cAMP production by TSAb and conversion of TBAb.

Animals↗

[Introduction of manual for the management radioactive medical waste].

Societies concerned with radioactive rays and nuclear medicine have recently highlighted the necessity of managing radioactive medical waste resulting from nuclear medicine examinations. We introduce a manual that we have created and explain its use in decision-making and management practices aimed at the reduction of radioactive medical waste at hospitals that have not yet solved this problem. We hope that our manual will help in reducing this medical waste.

Japan↗

Demonstration of anti-TSH antibody in TSH binding inhibitory immunoglobulin-positive sera of patients with Graves' disease.

OBJECTIVES: The presence of anti-TSH antibodies in Graves' patients with unusually low TSH binding inhibitory immunoglobulin (TBII) has been reported. Recently, we found the first case of an anti-TSH antibody in TBII-positive sera of patients with Graves' disease. The prevalence and immunological specificity of this anti-TSH antibody were examined. DESIGN: The presence of 125I-bovine(b) TSH binding antibody in TBII positive serum was examined by prolonged incubation of more than 1 day because only weak binding occurred after 1 h incubation at 37 degrees C. The clinical course of these patients and binding characteristics of anti-bTSH antibody were examined. RESULTS: The corrected method-TBII activity (%)[1 - (a - b)/(c - d)] x 100 and the standard method-TBII activity (%) [1 - (a - d)/(c - d)] x 100 [a, 125I-bTSH binding with TSH receptor (R) in the presence of test serum; b, 125I-bTSH binding with test serum; c, 125I-bTSH binding with TSH R in the presence of normal serum; d, 125I-bTSH binding with normal serum] were calculated. The corrected method-TBII activity was always higher than the standard method-TBII activity in anti-bTSH antibody-positive serum. Anti-bTSH antibody-positive cases in TBII-positive Graves' disease were found in approximately 1% of Graves' patients. Anti-bTSH antibodies were confirmed as IgG from the increase of precipitated radioactivity by adding rabbit antihuman IgG antibody after the incubation of 125I-bTSH with test serum. These antibodies bind with not only bTSH, bTSH(alpha) and bLH, but also porcine (p)TSH, pTSH(alpha) and pFSH. However, these antibodies did not bind with human TSH. Binding of 125I-bTSH with patient's serum was neither inhibited by other Graves' thyroid stimulating antibody (TSAb), nor thyroid blocking antibody (TBAb) in primary hypothyroidism. CONCLUSIONS: The presence of anti-bTSH antibody in TBII-positive serum of high titre means that TBII-positive sera cannot rule out the absence of anti-bTSH. Thus, determination of 125I-bTSH binding with test serum in TSH receptor assays is necessary to determine the precise TBII activity and to detect anti-bTSH antibody.

Adult↗