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Featured researches published by Yoshihiro Kajita.


Neurology | 1997

Multiple Brain Gas Embolism After Ingestion of Concentrated Hydrogen Peroxide

Toshiharu Ijichi; Tsuyoshi Itoh; Ryuta Sakai; Keisuke Nakaji; Takumi Miyauchi; Ryoichi Takahashi; Shozo Kadosaka; Masahiro Hirata; Seiichi Yoneda; Yoshihiro Kajita; Yoichi Fujita

We present a 63-year-old man who developed multiple brain infarction after ingesting a 35% hydrogen peroxide solution. Neurologic examination revealed left hemiparesis, primarily affecting the lower limb, and mild weakness of the right lower limb. Gadolinium-enhanced MRI revealed patchy bilateral brain lesions. Oxygen gas embolization is the likely cause of the brain infarctions. NEUROLOGY 1997;48: 277-279


Clinica Chimica Acta | 1978

Demonstration of antibody for glutamic pyruvic transaminase (GPT) in chronic hepatic disorders.

Yoshihiro Kajita; Takaya Majima; Manabu Yoshimura; Takashi Hachiya; Tadayoshi Miyazaki; Hamao Ijichi; Yukio Ochi

The present paper describes the detection of an autoantibody for glutamic pyruvic transaminase (GPT) in sera of patients with chronic hepatic disorders. In 16 out of 500 patients, the existence of an antibody for pig GPT was demonstrated by the double antibody method, gel filtration and radioimmunoelectrophoresis. The antibody was demonstrated as an immunoglobulin G (IgG) with either polyclonal or monoclonal type (kappa or lambda). The binding portion of IgG with GPT was determined as the fragment Fab, but not Fc of IgG. Because the binding of 125I-pig GPT with the patients antibody was displaced by human GPT, this antibody may have the characteristic of cross reacting with both pig and human GPT. Although the mechanism of production of the antibody for GPT and the pathological significance of the antibody in chronic hepatic disorders remained obscure, possible inhibition of GPT activity in serum is suggested in the presence of this antibody.


Clinical Endocrinology | 1997

Demonstration of fragments with thyroid stimulating activity from Thyroid stimulation blocking antibodies-IgG molecules by papain digestion

Tsuyoshi Kouki; Takehiro Inui; Kei Yamashiro; Takashi Hachiya; Yukio Ochi; Yoshihiro Kajita; Nobuyuki Takasu; Yasushi Sato; Atsuo Nagata

Thyroid stimulation blocking antibodies (TSBAb) inhibit TSH action and may have a role in the pathogenesis of hypothyroidism. In order to study the relationship between blocking and stimulating activities we have examined the biologically active fragments in TSBAb‐IgG molecules after papain digestion.


Parasitology Research | 2006

A case of human fasciolosis: discrepancy between egg size and genotype of Fasciola sp

Ken Inoue; Hidetoshi Kanemasa; Kaori Inoue; Masafumi Matsumoto; Yoshihiro Kajita; Shoji Mitsufuji; Keisyo Kataoka; Takeshi Okanoue; Minoru Yamada; Ryuichi Uchikawa; Tatsuya Tegoshi; Naoki Arizono

In human fasciolosis, differential diagnosis of the causative flukes, Fasciola hepatica and Fasciola gigantica, is problematic. We report a rare case of human fasciolosis in which an adult worm was recovered from the bile duct of a Japanese man. Morphometric data of the worm were consistent with those of F. hepatica, whereas the size of eggs in the stool indicated infection with F. gigantica. Nucleotide sequences of ITS-1 and -2 and CO1 genes of the DNA extracted from the eggs revealed that the genotype was that of F. hepatica. These findings suggest that the size of eggs is not a suitable marker for species identification in human fasciolosis, especially in settings such as the East Asian region where different karyotypes and hybrid genotypes of F. hepatica and F. gigantica have been found.


Clinical Endocrinology | 2002

Demonstration of anti‐TSH antibody in TSH binding inhibitory immunoglobulin‐positive sera of patients with Graves’ disease

Yukio Ochi; Masanari Hamazu; Yoshihiro Kajita; Atsuo Nagata

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.


Clinica Chimica Acta | 1985

Immunological study of tissue polypeptide antigen (TPA)—demonstration of keratin-like sites and blood group antigen-like sites on TPA molecules

Yukio Ochi; Yasuaki Ura; Masanari Hamazu; Masao Ishida; Yoshihiro Kajita; Yoshiyuki Nakajima

We examined the immunological cross-reactivity between tissue polypeptide antigen (TPA) and keratin protein because of the reported sequence homology between these two proteins. TPA showed positive immuno-reactivity against both polyclonal and monoclonal antibodies for keratin. The binding of [125I]TPA with anti-keratin could be displaced dose-dependently by unlabeled keratin. However, no cross-reaction between keratin and anti-TPA was found. TPA also showed the positive immuno-reactivity with antibodies for blood group antigens (A, B and Lewis substances), but keratin did not. A standard solution of Lewis substance reacted with neither anti-TPA nor with anti-keratin. These data strongly suggest that TPA has an immunological similarity with both keratin protein and blood group antigens. When [125I]TPA and [125I]keratin were gel-filtered on a Sephadex G-200 column, the radioactivities of TPA and keratin were found mainly in the void volume fraction (MW greater than 200 000) and the MW of approximately 60 000, respectively. Chromatography on Sepharose 6B suggested that the MW of [125I]TPA was 320 000. When sera of cancer patients were gel-filtered on a Sephadex G-200 column, TPA activity was distributed mainly in the void volume fraction in all tested cases. This experiment suggests that TPA may be a glycoprotein (MW is 320 000) with both keratin-like and blood group antigen-like determinants.


Clinical Endocrinology | 1997

Demonstration of thyroid stimulating activity within H chain fragments of TSAb-IgG by protease digestion and reduction.

Tsuyoshi Kouki; Takehiro Inui; Takashi Hachiya; Hidetoshi Okabe; Yukio Ochi; Yoshihiro Kajita

OBJECTIVE Whether or not the distribution of biologically active fragments in TSAb‐IgG molecules parallels antigen‐binding activity in other anti‐thyroidal antibodies was examined.


Journal of Immunological Methods | 1982

Purification of carcinoembryonic antigen by affinity chromatography with anti-α1-acid glycoprotein

Yukio Ochi; Yoshihide Fujiyama; Shiro Hosoda; Masanari Hamazu; Yoshihiro Kajita; Tadayoshi Myazaki; Takashi Hachiya; Masao Ishida

Purification of radiolabeled carcinoembryonic antigen (CEA) preparations by affinity chromatography with anti-AG bound to Sepharose was attempted, since an immunological similarity between AG (alpha 1-acid glycoprotein) and a portion of CEA had been noted. When 125I-CEA was purified in this manner, the fraction which did not bind to the column showed decreased reactivity with either anti-AG or anti-CEA. The retained fraction showed enhanced reactivity with both anti-AG and anti-CEA. The yield of purified CEA increased when the CEA preparation was allowed to react with the anti-AG column overnight. Purification of CEA from tumor tissue was performed by affinity chromatography. A perchloric acid (PCA) extract from cancer tissue was mixed with antiserum against CEA to give an immune complex, and a CEA-reactive fraction obtained by PCA extraction. The CEA-reactive fraction was eluted from a Sephadex G-200 column, and final purification was by anti-AG chromatography. When purified CEA was applied to a Sephadex G-200 column with carrier protein after labeling with 125I, the eluted radioactivity was found only in the 180,000 dalton fraction. Almost all the radioactivity was precipitated from the labeled protein by either anti-AG or anti-CEA. Purification of CEA is possible by affinity chromatography with anti-AG bound to Sepharose.


Endocrine Research | 1999

Mechanism of the Augmentative Effect of High Polyethylene Glycol (PEG) Concentrations on the Thyroid Stimulating Activity in TSAb-IgG Using a Porcine Thyroid Cell Assay

Kei Yamashiro; Tsuyoshi Kouki; Nobuyuki Takasu; Takehiro Inui; Yukio Ochi; Yoshihiro Kajita; Yasushi Sato; Atsuo Nagata

We previously demonstrated that high polyethylene glycol (PEG) concentrations (5% PEG) significantly augmented cAMP production in response to TSAb-IgG using the porcine thyroid cell (PTC) assay. The mechanism of the stimulatory effect of 5% PEG on cAMP production was examined by a two-step incubation with PTC. TSAb-IgG was preincubated with or without addition of 5% PEG in the PTC assay for 2.5 hr (1st incubation) and separated PTC was re-incubated with fresh Hanks buffer for 5 hr (2nd incubation). cAMP production in the 1st incubation medium by co-incubation of TSAb-IgG and 5% PEG for 2.5 hr was significantly increased (3.3-fold) compared to that without 5% PEG. When the cAMP content in PTC and the incubation medium were compared in the same volume of incubation medium after co-incubation of TSAb-IgG and 5% PEG for 2.5 hr, cAMP contents in PTC were about 7-fold higher than that in the incubation medium, and this ratio did not change in the incubation medium of TSAb-IgG without 5% PEG. Similar increases in cAMP contents in PTC (6.6-fold) compared to the incubation medium were also observed with bTSH, although there was no augmentative effect of 5% PEG on cAMP production by bTSH in either the incubation medium or PTC. When PTC, which had been preincubated with normal-IgG and 5% PEG in the 1st incubation, was re-incubated with TSAb-IgG in the 2nd incubation medium, cAMP production by TSAb-IgG was not stimulated by 5% PEG. The augmentative effect of 5% PEG on cAMP production by TSAb-IgG was observed whenever 5% PEG and TSAb-IgG were co-incubated in either the 1st or 2nd incubation. However, no stimulatory effect of 5% PEG on bTSH was observed. These results suggested the stimulatory effect of 5% PEG on TSAb-IgG-stimulated cAMP production may be due to the increase of binding or incorporation of TSAb-IgG into the membranes of PTC compared to TSH.


Clinica Chimica Acta | 1992

Increased serum concentration of type IV collagen peptide and type III collagen peptide in hyperthyroidism

Takehiro Inui; Yukio Ochi; Wen Chen; Yoshiyuki Nakajima; Yoshihiro Kajita

Serum concentration of type IV collagen peptide, the 7S domain of type IV collagen (type IV collagen 7S) and the amino terminal propeptide of type III procollagen (type III procollagen peptide) is thought to be a useful marker of progressive liver disease. In the present study, serum levels of these collagens in patients with thyroidal diseases with normal liver function were assayed. Increased levels in the hyperthyroid state and relatively decreased levels in the hypothyroid state were observed. The increased levels in hyperthyroidism was most prominent in type IV collagen peptide. The increased level became normal in the subsidence of hyperthyroidism by treatment with anti-thyroid drug. A positive correlation between serum type IV collagen peptide levels and serum thyroid hormone levels such as T4, T3, free T4 and free T3 was observed. These facts show that serum type IV collagen peptide may be influenced by not only liver disease but also serum thyroid hormone levels. Type IV collagen peptide may provide a useful biochemical marker of hyperthyroid state.

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Yukio Ochi

Kyoto Prefectural University of Medicine

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Takashi Hachiya

Shiga University of Medical Science

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Tadayoshi Miyazaki

Kyoto Prefectural University of Medicine

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Manabu Yoshimura

Kyoto Prefectural University of Medicine

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Masao Ishida

Kyoto Prefectural University of Medicine

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Hamao Ijichi

Kyoto Prefectural University of Medicine

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Takehiro Inui

Shiga University of Medical Science

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Tsuyoshi Kouki

University of the Ryukyus

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Masanari Hamazu

Shiga University of Medical Science

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Kei Yamashiro

Shiga University of Medical Science

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