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Biomedical subjects

K Itagaki

Publications and source records attributed to K Itagaki.

At least 37 records · Page 2Linked to original sources
PubMed1989

[Clinical evaluation of radioimmunoscintigraphy using a I-131 anti CEA and CA 19-9 monoclonal antibodies cocktail (IMACIS-1)].

The clinical usefulness of a I-131 anti CEA F(ab')2 MoAB and CA 19-9 F(ab')2 MoAB cocktail(IMACIS-1) for the localization of a cancer has been studied in 35 patients (Lung Ca. 10, Pancreas Ca. 7, Gastric Ca. 6, Colon Ca. 5, Hepatoma 2, Cholangio Ca. 2, Esophageal Ca. 1, Uterus Ca. 1, and, Retroperitoneal tumor 1). Of these 28 patients (80%) had an abnormal accumulation of radioactivity in the tumor sites (Lung Ca. 5, Pancreas Ca. 7, Gastric Ca. 6, Colon Ca. 5, Hepatoma 2, Esophageal Ca. 1, Uterus Ca. 1, and, Retroperitoneal tumor 1). Eighteen cases (56.3%) in 32 cases in which the primary site was known showed an abnormal radioactive accumulation and, similarly, 20 metastatic sites (71.4%) in 16 cases with 28 metastatic sites also showed an abnormal accumulation of radioimmunoscintigraphy showed no correlation with the serum CEA or CA 19-9 concentration. Further, no side effect was observed.

Antibodies, Monoclonal↗
PubMed1987

Identification of a novel 1,4-dihydropyridine- and phenylalkylamine-binding polypeptide in calcium channel preparations.

A 1,4-dihydropyridine- and phenylalkylamine-binding polypeptide has been identified by photoaffinity labeling of purified rabbit and guinea pig skeletal muscle calcium channel preparations. The arylazide ligands (-)-[3H]azidopine and (-)-5-[(3-azidophenethyl)[N-methyl-3H]methylamino]-2-(3,4,5- trimethoxyphenyl)-2-isopropylvaleronitrile [( N-methyl-3H]LU 49888) were used to label 1,4-dihydropyridine- and phenylalkylamine-binding sites, respectively. A single, 155 to 170-kDa polypeptide was specifically labeled by both ligands in rabbit and guinea pig preparations provided that the skeletal muscle membranes used for purification were derived from fresh and not previously frozen and thawed tissue. The photoaffinity labeled polypeptide (termed here alpha 1) is different from the previously described alpha subunit in that it has the identical electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gels irrespective of pretreatment either with N-ethylmaleimide or with dithiothreitol. The use of transverse tubular membranes isolated from previously frozen and thawed skeletal muscle results in a purified calcium channel preparation devoid of the alpha 1 subunit. In these preparations proteolytic degradation products of alpha 1 are labeled with both (-)-[3H]azidopine and [N-methyl-3H]LU 49888. Another large molecular weight polypeptide (termed here alpha 2) was also present in every purified calcium channel preparation studied. alpha 2 is distinct from alpha 1 in that reduction with dithiothreitol changes its apparent mass from 160-190 to 130-150 kDa. The alpha 2 subunit is not photoaffinity labeled either with (-)-[3H]azidopine or [N-methyl-3H]LU 49888. These data suggest that two distinct high molecular weight polypeptides (termed alpha 1 and alpha 2) are putative subunits of skeletal muscle calcium channels. Only the alpha 1 subunit contains both 1,4-dihydropyridine and phenylalkylamine receptors. alpha 2 is the same as the previously described alpha subunit (Curtis, B. M., and Catterall, W. A. (1984) Biochemistry 23, 2113-2118), but is neither a 1,4-dihydropyridine- nor a phenylalkylamine-binding protein.

Animals↗
PubMed1984

Identification of sulfur-containing metabolites of m-dichlorobenzene and their disposition and relationship with glutathione in rats.

The sulfur-containing metabolites of m-dichlorobenzene (m-DCB) were identified by using gas chromatography-mass spectrometry and disposition of these metabolites was studied. In the blood, urine and feces of rats dosed with m-DCB, 2,4- and 3,5-dichlorophenyl methyl sulfoxides and 3,5- and 2,4-dichlorophenyl methyl sulfones emerged, while their possible precursors, 3,5- and 2,4-dichlorophenyl methyl sulfides (Me' and Mf', respectively), were not detected in the blood, urine and feces. However, after heating the alkalinized urine and feces, the methyl sulfides appeared. Each cumulative amount of the methyl sulfoxides and methyl sulfones excreted in both the urine and feces for 120 h was less than 0.3% of the dose, while the amounts of Me' and Mf' excreted were about 0.9 and 0.2%, respectively. The amounts of 2,4- and 3,5-dichlorophenyl mercapturic acids excreted in the urine were 2.3 and 1.2%, respectively. However, the former was increased to 27.3% and the latter to 4.3% after heating the acidified urine. The cystein conjugates were not detected. The administration of m-DCB decreased the glutathione level in liver of fasted rats but it was not further reduced by diethyl maleate (DEM)-pretreatment. The kidney glutathione level was not altered by the administration of m-DCB. The blood level of methyl sulfoxides and methyl sulfones and their excretion in urine were markedly decreased in DEM-pretreated rats, while the mercapturic acids in acid-treated urine of DEM-pretreated rats were not significantly decreased. These results suggest that the methyl sulfoxides and methyl sulfones were derived from glutathione in liver and the formation process of mercapturic acids was somewhat what different from that of methyl sulfoxides and methyl sulfones.

Acetylcysteine↗