Search PubMed⌕ Search

Biomedical subjects

K Tada

Publications and source records attributed to K Tada.

At least 469 records · Page 26Linked to original sources
PubMed1982

D-lactic acidosis in two patients with short bowel syndrome: bacteriological analyses of the fecal flora.

Two cases of D-lactic acidosis associated with short bowel syndrome are described. The administration of kanamycin to the patients showed a decrease in D-lactate in blood and urine in parallel with disappearance of metabolic acidosis. Bacteriological analyses of the fecal flora showed an increase in Lactobacillus buchneri in the first patient and Lactobacillus fermenti IVa in the second; both bacteria were sensitive to kanamycin. Quantification of in vitro production of D-lactate by each species of bacteria isolated from the feces revealed that Lactobacillus produced more D-lactate than other species of bacteria. These observations indicate that Lactobacillus may play an important role in the induction of D-lactic acidosis in patients with short bowel syndrome.

Acidosis↗
PubMed1982

Glycogen storage disease type 1b due to a defect of glucose-6-phosphate translocase.

Patients with glycogen storage disease (GSD) type 1b have shown normal activity of glucose-6-phosphatase (EC 3.1.3.9) as assayed in frozen liver, though their clinical and biochemical findings were similar to those of patients with GSD 1a (McKusick 23220) (Senior and Loridan, 1968). In 1978, we suggested that a basic defect of GSD 1b exists in the glucose-6-phosphate (G6P) transport system (Narisawa et al., 1978; Igarashi et al., 1979). Since then, there have been reports confirming our observation (Beaudet et al., 1980; Lange et al., 1980; Corbeel et al., 1981; Schaub et al., 1981). Recently, it was postulated that the G6Pase system contains a phosphate translocase which mediates the efflux of phosphate, in addition to a G6P translocase and a non-specific phosphohydrolase (Arion et al., 1980). Therefore, it is possible that GSD 1b is caused by a defect of phosphate translocase. In this paper, the basic defect in GSD type 1b was investigated in two patients; one with severe, the other with mild, clinical symptoms.

Antiporters↗
PubMed1982

Apert's syndrome--a report of five cases.

This report presents five cases of Apert's syndrome with features of acrocephaly, characteristic face and complete syndactyly of the hand and foot with bony fusion. Three cases out of five showed preaxial polydactylies of the foot, considered to be one of the characteristic features of Carpenter's syndrome. In the remaining two cases, the first digital ray of the foot was broad and deformed. In addition one case had a postaxial polydactyly of the hand. Three cases showed severe deformity of the shoulder; two had dysplasia and one had synchondrosis of the glenohumeral joint. On the basis of our findings in this, we feel that there is much phenotypic overlap between Apert's and Carpenter's syndrome. A polydactylous presentation of the hand and foot can be found in not a few cases of Apert's syndrome and it is not always an exclusive feature of Carpenter's syndrome.

Acrocephalosyndactylia↗
PubMed1982

Crystallization and properties of human liver ornithine aminotransferase.

Ornithine aminotransferase [EC 2.6.1.13] was purified and crystallized from human liver by a procedure involving heat treatment, chromatographies on DEAE-cellulose, Octyl-Sepharose CL-4B and Sephadex G-200, and crystallization. The purified enzyme appeared to be homogeneous on polyacrylamide gel electrophoresis with and without sodium dodecyl sulfate. The molecular weight of the enzyme was estimated as 44,000 by sodium dodecyl sulfate electrophoresis and as 177,000 by sucrose density gradient centrifugation, indicating that the enzyme is tetrameric. Various properties of the enzyme from human liver are similar to those of the enzyme from rat liver, including its molecular weight, pH optimum, Km values for ornithine, alpha-ketoglutarate and pyridoxal phosphate and specificity for amino acceptor from ornithine. The amino acid compositions of the two enzymes also have certain similarities, but the enzymes differ in electrophoretic mobility and antigenicity: the human enzyme moved more slowly to the anode, and on immunodiffusion analysis, the single precipitin lines formed between anti-human enzyme serum or anti-rat liver enzyme and the enzyme from human liver or lymphoblastoid cells and the rat liver enzyme fused with spur formation.

Amino Acids↗
PubMed1982

Glycine cleavage system in ketotic hyperglycinemia: a reduction of H-protein activity.

Glycine cleavage activity was compared in the livers from three cases of ketotic hyperglycinemia (two cases of propionic acidemia and one case of methylmalonic acidemia) and three controls. In one case of propionic acidemia, glycine cleavage activity (5.2 nmole/mg protein/hr) was normal in the liver obtained at biopsy when the patient was well controlled by the treatment with low protein diet (0.8 g/kg/day) and the level of serum glycine was lowered to normal. In the two other cases of ketotic hyperglycinemia, glycine cleavage activity was significantly reduced in the liver obtained at autopsy when the patients died in the state of metabolic acidosis. Its activity in the liver of one case of propionic acidemia (0.7 nmole/mg protein/hr) was 6-26% of that in controls (2.7-10.8 nmole/mg protein/hr), and 2-7% in the case of methylmalonic acidemia (0.2 nmole/mg protein/hr). Analysing of the individual components of the glycine cleavage system, a marked decrease in the activity of H-protein was revealed in the livers of the both patients; it (0.2 nmole/mg protein/hr) was only 3-4% of that in controls (4.9-6.3 nmole/mg Protein/hr). These findings suggest that the reduction of the glycine cleavage system in the liver of ketotic hyperglycinemia occurs secondarily as speculated previously and is caused mainly by a decrease of H-protein activity.

Acidosis↗
PubMed1982

Lymphoblasts and diagnosis of pyruvate carboxylase deficiency.

Pyruvate carboxylase activity was measured in phytohemagglutinin-transformed lymphocytes (i.e. lymphoblasts). Mean value +/- S.D. for 10 controls was 259 +/- 38 pmoles/min per mg protein. It was about 7 times higher than that of peripheral leukocytes and a half of cultured skin fibroblasts with similar techniques. Deficient pyruvate carboxylase activity less than 6 pmoles/min per mg protein was demonstrated in the lymphoblasts from a patient with biotin-dependent multiple carboxylase deficiency. It is suggested that lymphoblasts may allow more reliable and ready diagnosis of patients with pyruvate carboxylase deficiency.

Adult↗
PubMed1982

Delivery of fungal beta-galactosidase to rat brain by means of liposomes.

A significant increase in beta-galactosidase activity was observed in the brain of rats 1 hr after an intravenous injection of liposomes containing beta-galactosidase purified from Aspergillus oryzae. The increased activity was proved to have features of the fungal enzyme by differentiating it from rat's native beta-galactosidase in both heat stability and immunochemical studies. Blood content of rat brain tissue under the experimental conditions employed was estimated as 0.83% (v/w) from an infusion experiment of 131I-labeled human serum albumin. The net uptake of fungal beta-galactosidase by rat brain was calculated as equal to 10 micrograms protein of the fungal enzyme or 0.31% of the injected dose/g tissue, which gave rise to 4.4-fold net increase in enzyme activity above control levels. The experiments clearly demonstrated that liposome-entrapped fungal enzyme was allowed to penetrate the blood-brain barrier and to gain access to rat brain, suggesting liposomes as an effective carrier for exogenous enzyme delivering to the central nervous system of patient with inherited lysosomal storage diseases.

Animals↗
PubMed1982

Comparison of cytosolic and mitochondrial enzyme alterations in the livers of propionic or methylmalonic acidemia: a reduction of cytochrome oxidase activity.

The activities of mitochondrial, cytosolic and microsomal enzymes in liver specimens obtained from three patients with propionic or methylmalonic acidemia were compared with those of control patients who had died from unrelated causes. Only the activity of cytochrome oxidase (mitochondrial enzyme) was significantly reduced in the patients of propionic acidemia and methylmalonic acidemia who were in the state of metabolic acidosis; in two patients the activity was less than 30% of that in controls, but in the other patient of propionic acidemia, who was under the treatment with a low protein diet (0.8 g/kg/day), the activity was 50% of that in controls. The metabolites of branched chain amino acids (tiglic acid, propionic acid, methylmalonic acid, succinic acid, tiglyl-CoA and propionyl CoA) exhibited no inhibitory effect on the cytochrome oxidase activity of the sonicated rat liver mitochondria. The reduction of cytochrome oxidase activity found in these organic acidemias may be caused secondarily by some unknown mechanism.

Amino Acid Metabolism, Inborn Errors↗
PubMed1982

Pyruvate decarboxylase deficiency in a patient with Leigh's encephalomyelopathy.

A 23-month-old boy with progressive muscular hypotonia and mental and motor deterioration was described. Four days after the admission he had a respiratory arrest and required the care in a respirator thereafter. Laboratory examinations showed metabolic acidosis and high levels of pyruvate, lactate and alanine in blood and cerebrospinal fluid. Oral administration of thiamine-HCl and lipoic acid was noneffective and he died 7 months after the admission. Autopsy findings were compatible with subacute necrotizing encephalomyelopathy (Leigh's disease). The activity of pyruvate decarboxylase in autopsy samples was not detectable and that in fibroblasts was 9% of that in control cell lines. The present study confirmed that pyruvate decarboxylase deficiency is one of the causes of Leigh's disease.

Brain↗
PubMed1982

Urinary metabolite profile of tiaramide in man and in some animal species.

1. The metabolism of tiaramide, 4-[(5-chloro-2-oxo-3(2H)-benzothiazolyl)acetyl]-1-piperazineethanol, was studied in healthy male volunteers and experimental animals. 2. Tiaramide was extensively metabolized in human with only 1.5% excreted unchanged. 3. Urinary metabolites were identified by FD, CI and EI mass spectral comparison with authentic standards. The major urinary metabolites in human were 4-[(5-chloro-2-oxo-3(2H)-benzothiazolyl)acetyl]-1-piperazineacetic acid (TRAA), 4-[(5-chloro-2-oxo-3(2H)-benzothiazolyl)acetyl]-1-piperazineacetic acid 1-oxide (TRAO) and the O-glucuronide of tiaramide. 4. TRAO, a new metabolite identified in human urine, was also present in mouse, rat, guinea-pig and monkey, but in smaller amounts than for human. 5. Sex differences in the excretion of sulphate of tiaramide were noted only in the rat.

Adult↗
PubMed1982

[Concentrations of cefmenoxime and cefotiam in the human bone marrow blood (author's transl)].

In order to examine the venous blood and bone marrow blood concentrations of cefmenoxime (CMX) and cefotiam (CTM) in man, 1 g of CMX or CTM was administered by one shot intravenous injection prior to surgery of the hip joint. At 30, 60, 120 and 180 minutes after the administration, venous blood and bone marrow blood were collected from each of 3 patients and the concentration assayed by the agar well method. Both CMX and CTM showed excellent distribution to bone marrow blood with peak levels of 50.1 micrograms/ml and 50.9 micrograms/ml on the average 30 minutes after administration. The levels of CMX in bone marrow blood exceeded those in the venous blood at 60 minutes and thereafter and CTM at 30 minutes of administration and thereafter. It is therefore considered that both CMX and CTM appear to be useful drugs for the prophylaxis and treatment of bone marrow infection, e.g. osteomyelitis.

Adolescent↗