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Biomedical subjects

M Matsuo

Publications and source records attributed to M Matsuo.

At least 523 records · Page 29Linked to original sources
PubMed1982

Increased excretion of four acetyl-CoA precursors during clinical episode of propionic acidaemia.

Propionic acidaemia (McKusick 23200) is caused by reduced activity of propionyl-CoA carboxylase (EC 6.4.1.3). A number of metabolites characteristic of this disease are excreted in patients' urine. We have developed a method of chemical diagnosis using gas chromatography-mass spectrometry (GC-MS). Since our first chemical diagnosis (Matsumoto et al., 1978), we have diagnosed seven patients. Profiles of urinary acids, however, varied from patient to patient. Factors affecting these profiles may be genetic make-up, age, or the patient's clinical and nutritional conditions. We have compared two metabolic profiles of a girl under different clinical conditions and found increased excretion of acetyl-CoA precursors during clinical episodes.

Acetyl Coenzyme A↗
PubMed1982

Ploidy of human embryonic fibroblasts during in vitro aging.

The DNA content of single nuclei in confluent cultures of aging human embryonic fibroblasts, TIG-3, was measured by means of flow cytofluorometry. In the early and late stages of their in vitro lifespan, they had considerable numbers of 4C, 8C and 16C nuclei. In the other period more than 95% of their nuclei were 2C nuclei. These results were confirmed by karyotype analysis. Presumably, the polyploid cells in young cell populations are removed due to their low growth potential and those in old cell populations are accumulated as a result of cellular aging. The saturation density of TIG-3 cells increased at the beginning of their lifespan and thereafter decreased. The rise in their saturation density seems to reflect cell selection advantageous for young diploid cells.

Cell Survival↗
PubMed1982

[Evaluation of the clinical effect and tissue distribution of piperacillin in the field of obstetrics and gynecology].

Piperacillin (PIPC) was administered to patients with obstetrical and gynecological infectious diseases and we studied its clinical effect and tissue distribution. 1. Clinical results. PIPC was administered to 26 patients at a dose of 2--4 g per day (twice a day) by dripping infusion over a period of 3--10 days (total 8--30 g). These included 16 cases with intrauterine infection, 1 with adnexitis, 4 with pelvic inflammatory disease and 5 with infections of the external genitalia. The clinical results were excellent in 11 cases, good in 13 cases and poor in 2 cases so that the overall efficacy rate was 92.3%. For bacteriological study 33 strains were isolated from 20 patients. These included Gram positive bacteria (6 strains), Gram negative bacteria (23 strains) and anaerobes (4 strains). After PIPC treatment 32 strains (including S. epidermidis 4 strains, E. coli 12 strains, K. pneumoniae 3 strains, E. aerogenes 2 strains, P. aeruginosa 2 strains and anaerobes 4 strains, etc.) disappeared except for 1 strain of K. pneumoniae which persisted. The disappearance rate was 97.0%. The only side effect observed was a slight case of malaise during the first administration day, however the relationship between the appearance of this symptom and the drug was unclear. No adverse reaction in laboratory findings was observed. 2. Tissue distribution. We determined the tissue concentration from 90 to 240 minutes after dripping infusion for 1 hour at a dose of 2 g. PIPC concentrations in these tissues including the endometrium, myometrium, cervix uteri, portio vaginalis, oviduct and ovary showed the highest level (18.0--11.7 micrograms/g) at 90 minutes after the beginning of administration. These values were 48.6--31.6% in respect to the uterine arterial blood level (37 micrograms/ml at 90 minutes after infusion).

Adult↗
PubMed1981

Congenital insensitivity to pain with anhidrosis in a 2-month-old boy.

In a 2-month-old boy with congenital insensitivity to pain and anhidrosis, the initial symptom was recurrent fever of unknown origin. After eruption of the first teeth, self-mutilation of the tongue was limited by extraction of the teeth. Unmyelinated fibers were essentially lacking, and the number of small myelinated fibers was decreased in sural nerve. This case is the youngest to be diagnosed and the first one in which nerve biopsy clearly showed the characteristic findings.

Humans↗
PubMed1980

Modification and identification of glutamate residues at the arginine-recognition site in the catalytic subunit of adenosine 3' :5'-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle.

It has been proposed that the active centre of cyclic AMP-dependent protein kinase contains an arginine-recognition site, which is considered to be essential for the function of the catalytic subunit of the kinase [Matsuo, Huang & Huang (1978) Biochem. J.173, 441-447]. The catalytic subunit can be inactivated by 3-(3-dimethylaminopropyl)-1-ethylcarbodi-imide and glycine ethyl ester at pH6.5. The enzyme can be protected from inactivation by preincubation with histone, a protein substrate of the enzyme. On the other hand, ATP, which also serves as a protein kinase substrate, does not afford protection. Polyarginine, a competitive inhibitor of protein kinase, which is known from kinetic studies to interact specifically with the arginine-recognition site, partially protects the catalytic subunit from inactivation by 3-(3-dimethylaminopropyl)-1-ethylcarbodi-imide. These results lead to the conclusion that the site of modification by carbodi-imide/glycine ethyl ester is most likely located at the arginine-recognition site of the active centre. A value of 1.7+/-0.2 (mean+/-s.d.) mol of carboxy groups per mol of catalytic subunit has been obtained for the number of essential carboxy groups for the function of protein kinase; a complete chemical modification of these essential carboxy groups results in total loss of catalytic activity. Finally, we have identified the essential carboxy group in the catalytic subunit of cyclic AMP-dependent protein kinase as being derived from glutamate residues. This is achieved by a three-step procedure involving an extensive proteolytic digestion of the [1-(14)C]glycine ethyl ester-modified enzyme and two successive high-voltage electrophoreses of the hydrolysate. It is concluded that 1.7mol of glutamyl carboxy groups per mol of catalytic subunit may be considered a component of the arginine-recognition site in the active centre of cyclic AMP-dependent protein kinase.

Amino Acids↗