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Biomedical subjects

S Maehara

Publications and source records attributed to S Maehara.

At least 37 records · Page 2Linked to original sources

Immunochemical determination of the serum protein reacting with antibody against human urinary trypsin inhibitor by single radial immunodiffusion: use of polyethylene glycol.

A single radial immunodiffusion method is described for determining the serum protein which reacts with antibody against the urinary trypsin inhibitor, but does not react with anti-inter-alpha-trypsin inhibitor antibody. Since the amount of this protein could not be determined with an agar plate containing antibody alone, we first prepared an agar plate containing 4% polyethylene glycol 6 000 and 1 mg of anti-urinary trypsin inhibitor gamma-globulin and confirmed that the amount of this protein could be measured accurately from the sizes of precipitin rings after 72 h incubation at room temperature. Levels of this serum protein, alpha 1-antitrypsin, alpha 2-macroglobulin and inter-alpha-trypsin inhibitor were measured in normal human serum by the single radial immunodiffusion method, and it was confirmed that the level of this serum protein did not correlate with the levels of these 3 other proteins.

Antibodies↗

A case of prostatic carcinoma with skin metastases.

The 30th case of metastatic skin carcinoma of prostatic origin was presented. The cytosolic R1881 receptor was detected moderately in the metastatic nodule of the skin, however, the measurement of this receptor had a limited value for the purpose of treating the patient with antiandrogenic agents.

Adenocarcinoma↗

Displacing effects of chenodeoxycholic acid, ursodeoxycholic acid and sulfadimethoxine on plasma protein binding of tolbutamide.

The interactions between chenodeoxycholic acid (CDCA) or ursodeoxycholic acid (UDCA) and tolbutamide including its displacement from plasma protein binding sites were investigated pharmacokinetically. An increasing concentration of unbound tolbutamide was observed in the in vitro experiment, conducted by equilibrium dialysis method at 30 degrees C after the addition of CDCA and UDCA to human serum albumin (HSA), bovine serum albumin (BSA) and rabbit plasma containing tolbutamide. Small changes in total plasma concentration of tolbutamide were noted after high dose (0.167 mg/kg/min) intravenous infusion of CDCA to rabbits receiving a constant intravenous infusion of tolbutamide, but, such an observation was not obtained with low dose (0.083 mg/kg/min) of CDCA or with either high or low dose of UDCA. These results seem to indicate the displacement of high doses of CDCA. The coadministration of sulfadimethoxine which not only displaces tolbutamide from binding sites but also inhibits its metabolism was investigated. A different plasma pattern was obtained under the same intravenous infusion conditions, as compared with the plasma pattern resulting from tolbutamide-CDCA or UDCA combination.

Animals↗

Effect of anticancer drugs on renal neoplasm induced with xenotropic pseudotype kirsten murine sarcoma virus.

The sensitivity of a renal neoplasm induced in vivo with C type RNA virus to anticancer drugs was evaluated. The proliferation rate of the virus induced neoplasm cells depended on the concentrations of antimetabolites, alkylates and antibiotics, but not depends on that of alkaloids. An inhibitory effect of drugs on the virus induced neoplasm cells became evident in the following order, i.e., antimetabolites, alkylates, antibiotics and then alkaloids.

Animals↗

Pain and internal hypertension in bone lesions.

Internal pressures of bone tumors and tumorous conditions were measured in 20 patients. High pressures were frequently found in patients with painful bone lesions while low pressures were common in patients with no pain. Internal hypertension may be a causative factor of aching bone pain at rest.

Blood Pressure↗

[In vitro cytotoxicity of methotrexate].

Five murine tumor cells (sarcoma 1509a, Gc-4, YAC-1, Dunn osteosarcoma, Lewis lung carcinoma) were exposed to methotrexate (MTX) at concentrations of 10(-1)-10(-9) mg/ml for 4-72 hours in vitro and then assayed for their viability. The effect of cell killing by MTX was dependent on both exposure time and concentration of the agent. MTX at a concentration of 10(-5) mg/ml killed the entire cell population in 72 hours, whereas the agent was not particularly effective even at a concentration of 10(-1) mg/ml on exposure for 4 hours. There was a close relation between doubling time of tumor cells and exposure time to MTX for killing entire populations of the tumor cells. The longer doubling time of the tumor cells was, the longer exposure time to MTX was needed to kill them. Lewis lung carcinoma was less sensitive to MTX than other sarcomas. The effect of citovorum factor (CF) on tumor cell killing by MTX was studied on sarcoma 1509a. After exposure to MTX sarcoma 1509a populations could not be rescued by the treatment of CF.

Animals↗

Radioimmunological quantitation of urinary trypsin inhibitor.

Using monospecific antibody to human urinary trypsin inhibitor, we developed a highly specific and sensitive radioimmunoassay (RIA) for measuring human urinary trypsin inhibitor. No cross-reactivity of the antibody with protein standard serum, which contained albumin, alpha 1-antitrypsin, haptoglobin, alpha 2-macroglobulin, transferrin, IgG and IgA, was observed. The sensitivity of the system was 10 ng of trypsin inhibitor per assay tube, and 5-10 microliters of urine was sufficient to determine the concentration of trypsin inhibitor in urine. The amounts excreted in the urine of 10 healthy men and 10 healthy women were 4.83 +/- 2.46 (mean +/- SD) and 3.86 +/- 1.35 mg/day, respectively. The correlation between estimates by RIA and those by enzymic assay was r = 0.96 (p less than 0.005). The method proposed here can be used to determine the concentration of urinary trypsin inhibitor in a small amount of biological fluids and cells.

Adult↗

Multiple molecular forms of acid-stable plasmin inhibitor derived from human urinary trypsin inhibitor.

It was found that cyanogen bromide (BrCN) treatment of the highly purified human urinary trypsin inhibitors (H-UTI; specific activity 1,897 U/mg protein, and L-UTI; specific activity 1,850 U/mg protein) readily produced new plasmin inhibitors with almost no loss of UTI activity. Five multiple forms of chemically cleaved inhibitors (UTIB-I, UTIB-II, UTIB-III, UTIB-IV and UTIB-V) could be isolated from BrCN-treated L-UTI by isoelectric focusing and gel filtration. These inhibitors were very acid-stable and their isoelectric points (pI) were 4.5, 4.6, 4.9, 5.1 and 6.4, respectively. The molecular weights by SDS-polyacrylamide gel electrophoresis were almost the same at about 23,000 +/- 3,000. Although these inhibitors showed both anti-plasmin and anti-trypsin activities, much higher anti-plasmin/anti-trypsin activities were observed in the cleaved inhibitors than in the parent UTI. They competitively inhibited human plasmin with Ki values of 3.0-4.1 X 10(-8) mol/l (H-D-Val-Leu-Lys-pNA substrate).

Antifibrinolytic Agents↗

The aetiology and treatment of simple bone cysts.

The internal pressure of simple bone cysts was found to be slightly higher than the normal pressure of the bone marrow in the contralateral limb. The pressure within the cyst was measured during drilling with a Kirschner wire; it gradually decreased as the number of drill-holes increased. The PO2 of the cyst fluid was markedly lower than that of either venous or arterial blood measured synchronously. It is suggested that venous obstruction in the bone is the likely cause of these cysts. Seven patients with simple bone cysts were treated by the multiple drill-hole method, and the clinical outcome was excellent. Multiple drilling may prove to be the treatment of choice for simple bone cysts in the younger patient, as it presents fewer hazards than other procedures.

Adolescent↗

Purification and some properties of a plasma protein which reacts with an antiserum against urinary trypsin inhibitor-1.

A plasma protein which forms a precipitation line with antiserum against urinary trypsin inhibitor was purified by ammonium sulphate fractionation, anti-urinary trypsin inhibitor rabbit IgG antibody coupled sepharose immunoadsorbent column chromatography and polyacrylamide-gel disc electrophoresis. By these procedures, 0.14 mg of purified material was obtained from 20 ml of plasma. It was homogeneous as ascertained by sodium dodecyl sulphate polyacrylamide-gel disc electrophoresis and had an apparent molecular weight of 90,000. It was found that this inhibitor was immunologically distinct from inter-alpha-trypsin inhibitor.

Alpha-Globulins↗