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Biomedical subjects

S Fujii

Publications and source records attributed to S Fujii.

At least 919 records · Page 51Linked to original sources
PubMed1980

Plasma active and inactive renin in patients with diabetes mellitus.

Plasma active and acid activated inactive renin was measured in healthy subjects and in patients with diabetes mellitus. The angiotensin I generated from the incubation of non-acidified plasma with pig renin substrate was expressed as plasma renin concentration (PRC) and that from acidified plasma was expressed as total renin concentration (TRC). The inactive renin concentration (IRC) was calculated as TRC minus PRC. With regard to plasma renin activity (PRA) and PRC, no significant difference was found between normal and diabetic groups. TRC and IRC in diabetics with no clinical sign of microangiopathy were 22.8 +/- 1.7 and 15.2 +/- 1.3 ng/ml/h (mean +/- SE), and these values were not significantly different from those in the healthy subjects (20.5 +/- 1.5 and 13.2 +/- 1.5 ng/ml/h). However, TRC and IRC in diabetics with retinopathy and clinical nephropathy was 38.8 +/- 3.4 and 30.7 +/- 3.2 ng/ml/h, and these values were significantly higher than those in the above two groups, respectively. Moreover TRC and IRC in diabetics with retinopathy and no clinical nephropathy was 33.8 +/- 5.7 and 24.9 +/- 5.5 ng/ml/h, and these values were significantly higher than those in the control group. IRC was not significantly correlated with fasting blood sugar and mean blood pressure levels, however however a significant correlation was found between IRC and BUN, and IRC and P.S.P. excretion in 15 minutes. These findings suggest that increased inactive renin in diabetes mellitus may be related to the progression of the renal lesions associated with diabetic microangiopathy.

Adult↗
PubMed1980

Effect of coadministration of thymine or thymidine on the antitumor activity of 1-(2-tetrahydrofuryl)-5-fluorouracil and 5-fluorouracil.

The antitumor activity of 1-(2-tetrahydrofuryl)-5-fluorouracil (FT-207) on sarcoma was enhanced by oral coadministration of uracil, thymine, or thymidine. The activity was enhanced equally by thymine and by uracil than by thymidine, but thymine caused loss in body weight. The antitumor activity of 5-fluorouracil (5-FU) was also enhanced by thymine or uracil, but both caused loss in body weight. Degradation of 5-FU in vitro was inhibited more by thymine than by uracil. Phosphorylation of 5-FU, however, was not inhibited by uracil, thymine, or thymidine, even at 100 times the concentration of 5-FU. These results suggest that the mechanism of enhancement of the antitumor activity of FT-207 by thymine or thymidine was similar to that by uracil, and that uracil had more effect than thymine or thymidine in enhancing antitumor effect of these drugs to FT-207 without toxicity.

Administration, Oral↗
PubMed1980

Metabolism, antitumor activity, and acute toxicity of 5-fluoro-1,3-bis(tetrahydro-2-furanyl)-2,4-pyrimidinedione by oral administration to animals.

The metabolism, antitumor activity, and acute toxicity of 5-fluoro-1,3-bis-(tetrahydro-2-furanyl)-2,4-pyrimidinedione (FD-1) were investigated in animals, compared with 5-fluoro-1-(tetrahydro-2-furanyl)-2,4-pyrimidinedione (FT). It was found that after oral administration of FD-1, the level of 5-fluorouracil (5-FU) was maintained higher and longer than after administration of FT, and that a large amount of 5-FU was released from FD-1 by liver microsomal drug-metabolizing enzymes or spontaneous hydrolysis via 5-fluoro-3-(tetrahydro-2-furanyl)-2,4-pyrimidinedione (3-FT) and FT. FD-1 had a significant activity against the solid form of Ehrlich carcinoma, sarcoma-180, hepatoma AH130, Yoshida sarcoma, Walker carcinosarcoma-256, and leukemia L1210 and P388, but not the ascitic forms, and it produced greater inhibition of tumor growth than FT. The acute toxicity of FD-1 was less than that of FT.

Administration, Oral↗
PubMed1980

Comparison of proteases in normal and metaplastic human stomach mucosa.

The proteases in normal and metaplastic human stomach mucosa were examined by preparing zymograms of tissue extracts with tosyl-L-lysine-alpha-naphthyl ester and L-prolyl-L-phenylalanyl-L-arginine-alpha-naphthyl ester as substrates. With both substrates, the zymogram of metaplastic mucosa showed an additional band (Rf 0.64) not present with normal mucosa. This band was also observed with extracts of normal small intestine and cancerous stomach tissue. It disappeared on treatment of the preparations with leupeptin, but not with esterastin.

Gastric Mucosa↗
PubMed1980

DNA synthesis in tumor-bearing rats: purification of liver thymidine kinase stimulating factor from Yoshida sarcoma.

Yoshida sarcoma cells contain a factor that stimulates thymidine kinase activity in the liver of mice in vivo; intraperitoneal injection of an extract from Yoshida sarcoma into normal mice stimulated their liver thymidine kinase activity 2- to 3-fold, whereas injection of a crude extract of normal rat liver did not stimulate the activity at all. A factor that stimulates the de novo synthesis of thymidine kinase in the liver was partially purified from Yoshida sarcoma by ammonium sulfate fractionation, DEAE-cellulose column chromatography and gel filtration. It appeared to be thermolabile and sensitive to trypsin treatment. These results suggested that it was a high-molecular weight protein. Intraperitoneal injection of this factor into 67% hepatectomized rats stimulated thymidine kinase activity 2- to 3-fold. Increase of liver thymidine kinase activity after injection of the factor into mice was blocked by simultaneous injection of actinomycin-D. These results suggest that this factor stimulates de novo synthesis of thymidine kinase in the liver.

Animals↗
PubMed1980

[The effect of human cord plasma on the incorporation of 3H-thymidine by PHA-stimulated peripheral blood lymphocytes of cervical cancer patient (author's transl)].

It has been proposed that human cord plasma can suppress the PHA response of adult lymphocytes. To compare the suppressive effects between plasma from cancer patients and human cord plasma, we investigated the PHA responses of lymphocytes which were sampled from patients with various stages of cervical cancer and cancer free women, by adding cancer auto-plasma, human cord plasma and control plasma. The PHA responses of normal lymphocytes cultured with plasma from patients with 2nd and advanced stage of cancer were suppressed, but they were not suppressed by the plasma from O-I stage of cancer. The addition of control plasma enhanced PHA responses of lymphocytes of the 2nd and advanced stage of cancer, but no changes were observed in the lymphocytes from O-I stage of cancer. These results suggest that inhibitory factor does not appear in the plasma from the patients with O-I stage of cervical cancer. Human cord plasma moderately suppressed the PHA responses of normal lymphocytes; it also suppressed the PHA responses of lymphocytes from O-I stage of cancer. However, the PHA responses of lymphocytes from 2nd and advanced stage of cancer were improved significantly. Cord plasma may have a factor which promotes the PHA responses of lymphocytes from advanced cancer.

Adult↗
PubMed1980

Dinucleoside monophosphate having a high anti conformation. II. The crystal structure of 8,2'-S-cycloinosinyl-(3',5')-8,2'-S-cycloadenosine hexahydrate.

The crystal and molecular structure of 8,2'-S-cycloinosinyl-(3',5')-8,2'-S-cycloadenosine (IspAs) hexahydrate has been determined by X-ray diffraction method. The torsion angles around the sugar-phosphate backbone are unique and different from those found in the crystalline dinucleoside monophosphates so far determined. The rotation around the P-O bond, (omega',omega), is (g+,t). An IspAs molecule is in a folded form. There is no intramolecular base stacking or base-pairing but the intermolecular base stacking is dominant.

Base Composition↗
PubMed1980

Metabolic differences in deoxyribonucleoside triphosphate hydrolysis between rat liver and Yoshida sarcoma cell chromatins.

Enzymatic activities for deoxyribonucleoside triphosphate hydrolysis associated with Yoshida sarcoma and normal rat liver chromatins were comparatively studied. Deoxyribonucleoside triphosphate-hydrolyzing activities were isolated from purified chromatins of Yoshida sarcoma cells and normal rat liver, and gel-filtered on Sephadex G-200 columns. A single peak of dUTP-hydrolyzing activity from the Yoshida sarcoma chromatin and three peaks from the normal liver chromatin were observed. The first peak from the normal chromatin hydrolyzed dATP, dCTP and TTP mainly to the corresponding deoxyribonucleoside diphosphates, and dUTP and dGTP to the corresponding di- and mononucleotide forms. The activity in the first peak from the normal liver chromatin had an apparent Km of 2.5 X 10(-4) M for dUTP, required divalent cations and was inhibited by NaF. The peak from the Yoshida sarcoma chromatin corresponding to the first peak from the normal liver chromatin hydrolyzed all five deoxyribonucleoside triphosphates to deoxyribonucleoside diphosphates with minor co-production of mononucleotides. The enzyme activity from the malignant cells had an apparent Km of 2.5 X 10(-5) M for dUTP, required Mg2+, but was not inhibited by NaF.

Animals↗
PubMed1979

Occurrence of Leu-Lys-bradykinin and histidine-rich peptide in high-molecular-weight kininogen isolated from horse plasma.

On incubation of purified horse plasma high-molecular-weight kininogen with purified plasma kallikrein, three new peptides, named fragment 1.2, fragment 1 and fragment 2, were released, in addition to the vasopeptide, bradykinin. Fragment 2 contained an extremely high level of histidine, in which eleven residues out of the total 48 residues were characterized. Thus the result proves the existence of the histidine-rich region in horse high-molecular-weight kininogen, which is similar to the region previously identified in bovine high-molecular-weight kininogen. Moreover, we have identified a new kinin derivative, Leu-Lys-bradykinin, in horse high-molecular-weight kininogen.

Amino Acid Sequence↗
PubMed1979

The crystal and molecular structure of 8-methyladenosine 3'-monophosphate dihydrate.

8-Methyladenosine 3'-monophosphate dihydrate was synthesized and crystallized in the monoclinic space group P21 with the unit cell dimensions: a = 9.095(2) A, b = 16.750(3) A, c = 5.405(2) A and beta = 97.61(3) degrees. The structure was determined by the application of the heavy atom method and refined to give a final R factor of 0.047. The pertinent conformations are as follows: the syn conformation about the glycosyl bond (chiCN = 216.8 degrees), the C(2')-endo sugar puckering with the displacement of 0.55 A; and the gauche-gauche conformation about the C(4')-C(5') bond capable of forming an intramolecular hydrogen bonding between N(3) of adenine base and O(5') of the hydroxymethylene group on the ribose. The molecule exists in the zwitterionic form with the N(1) of the adenine base protonated by a phosphate proton and is stabilized by three-dimensional networks of hydrogen bonding through the crystalline water molecules or directly between the adjacent nucleotide molecules; no base stacking was observed.

Adenosine Monophosphate↗
PubMed1979

Rat stomach kallikrein: its purification and properties.

From rat stomach, kallikrein was purified by chromatographies on columns of p-aminobenzamidine-Sepharose, DEAE-Sephadex A-50 and Sephadex G-150 and by isoelectric focusing, measuring its activities to hydrolyse prolylphenylalanyl-arginine-4-methyl-coumarine amide (Pro-Phe-Arg-MCA) and to release kinin from rat heated-plasma. The purified stomach kallikrein showed a single band on Disc electrophoresis at pH 7.0. The molecular weight of the kallikrein was calculated to be 29,000 by gel-filtration on a column of Sephadex G-50. The kallikrein was stable between pH 6 and 11 and hydrolysed Pro-Phe-Arg-MCA optimally at pH 11.0. The Pro-Phe-Arg-MCA hydrolysing activity of rat stomach kallikrein was inhibited by DFP and Trasylol, but not by trypsin inhibitors from soyabean, limabean and ovomucoid. These properties of rat stomach kallikrein was clearly distinguishable from those of partially purified rat plasma kallikrein, but similar properties to other glandular kallikreins from other species. From these results, it was concluded that kallikrein is present in rat stomach, which can be classified into glandular kallikrein.

Animals↗