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Biomedical subjects

S Fujii

Publications and source records attributed to S Fujii.

At least 865 records · Page 48Linked to original sources
PubMed1982

Molecular structure of the octamer d(G-G-C-C-G-G-C-C): modified A-DNA.

The deoxynucleotide fragment d(GpGpCpCpGpGpCpC) was synthesized and crystallized, and its three-dimensional structure was determined by x-ray diffraction techniques to a resolution of 2.25 A. The molecule forms a right-handed double helix in which the two base pairs at either end of the molecule are in the conventional A-DNA conformation, while the central four base pairs have a modified form in which alternate residues have sugar conformations that are closer to those in B-DNA than in A-DNA. The molecules have an intermolecular contact in which the planar terminal guanine . cytosine base pair lies on the flat minor groove surface of the A-DNA helix.

Crystallization↗
PubMed1982

Dynamic states of the three methionyl residues of Streptomyces subtilisin inhibitor. 1H NMR studies.

High resolution 1H NMR spectroscopy at 360 and 400 MHZ was used to study the dynamic states of the three methionyl residues (Met 70, 73, and 103) of Streptomyces subtilisin inhibitor (SSI) in a neutral aqueous (2H2O) solution. Chemical modification and nuclear Overhauser effect studies show that one of the methyl groups exists in the interior of the protein and is surrounded by phenylalanyl residues. With reference to the crystal structure, this methyl group is assignable to that of Met 103 in the hydrophobic core. The other two methionyl residues (Met 70 and 73) are equally susceptible to chemical modifications, but their methyl signals are affected in a different manner by the alpha-chymotrypsin-cleavage of the peptide bond between Met 73 and Val 74 at the reactive site. The observed linewidths of the methyl groups are consistent with the assumption that the whole side-chain of both Met 70 and 73 are already undergoing rapid internal motions at 20 degrees C, whereas for Met 103 only the rotation of the methyl group is allowed, even above approximately 40 degrees C. The high-field shift of the methyl proton resonance of Met 103 by about 0.3 ppm is attributable to the ring current effect from the surrounding phenylalanyl residues. This shift is invariant in the temperature range of 40-90 degrees C, showing that the native environment of the methyl group of Met 103 persists up to 90 degrees C at neutral pH. Destruction of the native methionyl environments occurs only above 90 degrees C, and the rate of conversion between the native and the denatured conformations is slower than 10 s-1. When SSI is mixed with subtilisin BPN' in a one-to-one molar ratio, at least one of the methyl signals of Met 70 and 73 is completely broadened, showing that the side-chain of this methionine is directly involved in the interaction with the enzyme.

Bacterial Proteins↗
PubMed1982

Spontaneously acquired factor VIII inhibitor in a 7-year-old girl.

The youngest case with spontaneously acquired inhibitor to factor VIII is reported. A 7-year-old girl without any previous disorders presented with a hemarthrosis in the left knee and developed a rapidly expanding hematoma on the right arm, shoulder and chest after an initial infusion of factor VIII concentrate (1,000 units). Circulating antifactor VIII antibody was detected. Her coagulopathy was successfully managed with an additional massive infusion of factor VIII concentrate (7,500 units) and combination therapy of prednisolone and cyclophosphamide.

Autoantibodies↗
PubMed1982

Inhibition of various immunological reactions in vivo by a new synthetic complement inhibitor.

FUT-175 (6 amidino-2-naphthyl-4-guanidino benzoate-dimethanesulfonate), a new synthetic protease inhibitor, inhibits the enzyme activities of various proteases, such as Clr, C1 esterase, thrombin, kallikrein, plasmin and trypsin. FUT-175 strongly inhibited complement-medicated hemolysis via the classical and alternative pathways. The effects of FUT-175 on various immunological reactions in vivo were studied. The minimal effective dose of FUT-175 in systemic Forssman shock in guinea pigs was 6.25 mg/kg i.p. and 25 mg/kg p.o. In passive Arthus reactions in rats, the effective dose was 25 mg/kg i.p. and 250 mg/kg p.o. FUT-175 also inhibited other immunological reactions, such as passive cutaneous anaphylaxis and delayed hypersensitivity. Furthermore, at a dose of 25 mg/kg i.p. it strongly protected mice from death in endotoxin shock.

Animals↗
PubMed1982

Cerebrospinal fluid edema: a rare complication of shunt operations for hydrocephalus. Report of three cases.

Three cases are presented in which a rare complication occurred after a shunt operation for hydrocephalus. On postoperative computerized tomography (CT) scans, extensive low-density areas appeared in the white matter along the ventricular catheter. After shunt revision, gradual resolution or disappearance of the low-density area was clearly demonstrated on CT. In one patient, a collection of cerebrospinal fluid (CSF) was confirmed at operation and appeared to lie in the extracellular spaces of the white matter. The phenomenon is considered to be localized CSF edema, different from porencephaly.

Cerebrospinal Fluid↗
PubMed1982

Activities of various enzymes of pyrimidine nucleotide and DNA syntheses in normal and neoplastic human tissues.

The activities of the key enzymes of pyrimidine nucleotide and DNA syntheses in 43 human tumors and 28 normal human tissues were investigated. The activities of cytidine triphosphate synthetase, deoxycytidine monophosphate deaminase, uridine kinase, thymidine kinase, thymidine monophosphate kinase and DNA polymerase were markedly increased in tumor tissues, compared with those in the corresponding normal tissues, while the activities of deoxycytidine kinase, cytidine deaminase and deoxycytidine deaminase were only slightly increased. The use of thymidine and deoxyuridine as substrates of human pyrimidine nucleoside phosphorylase gave 1 to 2 orders of magnitude higher activity than that of uridine.

Carbon-Nitrogen Ligases↗
PubMed1982

Effect of oral administration of protease inhibitor [N,N-dimethylcarbamoylmethyl 4-(4-guanidinobenzoyloxy)-phenylacetate] methanesulfate on the growth of 3-methylcholanthrene-induced carcinoma in mice.

Oral administration of a synthetic protease inhibitor. [N,N-dimethylcarbamoyl-methyl 4-(4-guanidinobenzoyloxy)-phenylacetate] methanesulfate, was used to challenge 3-methylcholanthrene-induced carcinoma. This drug was administered 3 times daily via a stomach tube at doses of 12.5, 25 and 50 mg/kg in 33 mice harboring solid tumors. Oral administration of more than 50.0 mg/kg of this protease inhibitor significantly inhibited tumor growth and prolonged the survival time of cancer-harboring animals (P les than 0.05). These results indicate that oral administration of an inhibitor of kinin-forming protease has an antitumor effect on malignant tumors.

Animals↗
PubMed1982

Growth factor from tumor cells.

Suitable conditions for assay of the growth factor from Yoshida sarcoma and AH-130 tumor cells were investigated using three different cell lines: baby hamster kidney cells, human embryonic lung cells and Swiss Albino mouse 3T3 embryo fibroblast cells. The results indicated that the 3T3 cell line was more sensitive to the growth stimulating activity than the other two lines. A fraction of Yoshida sarcoma tumor cells containing the growth factor showed less growth stimulating activity than a fraction of AH-130 tumor cells prepared by the same method. Using the 3T3 cell line for assay of activity, the growth factor was partially purified from AH-130 tumor cells by ammonium sulfate fractionation, DEAE-cellulose column chromatography and gel filtration on a Sephacryl S-300 column. It appeared to be thermolabile, and its molecular weight was estimated as about 80,000 by gel filtration on Sephacryl S-300. These findings suggest that it is a high-molecular-weight substance.

Animals↗
PubMed1982

[Scanning electron microscopic observations of microcorrosion casts for non pregnant rat uterine vascular architecture (author's transl)].

Uterine vascular architecture through estrus cycle of the rat was investigated by the microcorrosion casting/scanning electron microscopy method. Arterial system in the uterine horn was divided into two types, one of which consisted of circumferential artery with its branches extending to both side walls and an antimesometrial wall. The other system consisted of arterioles which turned into the vascular congromerate in the mesometrial triangle and then distributed their branches to the mesometrial wall. Both of two kinds of arterioles, the terminal arteriole in the myoendometrium and the larger arteriole composing the vascular congromerate, showed the circular impressions around them. Arteriovenous anastomosis was not observed in the uterus. During proestrus and estrus, uterine blood vessels were lengthened except for arterioles in the vascular congromerate, and the subepitherial capillary network became to be filled completely with resin and showed the signs of leakage. These changes reached the maximum in estrus, then subsided during the later part of the cycle. These observations suggest that different types of arterioles in the uterus have their own sphinctors, and maximum enlargement of the uterine vascular bed occurs in estrus concomitantly with increased capillary permeability.

Animals↗
PubMed1981

New synthetic inhibitors of C1r, C1 esterase, thrombin, plasmin, kallikrein and trypsin.

p-Guanidinobenzoate derivates were prepared and their inhibitory effects on trypsin, plasmin, pancreatic kallikrein, plasma kallikrein, thrombin, C1r and C1 esterase were examined. Among the various inhibitors tested, 6'-amidino-2-naphthyl-4-guanidinobenzoate dihydrochloride, 4-(beta-amidinoethenyl)phenyl-4-guanidinobenzoate dimethanesulfonate and 4-amidino-2-benzoylphenyl-4-guanidinobenzoate dimethanesulfonate were the most effective inhibitors of trypsin, plasmin, pancreatic kallikrein. plasma kallikrein and thrombin and they strongly inhibited the esterolytic activities of C1r and C1 esterase, and then strongly inhibited complement-mediated hemolysis.

Benzamidines↗