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H Terayama

Publications and source records attributed to H Terayama.

At least 19 recordsLinked to original sources
PubMed2001

Aqueous dispersion behavior of drug particles by addition of surfactant and polymer.

The effect of surfactant and polymer on dispersion stability of aqueous suspensions of 5-(3-ethoxy-4-pentyloxyphenyl)-2,4-thiazolidinedione (CT112) was investigated by measuring the adsorbed amount of surfactant and polymer, zeta potential, particle size, and sedimentation rate of CT112. The addition of celluloses rather than sodium dodecyl sulfate (SDS) provided a high stable suspension of CT112. In addition, mixed systems of celluloses and SDS enhanced CT112 dispersion more effectively. The mechanism of dispersion stability of CT112 by addition of SDS and celluloses is discussed.

Journal Article↗
PubMed1993

Synthesis of a new allosamidin analog, N,N'-diacetyl-beta-chitobiosyl allosamizoline and its inhibitory activity against some chitinases.

A new allosamidin analog (2), possessing an N',N'-diacetylchitobiosyl moiety as a constituent, was stereoselectively synthesized through the coupling reaction between the disaccharide thioglycoside derivative (5) and allosamizoline derivative (6). The inhibitory activity of 2 against chitinases derived from an insect, yeast and mold were tested and compared with that of allosamidin (1).

Acetylglucosamine↗
PubMed1989

Calciferin and cathepsin D-like acid protease in serum in acute and chronic liver injuries in rats and humans.

Serum from patients with chronic liver diseases (chronic hepatitis, cirrhosis, and hepatomas) contained greater concentrations of calciferin (total 1.7-fold, free 3.3-fold) than that from normal subjects. There were also decreases in the concentration and affinity of the calciferin-binding protein(s) in the patients' sera, but the amount of cathepsin D (EC 3.4.23.5)-like acid protease (total and free) was within normal limits. In addition, rats with acute liver injuries (partial hepatectomy or CCl4 administration) showed increases in calciferin and acid protease in their serum. Rats subjected to continuous feeding of 3'-methyl-4-dimethylaminoazobenzene (a potent hepatocarcinogen) also showed an increase of both analytes in the earlier stages (two to eight weeks; acute phase). Later (13 weeks or more; chronic phase), however, only acid protease appeared to return to normal values.

Acute Disease↗
PubMed1988

Cell density dependent morphological changes in adult rat hepatocytes during primary culture.

In order to gain morphological insights about the cell density dependency, hepatocytes cultured at a low cell density (less than about 0.1 X 10(5) nuclei (cm2)-1) and at a high cell density (greater than about 1 X 10(5) nuclei (cm2)-1) were examined ultrastructurally 24 h after plating (just prior to the beginning of DNA synthesis). The results were as follows: (i) glycogen rosettes disappeared completely in low density culture as compared with sections from an intact liver. In contrast, glycogen rosettes were still present in high density culture. (ii) Polysomes seemed increased in low density culture in comparison with those seen in sections from an intact liver and from the high density culture. (iii) In low density culture, the shape of mitochondria deviated from that of hepatocytes in an intact liver and the mitochondria often lost a characteristic close contact with rough endoplasmic reticulum (rough ER). (iv) In low density culture, bundles of filamentous structure were detected, which were not found in an intact liver or high density culture. The following features were found only in high density culture; (v) numerous villous cytoplasmic protrusions developed along the area facing adjacent cells, and seemed to intertwine with each other, and (vi) between the hepatocytes, only abortive junctions were found. These results indicate that the hepatocytes cultured at a low density express most of the characteristics of the hepatocytes in a regenerating liver and the features of the cells cultured at a high density are very similar to those of the hepatocytes in sections from an intact liver.

Animals↗
PubMed1987

Ubiquitous presence of calciferin-like and cathepsin D-like activities in the sera (vertebrates) and humoral fluids (invertebrates).

1. Sera (or humoral fluids) from various animals (vertebrates and invertebrates) were assayed for calciferin-like and cathepsin D-like activities, indicating the ubiquitous presence of the latter and the former (with a few exceptions). Animals other than the mammals appeared to contain an organophilic calciferin-like activity in addition to a hydrophilic component (calciferin). 2. A correlation was found between the levels of calciferin and acid protease in most of the mammalian sera. An age-dependent decrease in calciferin (but not acid protease) was found in human sera. The possible presence of an acid protease-inhibitor was suggested.

Animals↗
PubMed1985

Mitogenic effects of certain cathepsins and calciferin on the intact liver in vivo.

Calciferin, a new parathyroid hormone stimulating the release of cathepsins D and L (but not B) from isolated lysosomes, or the release of cathepsin D from erythrocytes or ghosts in vitro, elevated free cathepsin D in the blood, and at the same time stimulated DNA synthesis in the intact liver when it was injected into mice. Both calciferin and free cathepsin D in the blood (rats) were elevated concomitantly soon after 70% hepatectomy, reaching a peak around 5 hr. The cathepsin D-elevation was almost proportional to fractional hepatectomies. Cathepsin L (but not B), when injected intraperitoneally into mice, stimulated DNA synthesis and mitosis in the intact liver much like cathepsin D, the effect of which was reported earlier. In contrast to the mitogenic effects of calciferin or cathepsins (D and L) in vivo, only cathepsin L (but not cathepsin D or calciferin) in low concentrations appeared to stimulate DNA synthesis in the cultured liver cells, and also stimulated adenylate cyclase of isolated liver plasma membranes in vitro. Dibutyryl-cyclic AMP in concentrations lower than 10(-5) M also stimulated DNA synthesis in cultured liver cells.

Animals↗
PubMed1984

Arginase as one of the inhibitory principles in the density-dependent as well as plasma membrane-mediated inhibition of liver cell growth in vitro.

Liver cells isolated from the adult rat livers under mild conditions were preincubated for 1 day with Williams medium E (WE) containing serum, dexamethasone and insulin, and then the cells (monolayered) were incubated for 2-3 days with WE (1 ml) containing only insulin to measure DNA synthesis and/or mitosis. DNA synthesis of cultured liver cells was dependent on cell densities within a region from 0.1 X 10(6) to 1.0 X 10(6) nuclei/dish (Falcon, diameter 35 mm). The addition of EGF from the beginning of preincubation stimulated DNA synthesis (or replication) as well as cell proliferation in vitro, but the density-dependent inhibition of DNA synthesis was observed similarly in the presence of EGF. In contrast to the low and high density cultures, DNA synthesis in the intermediary density cultures was enhanced by enlarging the medium volume or by adding ornithine (arginase inhibitor). DNA synthesis in low density cultures was inhibited by liver plasma membranes in a concentration-dependent fashion. The inhibition of DNA synthesis by liver plasma membranes in low concentrations (less than 30 micrograms protein/ml) was reduced by adding either extra arginine or ornithine. DNA synthesis of cultured liver cells (low density) was inhibited by replacing arginine in WE with equimolar ornithine and urea or by adding a commercial arginase (bovine liver). These, together with earlier findings indicating the presence of arginase in liver plasma membranes (outer leaflet), seem to support the idea that arginase may be involved in density-dependent as well as plasma membrane-mediated inhibition of DNA synthesis of cultured liver cells. However, this does not exclude possible involvement of other inhibitory principle(s), such as direct cell-to-cell or cell-to-plasma membrane interactions, especially in higher cell densities or larger plasma membrane concentrations.

Animals↗
PubMed1984

Cathepsin D stimulates DNA synthesis and mitosis in mouse liver in vivo.

Effects of a single intraperitoneal injection of cathepsin D (CatD) on DNA synthesis and mitosis in the mouse liver and kidney were investigated. Twenty micrograms of catD induced a significant stimulation of DNA synthesis in the liver, but not in the kidney, in a dose-dependent fashion and with a peak activity at 38 h after the injection. CatD also stimulated liver mitosis, with a peak value at 44 h after the injection.

Animals↗
PubMed1984

A proteoglycan fraction isolated from the EDTA extract of sea urchin (Hemicentrotus pulcherrimus) gastrulae stimulates reaggregation of dissociated embryonic cells.

A sulfated proteoglycan fraction was prepared from mid-gastrulae Hemicentrotus pulcherrimus by chromatographing the EDTA extract of embryos on DEAE-cellulose and then on Sepharose 6B. A peak fraction (with MW greater than 10(6] of the Sepharose eluates stimulated in a concentration-dependent manner the reaggregation of cells dissociated from Hemicentrotus blastulae by EDTA treatment, the activity being detected at a concentration of as low as 5.8 micrograms protein per ml or 2.5 micrograms fucose per ml. The proteoglycan fraction appeared to contain sulfated fucan and glycosaminoglycan chains linked to a common protein. The glycan moiety obtained by digesting the fraction with protease failed to stimulate the cellular reaggregation.

Animals↗
PubMed1984

A serum factor stimulating cathepsin D-release from erythrocytes or ghosts.

A serum factor preparation extensively purified from bovine serum stimulated cathepsin D-release from the rat blood cells in a concentration-dependent fashion within a range of physiological concentrations of the factor. Among the blood cells only the erythrocytes (or ghosts) were responsive to the factor, and the leucocytes and lymphocytes were unresponsive. The effects of Ca2+-concentrations, SH- blocking reagents, protease-inhibitors, calmodulin-inhibitors, calmodulin or EGTA-pretreatment of the ghosts on cathepsin D-release from the erythrocytes of ghosts in the presence or the absence of serum factor were investigated. The results suggested that the serum factor may first activate the Ca2+-calmodulin system via the mobilization of "Ca2+-pool" and then the calmodulin-dependent SH-protease in the erythrocyte plasma membranes. The activated protease in turn may break the linkage between cathepsin D and the plasma membranes, liberating cathepsin D activity into the incubation medium. The name of "calciferin" was proposed for the serum factor.

Animals↗
PubMed1984

Tissue producing the serum factor stimulating the release of cathepsin D from lysosomes in vitro.

Pancreatectomy as well as thyroparathyroidectomy resulted in the quick disappearance of a serum factor (stimulating cathepsin D release from lysosomes in vitro) from the rat or mouse blood. Extirpation of other organs such as duodenum, stomach, spleen, kidney, submaxillary gland, testis, adrenal gland or hypophysis, showed no effect on the serum factor level. Glucagon (but not insulin or thyroxine) given to the pancreatectomized animals restored the serum factor level in a dose-dependent manner. The serum factor-like activity was detected only in the parathyroids (but not thyroid), and the release of activity from parathyroid-slices was stimulated by glucagon, suggesting that the parathyroid may produce and/or secrete the serum factor under the influence of glucagon.

Animals↗
PubMed1983

Sulfated glycan present in the EDTA extract of Hemicentrotus embryos (mid-gastrula).

Light microscopical observations of the Alcian blue-stained gastrulae of Hemicentrotus pulcherrimus together with the scanning electron microscopical observations of the embryos revealed the presence of highly acidic glycans in the invaginating archenteron (inside surface), the surrounding of secondary mesenchyme cells (pseudopodial protrusions and filamentous structures) and the hyaline layer. In the embryos grown in sulfate-free sea water and thus with arrested gastrulation it was found that the dye stainability in the above regions was markedly reduced. The glycosaminoglycan fraction prepared from the whole embryos (mid-gastrulae) was found to contain various kinds of acidic glycans as analysed by chromatography on DEAE-cellulose. Among these glycan components, the "F" component was mainly recovered in the EDTA extract of the embryos, and was shown to be specifically deleted in the embryos grown in sulfate-free sea water, suggesting that the "F" component may be related to the Alcian blue-stainable material in Hemicentrotus embryos. The component "F" was found to consist of sulfated fucan and acid mucopolysaccharide (unidentified) chains, which are probably linked to a common peptide core, forming macromolecules with larger than 10(6) molecular weights.

Animals↗
PubMed1982

Arginase as an inhibitory principle in liver plasma membranes arresting the growth of various mammalian cells in vitro.

Plasma membranes prepared from rat livers inhibited the in vitro growth of various mammalian cells including hepatoma cells in a concentration-dependent manner, showing almost complete arrest of cell growth at 0.1 mg protein/ml. Some of these cells tested, i.e., leukemia (L1210 and P388) and myeloma (P3-NS-1/1-Ag4-1) cells, were labile in the presence of plasma membranes (losing the viability), and CHO (Chinese hamster ovary) cells became round without detaching from the substratum. The culture medium preincubated with liver plasma membranes no longer supported the growth of hepatoma cells (AHI3 and AH66F). However, the 'conditioned' medium supplemented with L-arginine, supported the growth of the cells. Moreover, the addition of L-ornithine to the cultures containing plasma membranes markedly reduced the inhibitory effect of plasma membranes. The plasma membrane preparations were found to possess considerable arginase activity. There results seem to indicate the possible involvement of arginase in the inhibition of cell growth by liver plasma membranes.

Animals↗
PubMed1981

Dynamics of calmodulin and cyclic AMP phosphodiesterase in plasma membranes of rat livers and ascites hepatomas.

1. Plasma membranes from ascites hepatoma cells (AH-7974, AH-130) contained much smaller amounts of calmodulin (about half) and cyclic AMP phosphodiesterase (about one-third) compared to plasma membranes of rat livers. 2. Some of calmodulin molecules in liver plasma membranes were released by repeated washing. The 'washed' liver plasma membranes showed the presence of specific binding sites for externally added calmodulin molecules (bovine brain) (N = 140 pmol/mg protein, Kd = 7.9 . 10(-8) M). The calmodulin content of AH-7974 plasma membranes was not reduced by repeated washing. The binding of calmodulin to the 'washed' AH-7974 plasma membranes was only of nonspecific nature with negative cooperativity. 3. Plasma membranes (liver and AH-7974) appeared to contain both calmodulin-dependent and calmodulin-independent phosphodiesterase, but the stimulation by externally added Ca2+ plus calmodulin was rather small. Externally added calmodulin-dependent phosphodiesterase (bovine brain) was bound more to 'washed' liver plasma membranes than to 'washed' AH-7974 plasma membranes. Newly bound phosphodiesterase appeared to be more sensitive to the stimulation by Ca2+ plus calmodulin in 'washed' hepatoma plasma membranes than in 'washed' liver plasma membranes. 4. Preincubation of 'washed' plasma membranes (liver and hepatoma) with calmodulin did not affect the binding of phosphodiesterase, but the sensitivity of phosphodiesterase to the stimulation by Ca2+ plus calmodulin in hepatoma plasma membranes was lost.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1981

Liver plasma membranes and proteoglycan prepared therefrom inhibit the growth of hepatoma cells in vitro.

1. Plasma membranes from rat liver or kidney inhibited the growth of hepatoma (AH-130) cells in vitro. AH-130 plasma membranes or erythrocyte ghosts inhibited the growth of AH-130 cells less effectively. The inhibitory activity of liver plasma membranes was lost by heat treatment, or mild protease (papain or bromelin, but not trypsin or pronase) treatment, whereas it was retained after sialidase treatment of delipidation by ethanol/ether. 2. Proteoglycan (proteoheparan sulfate) prepared from liver plasma membranes inhibited the growth of AH-130 cells, but heparan sulfate was less active. The inhibitory activity of liver plasma membranes seemed, however, not to be ascribable solely to proteoheparan sulfate associated with plasma membranes. 3. Preliminary investigation suggested that the molecular weight 40 000 component may be a major inhibitory principle in liver plasma membranes.

Animals↗
PubMed1981

Effects of deoxyribonuclease I and micrococcal nuclease on the release of dexamethasone-receptor complex from nuclei of sensitive and insensitive hepatoma cell lines.

(1) Fu5 cells were sensitive to the glucocorticoid inhibition of cell growth and the hormonal induction of tyrosine aminotransferase (but not fructose-1,6-bisphosphatase and glycogen synthase). AH-130 and AH-7974 cells were insensitive to both effects. (2) The release of [3H]dexamethasone radioactivity from the nuclei of Fu5 and AH-130 cells preincubated with [3H]dexamethasone increased as the KCl concentration increased from 0 to 0.4 M, with no significant difference between the two cell lines. (3) The radioactivity was more sensitively released in Fu5 nuclei than in AH-130 nuclei upon treatment with DNAase I. The release of radioactivity was always larger than the release of DNA in both cell nuclei. In contrast to DNAase I, micrococcal nuclease treatment did not show any difference between the two cell lines in the release of radioactivity from nuclei, always showing a release of radioactivity equal to that of DNA.

Animals↗