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Biomedical subjects

H Mishima

Publications and source records attributed to H Mishima.

At least 127 records · Page 7Linked to original sources
PubMed1988

Interactions of extracellular collagen and corneal fibroblasts: morphologic and biochemical changes of rabbit corneal cells cultured in a collagen matrix.

Corneal fibroblasts, also known as keratocytes are surrounded by an extracellular matrix of collagen in vivo. To understand the physiology and pathology of these corneal fibroblasts, it is important to study their interactions with this extracellular matrix. We cultured rabbit corneal fibroblasts on tissue culture plastic dishes or in a hydrated collagen gel and compared the changes in morphology and mitotic activity. Corneal fibroblasts on plastic dishes were flattened and widely spread, whereas those in collagen gel became spindle-shaped with long processes. Examination with an electron microscope revealed that the corneal fibroblasts in collagen gel formed gap junctions with neighboring cells. Gap junctions were hardly ever observed between corneal fibroblasts cultured on plastic dishes. Corneal fibroblasts cultured in a collagen matrix showed much less incorporation of [3H]thymidine than did corneal fibroblasts cultured on plastic, and this incorporation decreased with increasing concentration of collagen. Our present results suggest that the morphologic and biochemical characteristics of corneal fibroblasts cultured in collagen gel are different from those cultured on plastic.

Animals↗
PubMed1988

Changes in bovine dentin mineral with sodium hypochlorite treatment.

Dentin powders from bovine incisors were treated with 10% NaClO solution. Differential thermal analysis (DTA) indicated the removal of organic material from the dentin sample following the treatment, since the exothermic reaction at 320 degrees C had disappeared. X-ray diffraction studies revealed a change in the crystallinity of the dentin crystals and the formation of calcite after the treatment. Infrared absorption analysis showed that the band due to carbonate ions was weakened after the treatment, while atomic absorption spectroscopic analysis showed that magnesium ions had been dissolved from the dentin sample. The a-axis lengths of treated and heated dentin samples differed from those of untreated and heated samples. Whitlockite was always found in the untreated/heated samples, whereas it was absent in the treated/heated samples. The unit cell dimensions of the whitlockite indicated the partial substitution of magnesium for calcium. Magnesium ions seemed to be more effective than carbonate ions in forming whitlockite. These results showed that some magnesium and carbonate ions were removed from the dentin crystal structure upon NaClO treatment, while at the same time organic materials were removed from the dentin sample. It was suggested that crystals in the NaClO-treated dentin were similar to enamel crystals from a crystallographic viewpoint.

Animals↗
PubMed1988

Metabolism of drugs in the eye. Drug-reducing activity of preparations from bovine ciliary body.

Drug-metabolizing activities, especially the reductase activities towards N-oxide, hydroxamic acid, sulfoxide and nitro compounds were comparatively examined with bovine ciliary body. As described previously, the cytosol from the ocular tissue exhibits the nicotinamide N-oxide reductase activity when supplemented with 2-hydroxypyrimidine, an electron donor of aldehyde oxidase. When the cytosol was fractionated with ammonium sulfate, followed by assays of aldehyde oxidase and nicotinamide N-oxide reductase activities in each fraction, the distribution of aldehyde oxidase activity in the resultant ammonium sulfate fractions was nearly parallel to that of nicotinamide N-oxide reductase activity. Furthermore, reductase activities towards drugs such as sulfoxide, hydroxamic acid and nitro compounds were observed with the cytosol in the presence of 2-hydroxypyrimidine or N1-methylnicotinamide. In general, these reductase activities of the fraction were markedly inhibited by menadione, an inhibitor of aldehyde oxidase. These results suggest that aldehyde oxidase present in ciliary body plays an important role in the reduction of a variety of xenobiotics in mammalian eyes. However, in the case of imipramine N-oxide, its reduction in the ocular tissue appears to be more readily catalyzed by a menadione-linked enzyme different from aldehyde oxidase.

Aldehyde Oxidoreductases↗
PubMed1988

Ocular pigmentation and intraocular pressure response to forskolin.

We studied the effects of a forskolin suspension on intraocular pressure (IOP) in normal albino and pigmented rabbits and in alpha-chymotrypsin induced ocular hypertensive rabbits. Experimental-induced ocular hypertensive rabbits were produced by injecting of alpha-chymotrypsin (167 units) into the posterior chamber of the eye of albino rabbits. Ocular hypertensive rabbits were classified into 3 groups according to the IOP (Group A; 15-19 mmHg, B; 20-24 mmHg, C; 25-29 mmHg). Topical application of 1% forskolin caused a significant decrease in IOP in Groups B and C, as well as in normal albino and pigmented rabbits. The hypotensive effects were lower in pigmented rabbits than in albino rabbits, although the duration was longer. Subconjunctival injection of 1% forskolin reduced IOP 1 to 5 hrs after treatment in albino rabbits. However, in pigmented rabbits, a slight increase in IOP was observed at 30 min, followed by a significant decrease 5 to 10 hrs after injection. Furthermore, the binding ability of forskolin to melanin granules was determined in vitro. Forskolin exhibited specific affinity towards melanin granules obtained from bovine eyes, with the binding reaching a plateau after 5 min of incubation.

Albinism↗
PubMed1988

Localization of fibronectin and actin in cultured rabbit keratocytes.

Migration of activated keratocytes toward the corneal stromal wound is one of the most important processes of successful healing. To understand the motility of keratocytes and the interaction of fibronectin and intracellular actin filaments, we cultured rabbit corneal keratocytes and studied dynamic movements of the cells by time-lapse cinematography. We also examined the changes in the localization of fibronectin and actin using double staining immunofluorescent microscopy. The cultured keratocytes first attached to the substratum in round globular shape and then spread with many extending processes. In the early stage of the cultivation, fibronectin was observed inside the cells. Later, fibronectin was observed outside the cells, suggesting formation of the extracellular matrix. When keratocytes spread, actin was observed as a stress fiber inside the cells. At the edge of the cellular processes, a close interaction between fibronectin and actin was observed. The present results demonstrated that cultured keratocytes had active motility and that there were close interactions between the extracellular fibronectin and intracellular actin filaments. The organization of fibrillar actin filaments (F-actin) might be affected by the binding of extracellular fibronectin to the cell surface receptor for fibronectin.

Actins↗
PubMed1987

Nicotinamide N-oxide reductase activity in bovine and rabbit eyes.

The nicotinamide N-oxide reductase activity of a variety of ocular tissues was investigated. The 9,000g supernatant of ciliary body, retinal pigment epithelium-choroid, iris, retina and cornea, but not lens, exhibited reductase activity under anaerobic conditions when supplemented with 2-hydroxypyrimidine, an electron donor of aldehyde oxidase. Among these tissues, the highest activity was observed with ciliary body. When the 9,000g supernatant of ciliary body was fractionated, the 2-hydroxypyrimidine-linked reductase activity was mainly associated with the cytosolic fraction and was markedly inhibited by menadione, an inhibitor of aldehyde oxidase. Similarly, in the presence of 2-hydroxypyrimidine, the cytosolic fraction of rabbit ciliary body exhibited nicotinamide N-oxide reductase activity which was susceptible to inhibition by menadione. These facts strongly suggest that aldehyde oxidase present in mammalian eyes is involved in the reduction of nicotinamide N-oxide to nicotinamide.

Aldehyde Oxidase↗