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Y Urade

Publications and source records attributed to Y Urade.

132 records · Page 8Linked to original sources
PubMed1983

Induction of indoleamine 2,3-dioxygenase in alveolar interstitial cells of mouse lung by bacterial lipopolysaccharide.

The cellular localization of indoleamine 2,3-dioxygenase was studied in the mouse lung after induction by lipopolysaccharide treatment. No significant indoleamine 2,3-dioxygenase activity was detected in alveolar macrophages and type II epithelial cells, which were recovered by alveolar lavages and trypsin-treatment, respectively. To determine this enzyme activity in other types of lung cells, we prepared monodispersed lung cells (6.5 X 10(7) cells/lung) by incubation with 0.1% collagenase and 0.1% trypsin. In a Percoll isopycnic gradient, the dispersed cells were distributed with two peaks at the densities of 1.040 and 1.080 g/ml. The enzyme activity was recovered exclusively in the lighter fractions. As examined by electron microscopy or more quantitatively by using various marker enzyme activities, endothelial cells (angiotensin-converting enzyme as a marker enzyme of these cells), alveolar interstitial cells (prostaglandin dehydrogenase), type I epithelial cells, type II epithelial cells, alveolar macrophages (beta-glucuronidase), Clara cells (coumarin hydroxylase), and polymorphonuclear leucocytes (arylsulfatase) were distributed with peaks at the densities of 1.033, 1.040, 1.042, 1.045, 1.070, 1.082, and 1.093 g/ml, respectively. The distribution pattern of the indoleamine 2,3-dioxygenase activity exactly coincided with that of alveolar interstitial cells. The localization of this enzyme in alveolar interstitial cells was immunohistochemically confirmed with the anti-indoleamine 2,3-dioxygenase antibody.

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PubMed1979

Induction of indoleamine 2,3-dioxygenase in mouse lung during virus infection.

Indoleamine 2,3-dioxygenase [indoleamine: oxygen 2,3-oxidoreductase (decyclizing)] activity in the supernatant fraction (30,000 X g, 30 min) of mouse lung homogenate increased approximately 120-fold after infection with PR8 influenza virus. Both specific and total enzyme activities started to increase linearly from the 5th day after infection, reached the highest level around the 11th day, and then gradually decreased to normal values in about 3 weeks. Other enzymes in the lung, such as certain lysosomal enzymes and monoamine oxidase, did not change significantly throughout the experiments. The time course of the increase in the enzyme activity was quite different from that of virus replication in the lung (a peak by the 3rd day and persistence until the 9th day) or that of serum antibody content (started to rise on the 9th day). Rather, it appeared to be closely related to the infiltrations of mononuclear and lymphocytic cells. When mice were exposed to a higher dose of virus and did not recuperate, the time course of the increase of the enzyme activity was essentially identical to that seen with a low concentration of virus. A maximum stimulation of the enzyme activity in the lung occurred on the 9th day after infection; the increase was approximately 100-fold. However, serum antibody content was slight and virus titer in the lung remained high.

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PubMedDate not supplied

Stage and region-specific localization of lipocalin-type prostaglandin D synthase in the adult murine testis and epididymis.

Lipocalin-type prostaglandin D synthase in semen has been associated with male fertility, although this relationship is not well defined. To gain insight into potential mechanisms, the objective of the present study was to immunocytochemically localize lipocalin-type prostaglandin D synthase within the testis, efferent ducts, and 4 segments of mouse epididymis. In the testis, immunoperoxidase staining was localized within the Sertoli cells only at stages VI-VIII of the spermatogenic cycle, which is just prior to spermiation. Intense staining was also evident throughout the interstitial tissue, including Leydig cells. The entire epithelium of the efferent ducts, including ciliated and nonciliated cells, was immunoreactive. A distinct pattern of immunostaining for lipocalin-type prostaglandin D synthase was observed in different regions of epididymis, suggesting a possible role in sperm maturation. Staining for lipocalin-type prostaglandin D synthase was strikingly absent in the initial segment. In caput epididymidis, staining was evident throughout the cell cytoplasm of principal cells with some cells more intensely stained than adjacent ones. In the corpus region, overall staining intensity decreased and appeared to be concentrated in the apical region of principal cells, but some cells were completely unreactive. Reaction product in the cauda region was heavily concentrated on microvilli and within the epididymal lumen. In all epididymal regions, expression of lipocalin-type prostaglandin D synthase was specific to epithelial principal cells; no immunoreactivity was apparent in other cell types. The specific localization of lipocalin-type prostaglandin D synthase within the testicular interstitial tissue, Sertoli cells, and principal cells of caput epididymidis strongly suggests that this protein plays an integral role in both the development and maturation of sperm.

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