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Biomedical subjects

H N Fukui

Publications and source records attributed to H N Fukui.

15 recordsLinked to original sources

Corneal re-epithelialization in galactosemic rats.

Abnormalities in corneal epithelial healing in diabetic patients have been described recently. Defects in corneal re-epithelialization in diabetic rats have been reported, and it was found that treatment with aldose reductase (AR) inhibitors effectively prevented these defects. Experiments using galactosemic rats to study further the role of AR in these defects, since AR is known to be the common factor involved in sugar cataractogeneses, are reported herein. Similar defects in corneal re-epithelialization in galactosemic rats as in diabetic rats were found. The delay in re-epithelialization was documented by computer planimetry. Light microscopy showed marked corneal stroma edema and wider intercellular spaces in the epithelium after complete re-epithelialization, while scanning electron microscopy revealed fewer filopodia projecting from the leading margin during the active migration stage. These defects were prevented by treating galactosemic rats with the aldose reductase inhibitor, Pfizer's Sorbinil. These suggest that AR plays a role in the defects in corneal re-epithelialization observed in diabetes.

Animals↗

Differential metabolism and leakage of protein in an inherited cataract and a normal lens cultured with ouabain.

Ocular lenses in Nakano mice showed marked changes in synthesis, degradation and leakage of protein during cataractogenesis. The cataract-associated changes included the differential lowering of crystallin synthesis, the cleavage of crystallin polypeptides to lower molecular weight forms and the leakage of crystallins from cultured lenses. Ouabain treatment of normal lenses induced these alterations, suggesting that changes in the intracellular levels of Na+ and K+ affect the anabolism and catabolism of protein during cataract formation.

Animals↗

Tissue culture of lens epithelial cells from normal and Nakano mice.

Lens epithelial cells from normal and Nakano adult mice have been cultured for over 1 year, and the cells have retained certain differentiated characteristics. Fluorescent antibody to mouse gamma crystallin reacted with the spherical lentoid bodies which appeared approximately 2 weeks after the start of the culture. The lentoid bodies also contained cells which had few cell organelles and homogenous cytoplasms. Both gamma crystallin production and loss of cellular organelles are characteristics of differentiated fiber cells rather than epithelial cells. An inhibitor of the Na-K ATPase is responsible for the hydration and subsequent cataract formation in the Nakamo mouse. The inhibitor of the Na-K ATPase was demonstrated in the lens in culture from the Nakamo mice, but no inhibitory activity was detected in the cultures from normal mice.

Adenosine Triphosphatases↗

Cataractogenic effects of a boron hydride disulfide compound.

The disulfide form but not the sulfhydryl form of a boron hydride compound was found to be cataractogenic. Apparently this compound attaches to the sulfhydryl group of Na-K ATPase in the lens epithelium inactivating this crucial enzyme. The consequence is that a defect in the cation pump activity arises, leading to a rapid influx of Na ions and loss of K ions and marked increase in hydration. These changes are thought to lead to opacification.

Acute Disease↗

Lens growth in the Nakano mouse.

The growth curve of the lens of the Nakano mouse was compared to that of the normal mouse. There was no obvious difference for the first two weeks of age. After this period the growth of the normal lens continued while that of Nakano mouse lens slowed abruptly and eventually ceased. Studies with labeled leucine, however, showed that even after the appearance of the "pin-head" opacity the protein synthesis, although depressed, continued. These findings combined with previous histological observations suggest that new fiber formation is probably unaffected in the early stages of the Nakano cataract. The apparent cessation of lens growth is probably associated with the extensive liquefaction that is observed to occur at the posterior nuclear region.

Aging↗