Study on the change of lung lamellar body to lattice tubular myelin by N-acetylglucosaminidase with special reference to membrane components and calcium.
The possibility of a role of N-acetylglucosaminidase or beta-galactosidase in the morphological change of lung lamellar body to lattice tubular myelin was examined in an in vitro incubation study. Electron microscopic observation of the incubation product and gas-chromatographic analysis of released sugars during incubation were used to understand the mechanism of these enzymes in the change of membrane constitution. N-acetylglucosaminidase proved to play a role in developing membrane of lamellar body toward lattice tubular structure with the support of Ca++. In this process, inositol release was indispensable in the modulation of membrane as well as the release of a small amount of N-acetylglucosamine. However, further reaction of this enzyme caused destruction or fusion of lattice-tubular integration with the release of other membrane components. Beta-galactosidase played no role in this process.
Kishikawa
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WHO Collaborating Center for Research and Training in Diagnostic Electron Microscopy, Nippon Medical School, Tokyo, Japan.
D000118:Acetylglucosaminidase / Q000378:metabolism*; D000818:Animals; D001688:Biological Products; D002118:Calcium / Q000378:metabolism*; D007294:Inositol / Q000378:metabolism; D008168:Lung / Q000378:metabolism* / Q000648:ultrastructure; D008297:Male; D009186:Myelin Sheath; D011506:Proteins; D011663:Pulmonary Surfactants / Q000096:biosynthesis*; D051381:Rats; D017207:Rats, Sprague-Dawley; D013347:Subcellular Fractions / Q000378:metabolism / Q000648:ultrastructure
D001688:Biological Products; D011506:Proteins; D011663:Pulmonary Surfactants; C018167:tubular myelin; D007294:Inositol; D000118:Acetylglucosaminidase; D002118:Calcium