Evidence that insulin causes translocation of glucose transport activity to the plasma membrane from an intracellular storage site.
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<jats:p>The glucose transport activity of fat cells was assayed in a cell-free system. The activity was solubilized and incorporated into egg-lecithin liposomes. The carrier-mediated glucose transport activity was estimated by subtracting the cytochalasin B-insensitive component from the total glucose uptake activity of the modified liposomes. When a crude microsomal preparation from fat cells was fractionated by sucrose density gradient centrifugation, two transport activities (peaks A and B) were separated. Peak A coincided with the peak of 5'-nucleotidase, a marker of the plasma membrane. Peak B appeared to coincide with the peak of UDPGal:N-acetylglucosamine galactosyltransferase, a marker of the Golgi apparatus. Peak A was considerably smaller than peak B under basal conditions. When cells were exposed to 1 nM insulin for 5 min before homogenization, the height of peak A increased whereas that of peak B decreased. Insulin had no significant effect on the galactosyltransferase activity. The Km values of glucose transport facilitated by the activities in peaks A and B were both approximately 10-15 mM. These results imply that insulin facilitates translocation of the transport activity from an intracellular storage site to the plasma membrane.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 77 (5), 2542-2545, 1980-05
Proceedings of the National Academy of Sciences
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詳細情報 詳細情報について
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- CRID
- 1363388844992670720
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- NII論文ID
- 80000545853
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- ISSN
- 10916490
- 00278424
- http://id.crossref.org/issn/00278424
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