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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hu, R. J. Bennett, V. Moorthy, S. |
| Description | Author Affiliation: Hu RJ ( Howard Hughes Medical Institute, Duke University School of Medicine, Durham, North Carolina 27710.) |
| Abstract | Spectrin is a major structural protein associated with the cytoplasmic surface of plasma membranes of many types of cells. To study the functions of spectrin, we transfected Caco-2 intestinal epithelial cells with a plasmid conferring neomycin resistance and encoding either actin-binding or ankyrin-binding domains of beta G-spectrin fused with beta-galactosidase. These polypeptides, in principle, could interfere with the interaction of spectrin with actin or ankyrin, as well as block normal assembly of alpha- and beta-spectrin subunits. Cells expressing the fusion proteins represented only a small fraction of neomycin-resistant cells, but they could be detected based on expression of beta-galactosidase. Cells expressing spectrin domains exhibited a progressive decrease in amounts of endogenous beta G- spectrin, although alpha-spectrin was still present. Beta G-spectrin- deficient cells lost epithelial cell morphology, became multinucleated, and eventually disappeared after 10-14 d in culture. Spectrin- associated membrane proteins, ankyrin and adducin, as well as the Na+,K(+)-ATPase, which binds to ankyrin, exhibited altered distributions in cells transfected with beta G-spectrin domains. E- cadherin and F-actin, in contrast to ankyrin, adducin, and the Na+,K(+)- ATPase, were expressed, and they exhibited unaltered distribution in beta G-spectrin-deficient cells. Cells transfected with the same plasmid encoding beta-galactosidase alone survived in culture as the major population of neomycin-resistant cells, and they exhibited no change in morphology or in the distribution of spectrin-associated membrane proteins. These results establish that beta G-spectrin is essential for the normal morphology of epithelial cells, as well as for their maintenance in monolayer culture. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 6 |
| Volume Number | 128 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1995-03-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Epithelial Cells Giant Cells Metabolism Spectrin Biosynthesis Ankyrins Genetics Cell Death Cells, Cultured Epithelium Gene Transfer Techniques Intestines Microfilament Proteins Recombinant Fusion Proteins Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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