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Mutants of Polysphondylium pallidum altered in cell aggregation and in the expression of a carbohydrate epitope on cell surface glycoproteins
Francis, D., Toda, K., Merkl, Rainer, Hatfield, T. and Gerisch, G. (1985) Mutants of Polysphondylium pallidum altered in cell aggregation and in the expression of a carbohydrate epitope on cell surface glycoproteins. EMBO Journal 4 (10), pp. 2525-2532.Date of publication of this fulltext: 16 Nov 2009 09:11
Article
DOI to cite this document: 10.5283/epub.10909
Abstract
Mutants of the cellular slime mold Polysphondylium pallidum have been selected using a cell sorter and a fluorescentlabeled monoclonal antibody, mAb 293. This antibody blocks cell adhesion when applied as Fab, and recognizes a carbohydrate epitope containing L-fucose. This epitope is expressed on the cell surface and is present on >10 membrane glycoproteins of different apparent mol. wts. Twenty ...
Mutants of the cellular slime mold Polysphondylium pallidum have been selected using a cell sorter and a fluorescentlabeled monoclonal antibody, mAb 293. This antibody blocks cell adhesion when applied as Fab, and recognizes a carbohydrate epitope containing L-fucose. This epitope is expressed on the cell surface and is present on >10 membrane glycoproteins of different apparent mol. wts. Twenty mutants were obtained which did not bind mAb 293 when tested at 2 h of starvation. After longer periods of starvation the epitope became detectable in the mutants. In all these mutants aggregation patterns were atypical. Generally streams of cells that were radially orientated around aggregation centers were missing or were much shorter than in wild-type. Genetic analysis demonstrated that aberrant aggregation was linked to the alteration in carbohydrate epitope expression. One mutant was unstable and gave rise to subclones in which almost no antibody binding was observed, even after 24 h of starvation, and only few aggregation centers with no streams or very short ones were formed. These results indicate that the capability of the cells to aggregate is correlated with the exposure on their surfaces of the carbohydrate epitope recognized by mAb 293, whose function in development remains to be established.
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| Item type | Article | ||||
| Journal or Publication Title | EMBO Journal | ||||
| Volume: | 4 | ||||
|---|---|---|---|---|---|
| Number of Issue or Book Chapter: | 10 | ||||
| Page Range: | pp. 2525-2532 | ||||
| Date | 1985 | ||||
| Institutions | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Rainer Merkl | ||||
| Identification Number |
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| Dewey Decimal Classification | 500 Science > 570 Life sciences | ||||
| Status | Published | ||||
| Refereed | Yes, this version has been refereed | ||||
| Created at the University of Regensburg | No | ||||
| URN of the UB Regensburg | urn:nbn:de:bvb:355-epub-109091 | ||||
| Item ID | 10909 |
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