Rapid capping in α-spectrin-deficient MEL cells from mice afflicted with hereditary hemolytic anemia

Stephen C. Dahl, Roy W. Geib, Mary T. Fox, Michael Edidin, Daniel Branton

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

A spectrin-based membrane skeleton is important for the stability and organization of the erythrocyte. To study the role of spectrin in cells that possess complex cytoskeletons, we have generated α-spectrin-deficient erythroleukemia cell lines from sph/sph mice. These cells contain β- spectrin, but lack α-spectrin as determined by immunoblot and Northern blot analyses. The effects of α-spectrin deficiency are apparent in the cells' irregular shape and fragility in culture. Capping of membrane glycoproteins by fluorescent lectin or antibodies occurs more rapidly in sph/sph than in wild-type erythroleukemia cells, and the caps appear more concentrated. The data support the idea that spectrin plays an important role in organizing membrane structure and limiting the lateral mobility of integral membrane glycoproteins in cells other than mature erythrocytes.

Original languageEnglish (US)
Pages (from-to)1057-1065
Number of pages9
JournalJournal of Cell Biology
Volume125
Issue number5
DOIs
StatePublished - Jun 1 1994

ASJC Scopus subject areas

  • Cell Biology

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