ArticleThe Journal of cell biology1983
Avian lens spectrin: subunit composition compared with erythrocyte and brain spectrin.
Article in The Journal of cell biology, 1983. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 44 citations in OpenAlex.
- Tropomodulin1 is required for membrane skeleton organization and hexagonal geometry of fiber cells in the mouse lens.The Journal of cell biology · 2009Article
- Golgi spectrin: identification of an erythroid beta-spectrin homolog associated with the Golgi complex.The Journal of cell biology · 1994Article
- Dynamics of membrane-skeleton (fodrin) organization during development of polarity in Madin-Darby canine kidney epithelial cells.The Journal of cell biology · 1986Article
- Sequencing of the chicken non-erythroid spectrin cDNA reveals an internal repetitive structure homologous to the human erythrocyte spectrin.The EMBO journal · 1985Article
- A possible mechanism of morphometric changes in dendritic spines induced by stimulation.Cellular and molecular neurobiology · 1985Review
- Posttranslational control of membrane-skeleton (ankyrin and alpha beta-spectrin) assembly in early myogenesis.The Journal of cell biology · 1985Article
- Tissue-specific expression of distinct spectrin and ankyrin transcripts in erythroid and nonerythroid cells.The Journal of cell biology · 1985Article
- Expression of the intermediate-filament-associated protein synemin in chicken lens cells.Molecular and cellular biology · 1984Article
- Goblin (ankyrin) in striated muscle: identification of the potential membrane receptor for erythroid spectrin in muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 1984Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chicken lens spectrin is composed predominantly of equimolar amounts of two polypeptides with solubility properties similar, but not identical, to erythrocyte spectrin. The larger polypeptide, Mr 240,000 (lens alpha-spectrin), co-migrates with erythrocyte and brain alpha-spectrin on one- and two-dimensional SDS polyacrylamide gels and cross-reacts with antibodies specific for chicken erythrocyte alpha-spectrin; the smaller polypeptide, Mr 235,000 (lens gamma-spectrin), co-migrates with brain gamma-spectrin and does not cross-react with either the alpha-spectrin antibodies specific for chicken erythrocyte beta-spectrin. Minor amounts of polypeptides antigenically related to erythrocyte beta-spectrin with a greater electrophoretic mobility than lens gamma-spectrin are also detected in lens. The equimolar ratio of lens alpha- and gamma-spectrin is invariantly maintained during the extraction of lens plasma membranes under different conditions, or after immunoprecipitation of whole extracts of lens with erythrocyte alpha-spectrin antibodies. Two-dimensional peptide mapping reveals that whereas alpha-spectrins from chicken erythrocytes, brain, and lens are highly homologous, the gamma-spectrins, although related, have some cell-type-specific peptides and are substantially different from erythrocyte beta-spectrin. Thus, the expression of cell-type-specific gamma- and beta-spectrins may be the basis for the assembly of a spectrin-plasma membrane complex whose molecular composition is tailored to the functional requirements of the particular cell-type.
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Registered trials
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