Literature DB >> 8366343

Postmitotic expression of ankyrinR and beta R-spectrin in discrete neuronal populations of the rat brain.

S Lambert1, V Bennett.   

Abstract

Isoforms of ankyrin (ankyrinR) are expressed in both the erythrocyte and the brain. Four cDNAs representing regulatory domains of ankyrinR expressed in the rat spleen and brain were cloned and sequenced. These different cDNAs were found to result from tissue-specific alternative mRNA processing of the ankyrinR regulatory domain. One of the isolated cDNAs was used to develop an antibody to brain isoforms of ankyrinR, and this antibody was used to study the localization of ankyrinR in the rat brain. The protein was found to be widely expressed in neurons of the metencephalon but limited to a discrete subset of neurons in the rat forebrain. In the thalamus and areas of the basal ganglia, these neurons were grouped in defined nuclei, whereas in the cortex, hippocampus, and caudate putamen they appeared as isolated cells distributed randomly throughout these structures. A similar study using an antibody raised against erythrocyte spectrin (beta R) showed a comparable localization to that of ankyrinR. Both proteins were expressed late in the developing rat brain, as part of the maturation stage of neural development. These data suggest a specific role for these erythrocyte structural proteins in the postmitotic development of a subset of neurons in the rat brain.

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Year:  1993        PMID: 8366343      PMCID: PMC6576446     

Source DB:  PubMed          Journal:  J Neurosci        ISSN: 0270-6474            Impact factor:   6.167


  17 in total

1.  βII-spectrin promotes mouse brain connectivity through stabilizing axonal plasma membranes and enabling axonal organelle transport.

Authors:  Damaris N Lorenzo; Alexandra Badea; Ruobo Zhou; Peter J Mohler; Xiaowei Zhuang; Vann Bennett
Journal:  Proc Natl Acad Sci U S A       Date:  2019-06-17       Impact factor: 11.205

Review 2.  Cargo hold and delivery: Ankyrins, spectrins, and their functional patterning of neurons.

Authors:  Damaris N Lorenzo
Journal:  Cytoskeleton (Hoboken)       Date:  2020-02-14

3.  Ankyrin gene mutations in japanese patients with hereditary spherocytosis.

Authors:  H Nakanishi; A Kanzaki; A Yawata; O Yamada; Y Yawata
Journal:  Int J Hematol       Date:  2001-01       Impact factor: 2.490

Review 4.  Anchoring skeletal muscle development and disease: the role of ankyrin repeat domain containing proteins in muscle physiology.

Authors:  Jin-Ming Tee; Maikel P Peppelenbosch
Journal:  Crit Rev Biochem Mol Biol       Date:  2010-08       Impact factor: 8.250

5.  Obscurin targets ankyrin-B and protein phosphatase 2A to the cardiac M-line.

Authors:  Shane R Cunha; Peter J Mohler
Journal:  J Biol Chem       Date:  2008-09-09       Impact factor: 5.157

6.  β-III-spectrin spinocerebellar ataxia type 5 mutation reveals a dominant cytoskeletal mechanism that underlies dendritic arborization.

Authors:  Adam W Avery; David D Thomas; Thomas S Hays
Journal:  Proc Natl Acad Sci U S A       Date:  2017-10-16       Impact factor: 11.205

7.  Non-erythroid beta spectrin interacting proteins and their effects on spectrin tetramerization.

Authors:  Akin Sevinc; Leslie W-M Fung
Journal:  Cell Mol Biol Lett       Date:  2011-08-24       Impact factor: 5.787

8.  Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle.

Authors:  D Zhou; C S Birkenmeier; M W Williams; J J Sharp; J E Barker; R J Bloch
Journal:  J Cell Biol       Date:  1997-02-10       Impact factor: 10.539

9.  Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain.

Authors:  L L Peters; K M John; F M Lu; E M Eicher; A Higgins; M Yialamas; L C Turtzo; A J Otsuka; S E Lux
Journal:  J Cell Biol       Date:  1995-07       Impact factor: 10.539

10.  Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons.

Authors:  Y Matsuoka; X Li; V Bennett
Journal:  J Cell Biol       Date:  1998-07-27       Impact factor: 10.539

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