Brain spectrin( 240 235) and brain spectrin( 240 235E)

Conservation of structure and location within mammalian neural tissue

Beat M. Riederer, Lori L. Lopresti, Keith E. Krebs, Ian S. Zagon, Steven Goodman

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

We demonstrate that the brain spectrin isoforms (240/235) and (240/235E) are present in all mammalian species studied (human, bovine, mouse, and rat). Immunohistochemistry with a panel of eleven polyclonal antibodies have indicated an identical localization of the brain spectrin isoforms in all mammalian species. Brain spectrin( 240 235) is found primarily in axons, and brain spectrin(240/235E) primarily in cell bodies and dendrites. Immunoprecipitation and Western blotting studies have indicated that the subunit molecular weights of brain spectin( 240 235) and ( 240 235E) are identical in all mammalian species. We demonstrate that when proteolysis is not completely blocked during immunoprecipitation studies, the 235 kDa subunits are converted to a 230 kDa polypeptide [brain spectrin( 240 235)] and a 232 kDa polypeptide [brain spectrin( 240 235E)]. Finally, we show that both the α and β subunits of brain spectrin(240/235) and brain spectrin(240/235E) are antigenically distinct in every species examined. These studies indicate that previous findings on the structure, location, and function of mouse brain spectrin isoforms can now be generalized to all mammalian species.

Original languageEnglish (US)
Pages (from-to)607-616
Number of pages10
JournalBrain Research Bulletin
Volume21
Issue number4
DOIs
StatePublished - Jan 1 1988
Externally publishedYes

Fingerprint

Spectrin
Brain
Protein Isoforms
Immunoprecipitation
Peptides
Dendrites
Proteolysis

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

Cite this

Brain spectrin( 240 235) and brain spectrin( 240 235E) : Conservation of structure and location within mammalian neural tissue. / Riederer, Beat M.; Lopresti, Lori L.; Krebs, Keith E.; Zagon, Ian S.; Goodman, Steven.

In: Brain Research Bulletin, Vol. 21, No. 4, 01.01.1988, p. 607-616.

Research output: Contribution to journalArticle

Riederer, Beat M. ; Lopresti, Lori L. ; Krebs, Keith E. ; Zagon, Ian S. ; Goodman, Steven. / Brain spectrin( 240 235) and brain spectrin( 240 235E) : Conservation of structure and location within mammalian neural tissue. In: Brain Research Bulletin. 1988 ; Vol. 21, No. 4. pp. 607-616.
@article{980f08eaea11476596c1411c6fd4e671,
title = "Brain spectrin( 240 235) and brain spectrin( 240 235E): Conservation of structure and location within mammalian neural tissue",
abstract = "We demonstrate that the brain spectrin isoforms (240/235) and (240/235E) are present in all mammalian species studied (human, bovine, mouse, and rat). Immunohistochemistry with a panel of eleven polyclonal antibodies have indicated an identical localization of the brain spectrin isoforms in all mammalian species. Brain spectrin( 240 235) is found primarily in axons, and brain spectrin(240/235E) primarily in cell bodies and dendrites. Immunoprecipitation and Western blotting studies have indicated that the subunit molecular weights of brain spectin( 240 235) and ( 240 235E) are identical in all mammalian species. We demonstrate that when proteolysis is not completely blocked during immunoprecipitation studies, the 235 kDa subunits are converted to a 230 kDa polypeptide [brain spectrin( 240 235)] and a 232 kDa polypeptide [brain spectrin( 240 235E)]. Finally, we show that both the α and β subunits of brain spectrin(240/235) and brain spectrin(240/235E) are antigenically distinct in every species examined. These studies indicate that previous findings on the structure, location, and function of mouse brain spectrin isoforms can now be generalized to all mammalian species.",
author = "Riederer, {Beat M.} and Lopresti, {Lori L.} and Krebs, {Keith E.} and Zagon, {Ian S.} and Steven Goodman",
year = "1988",
month = "1",
day = "1",
doi = "10.1016/0361-9230(88)90200-6",
language = "English (US)",
volume = "21",
pages = "607--616",
journal = "Brain Research Bulletin",
issn = "0361-9230",
publisher = "Elsevier Inc.",
number = "4",

}

TY - JOUR

T1 - Brain spectrin( 240 235) and brain spectrin( 240 235E)

T2 - Conservation of structure and location within mammalian neural tissue

AU - Riederer, Beat M.

AU - Lopresti, Lori L.

AU - Krebs, Keith E.

AU - Zagon, Ian S.

AU - Goodman, Steven

PY - 1988/1/1

Y1 - 1988/1/1

N2 - We demonstrate that the brain spectrin isoforms (240/235) and (240/235E) are present in all mammalian species studied (human, bovine, mouse, and rat). Immunohistochemistry with a panel of eleven polyclonal antibodies have indicated an identical localization of the brain spectrin isoforms in all mammalian species. Brain spectrin( 240 235) is found primarily in axons, and brain spectrin(240/235E) primarily in cell bodies and dendrites. Immunoprecipitation and Western blotting studies have indicated that the subunit molecular weights of brain spectin( 240 235) and ( 240 235E) are identical in all mammalian species. We demonstrate that when proteolysis is not completely blocked during immunoprecipitation studies, the 235 kDa subunits are converted to a 230 kDa polypeptide [brain spectrin( 240 235)] and a 232 kDa polypeptide [brain spectrin( 240 235E)]. Finally, we show that both the α and β subunits of brain spectrin(240/235) and brain spectrin(240/235E) are antigenically distinct in every species examined. These studies indicate that previous findings on the structure, location, and function of mouse brain spectrin isoforms can now be generalized to all mammalian species.

AB - We demonstrate that the brain spectrin isoforms (240/235) and (240/235E) are present in all mammalian species studied (human, bovine, mouse, and rat). Immunohistochemistry with a panel of eleven polyclonal antibodies have indicated an identical localization of the brain spectrin isoforms in all mammalian species. Brain spectrin( 240 235) is found primarily in axons, and brain spectrin(240/235E) primarily in cell bodies and dendrites. Immunoprecipitation and Western blotting studies have indicated that the subunit molecular weights of brain spectin( 240 235) and ( 240 235E) are identical in all mammalian species. We demonstrate that when proteolysis is not completely blocked during immunoprecipitation studies, the 235 kDa subunits are converted to a 230 kDa polypeptide [brain spectrin( 240 235)] and a 232 kDa polypeptide [brain spectrin( 240 235E)]. Finally, we show that both the α and β subunits of brain spectrin(240/235) and brain spectrin(240/235E) are antigenically distinct in every species examined. These studies indicate that previous findings on the structure, location, and function of mouse brain spectrin isoforms can now be generalized to all mammalian species.

UR - http://www.scopus.com/inward/record.url?scp=0024157950&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024157950&partnerID=8YFLogxK

U2 - 10.1016/0361-9230(88)90200-6

DO - 10.1016/0361-9230(88)90200-6

M3 - Article

VL - 21

SP - 607

EP - 616

JO - Brain Research Bulletin

JF - Brain Research Bulletin

SN - 0361-9230

IS - 4

ER -