Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 17 June 1983:
Vol. 220. no. 4603, pp. 1295 - 1296
DOI: 10.1126/science.6190228
Prev | Table of Contents | Next

Articles

Science, Vol 220, Issue 4603, 1295-1296
Copyright © 1983 by American Association for the Advancement of Science

articles

Erythrocyte and brain forms of spectrin in cerebellum: distinct membrane-cytoskeletal domains in neurons

E Lazarides and WJ Nelson

Chicken cerebellum expresses a polypeptide antigenically and biochemically related to the alpha subunit of spectrin, an erythrocyte membrane-cytoskeletal protein. Most of this polypeptide is associated with a brain specific spectrin subunit, gamma-spectrin, and is localized in virtually all neuronal cell bodies and processes. Cerebellum also expresses polypeptides antigenically related to the beta subunits of erythrocyte spectrin and these are also found in association with cerebellar alpha-spectrin but are confined to the plasmalemma of the neuronal cell bodies. This suggests that there is a mechanism for segregating different spectrin complexes into distinct membrane domains within a single cell.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Rescue of Ca2+ overload-induced left ventriclur dysfunction by targeted ablation of phospholamban.
T. Tsuji, F. del Monte, Y. Yoshikawa, T. Abe, J. Shimizu, C. Nakajima-Takenaka, S. Taniguchi, R. J. Hajjar, and M. Takaki (2009)
Am J Physiol Heart Circ Physiol 296, H310-H317
   Abstract »    Full Text »    PDF »
Calpain inhibitor-1 protects the rat heart from ischemia-reperfusion injury: analysis by mechanical work and energetics.
Y. Yoshikawa, H. Hagihara, Y. Ohga, C. Nakajima-Takenaka, K.-y. Murata, S. Taniguchi, and M. Takaki (2005)
Am J Physiol Heart Circ Physiol 288, H1690-H1698
   Abstract »    Full Text »    PDF »
Golgi Localization of Syne-1.
L. L. Gough, J. Fan, S. Chu, S. Winnick, and K. A. Beck (2003)
Mol. Biol. Cell 14, 2410-2424
   Abstract »    Full Text »    PDF »
Rat cardiac contractile dysfunction induced by Ca2+ overload: possible link to the proteolysis of {alpha}-fodrin.
T. Tsuji, Y. Ohga, Y. Yoshikawa, S. Sakata, T. Abe, N. Tabayashi, S. Kobayashi, H. Kohzuki, K.-I. Yoshida, H. Suga, et al. (2001)
Am J Physiol Heart Circ Physiol 281, H1286-H1294
   Abstract »    Full Text »    PDF »
Segregation of Two Spectrin Isoforms: Polarized Membrane-binding Sites Direct Polarized Membrane Skeleton Assembly.
R. R. Dubreuil, P. B. Maddux, T. A. Grushko, and G. R. Macvicar (1997)
Mol. Biol. Cell 8, 1933-1942
   Abstract »    Full Text »
Golgi membrane skeleton: identification, localization and oligomerization of a 195 kDa ankyrin isoform associated with the Golgi complex.
K. Beck, J. Buchanan, and W. Nelson (1997)
J. Cell Sci. 110, 1239-1249
   Abstract »    PDF »
Reperfusion of Rat Heart After Brief Ischemia Induces Proteolysis of Calspectin (Nonerythroid Spectrin or Fodrin) by Calpain.
K.-i. Yoshida, M. Inui, K. Harada, T. C. Saido, Y. Sorimachi, T. Ishihara, S.-i. Kawashima, and K. Sobue (1995)
Circ. Res. 77, 603-610
   Abstract »    Full Text »
The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons.
F Malchiodi-Albedi, M Ceccarini, J. Winkelmann, J. Morrow, and T. Petrucci (1993)
J. Cell Sci. 106, 67-78
   Abstract »    PDF »
Immunological approaches to the nervous system.
L. Reichardt (1984)
Science 225, 1294-1299
   Abstract »    PDF »
Erythrocyte form of spectrin in cerebellum: appearance at a specific stage in the terminal differentiation of neurons.
E Lazarides and W. Nelson (1983)
Science 222, 931-933
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)