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Journal of Neuroscience, Vol 7, 3907-3914, Copyright © 1987 by Society for Neuroscience


ARTICLE

Amelin: a 4.1-related spectrin-binding protein found in neuronal cell bodies and dendrites

KE Krebs, IS Zagon and SR Goodman
Department of Physiology, Milton S. Hershey Medical Center, Pennsylvania State University, Hershey 17033.

An immunoreactive, structural, and functional analog of erythrocyte protein 4.1 is present in neuronal cell bodies and dendrites. Other investigators have described the isolation of a 4.1 analog in brain with structural characteristics suggesting that its identity was synapsin I, a neuronal phosphoprotein localized in the presynaptic terminal in association with small synaptic vesicles. In this report we demonstrate that the cell body/dendritic form of brain protein 4.1, which we have named amelin, is distinct from that of synapsin I on the basis of subcellular localization, migration in 2-dimensional gel electrophoresis, and structural criteria. We also demonstrate that amelin, like synapsin I, can bind brain spectrin on nitrocellulose paper. Neither amelin nor synapsin I binds calmodulin, as determined by a blot binding assay. We hypothesize that there exists in brain a family of 4.1-related proteins with distinct subcellular localization and function.


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M. Parra, P. Gascard, L. D. Walensky, J. A. Gimm, S. Blackshaw, N. Chan, Y. Takakuwa, T. Berger, G. Lee, J. A. Chasis, et al.
Molecular and Functional Characterization of Protein 4.1B, a Novel Member of the Protein 4.1 Family with High Level, Focal Expression in Brain
J. Biol. Chem., February 4, 2000; 275(5): 3247 - 3255.
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