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Expression of SV2 in the Seveloping Chick Cerebellum: Comparison with Calbindin and AMPA Glutamate Receptors 2/3
Author(s) -
Grabs Detlev,
Escher Lukas,
Bergmann Mathias
Publication year - 2008
Publication title -
the anatomical record: advances in integrative anatomy and evolutionary biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.678
H-Index - 62
eISSN - 1932-8494
pISSN - 1932-8486
DOI - 10.1002/ar.20691
Subject(s) - cerebellum , calbindin , ampa receptor , synaptic vesicle , neuroscience , postsynaptic potential , biology , glutamate receptor , purkinje cell , microbiology and biotechnology , granular layer , chemistry , receptor , vesicle , biochemistry , membrane , immunohistochemistry , immunology
The well‐organized cerebellum is an ideal model to investigate the developmental appearance and localization of pre‐ and postsynaptic structures. One of the synaptic proteins abundant in the central nervous system and localized in presynaptic vesicle membranes is the synaptic vesicle protein 2 (SV2). SV2 was shown to be involved in priming and modulating synaptic vesicles and having an effect in epileptic diseases. So far there are no data available describing the developmental localization of this protein in the cerebellum. We followed the expression pattern of SV2 and compared it with the expression of the neuronal calcium‐binding protein Calbindin and the AMPA glutamate receptor subunits 2/3 (GluR 2/3), both shown to be early expressed in the developing chick cerebellum predominantly in Purkinje cells. We detected the expression of SV2 in presynaptic terminals (mainly from climbing and mossy fibers) as soon as they are formed at embryonic day 16 in the inner molecular layer. Purkinje cells express Calbindin and GluR 2/3 in the soma and postsynaptically in the primary dendrites at this stage. With ongoing development, the pattern of SV2 expression follows the development of Purkinje cell dendrites in the molecular layer, suggesting a synaptic refinement of labeled climbing and later parallel fibers. Anat Rec, 291:538–546, 2008. © 2008 Wiley‐Liss, Inc.