Abstract
The smooth endoplasmic reticulum (SER) has been established as an intracellular calcium storage site in neurons. Although the SER appears to form a continuous membrane system within neurons, immunolocalization studies suggest that calcium regulatory proteins are not evenly distributed within the SER but are selectively concentrated or excluded from certain domains. The subcompartmenalization of the SER has been clearly demonstrated in Purkinje neurons where two proteins involved in the release of calcium from intracellular stores, the IP3 and ryanodine receptor, were differentially localized within dendrites. Both proteins were found associated with the SER in cell bodies and dendrites of chick Purkinje neurons but only labeling for the IP3 receptor was found within dendritic spines. A similar differential localization was described in Purkinje cell dendrites for the SER Ca++ATPase and calsequestrin, a lumenal calcium binding protein. The Ca++ATPase was found throughout dendrites and dendritic spines while calsequestrin was restricted to membranous profiles within the dendritic shaft.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Proceedings, annual meeting, Electron Microscopy Society of America
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
