The ultrastructural localization of calcium‐activated protease “calpain” in rat brain
作者:
Lynn S. Perlmutter,
Robert Siman,
Christine Gall,
Peter Seubert,
Michel Baudry,
Gary Lynch,
期刊:
Synapse
(WILEY Available online 1988)
卷期:
Volume 2,
issue 1
页码: 79-88
ISSN:0887-4476
年代: 1988
DOI:10.1002/syn.890020111
出版商: Wiley Subscription Services, Inc., A Wiley Company
关键词: Cytoskeleton;Immuno‐electron microscopy;Synaptic plasticity
数据来源: WILEY
摘要:
AbstractCalpain I, a calcium‐activated neutral protease which degrades a number of cytoskeletal proteins, has been implicated in the rapid turnover of structural proteins that may participate in synaptic plasticity. In the present study, an antibody raised against purified erythrocyte calpain I was biochemically characterized and demonstrated to specifically bind the Mr=80,000 subunit of both rat erythrocyte and brain calpain I. This antibody was used to examine the cellular distribution of calpain I at the electron microscopic level in rat brain and spinal cord using the avidin‐biotin immunocytochemical technique. Reaction product was observed throughout neuronal perikarya, within both axonal and dendritic processes, and within spine heads and necks. Postsynaptic densities in both shaft and spine synapses were also immunoreactive. Glial cell bodies and processes were densely stained. In both neurons and glia, the reaction product was deposited along cytoskeletal elements. The localization of calpain I immunoreactivity to glial processes suggests this degradative enzyme may play a role in the glial hypertrophy and process retraction seen in brain. The presence of the enzyme in spines and postsynaptic densities is consistent with the hypothesis that it is involved in the turnover of synaptic cytoskeleton, thus providing a means through which transient physiological events effect lasting changes in the chemistry and morphology of spi
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