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Selective distribution of multiple protein kinase C isoforms in mouse cerebellar cortex
Author(s) -
Bareggi Renato,
Narducci Paola,
Grill Vittorio,
Lach Sonia,
Martelli Alberto M
Publication year - 1996
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/j.1768-322x.1996.tb00966.x
Subject(s) - biology , gene isoform , isozyme , cerebellar cortex , cerebellum , protein kinase c , polyclonal antibodies , signal transduction , microbiology and biotechnology , protein kinase a , purkinje cell , kinase , biochemistry , enzyme , neuroscience , antibody , immunology , gene
Summary— An immunohistochemical study concerning the distribution of protein kinase C isoforms, a lipid‐regulated serine/threonine kinase essential for signal transduction, was performed in mice cerebellar cortex, with particular emphasis on the localization of ‐ι and ‐λ isozymes. By the means of immunoblotting analyses we detected the presence of 11 PKC subspecies in whole cerebellar extracts. Immunoreactivity on cryostat sections revealed, using polyclonal and monoclonal antibodies, that a few isoforms were widely but discretely distributed in all three cortical layers (molecular, granular and Purkinje cells) whereas other isozymes were present in a limited neuronal compartment. Overall, the distribution of several isoforms was in agreement with data obtained by other authors using rat cerebellum. As far as ‐ι and ‐λ isozymes were concerned, we found them abundantly expressed in endothelial cells. Moreover, protein kinase C‐λ was also present in the body of Purkinje cell, conceivably associated with a 200‐kDa neurofilament component. In all, these results hint at the possibility that in the cerebellar cortex at least some protein kinase C isoforms are involved in functions other than signal transduction at the synaptic level.