Publication: Protein kinase C isoforms and lipid second messengers: a critical nuclear partnership?
Authors
Neri, L.M. ; Borgatti, P. ; Capitani, S. ; Martelli, A.M.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
A growing body of evidence, accumulated
over the past 15 years,has highlighted that the protein
kinase C family of isozymes is capable of translocating
to the nucleus or is resident within the nucleus. The
comprehension of protein kinase C isoform regulation
within this organelle is under development. At present, it
is emerging that lipid second messengers may play at
least two roles in the control of nuclear protein kinase C:
on one side they serve as chemical attractants, on the
other they directly modulate the activity of specific
isoforms.
One of the best characterized lipid second messenger
that could be involved in the regulation of nuclear PKC
activity is DAG. The existence of two separate pools of
nuclear DAG suggests that this lipid second messenger
might be involved in distinct pathways that lead to
different cell responses.
Nuclear phosphatidylglycerol, D-3 phosphorylated
inositol lipids and nuclear fatty acids are involved in a
striking variety of critical biological functions which
may act by specific PKC activation.
The fine tuning of PKC regulation in cells subjected
to proliferating or differentiating stimuli, might prove to
be of great interest also for cancer therapy, given the fact
that PKC-dependent signaling pathways are increasingly
being seen as possible pharmacological target in some
forms of neoplastic diseases.
In this article, we review the current knowledge
about lipid second messengers that are involved in regulating the translocation and/or the activity of
different protein kinase C isoforms identified at the
nuclear level.
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