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Journal of Neuroscience, Vol 15, 1778-1796, Copyright © 1995 by Society for Neuroscience
Distinct mRNA expression of the highly homologous convertases PC5 and PACE4 in the rat brain and pituitary
W Dong, M Marcinkiewicz, D Vieau, M Chretien, NG Seidah and R Day
J. A. DeSeve Laboratory of Biochemical, Neuroendocrinology, Clinical Research Institute of Montreal, Quebec, Canada.
Posttranslational endoproteolysis is essential for the production of
biologically active peptides from inactive precursors. Six
kexin/substilisin-like endoproteases have been characterized in mammalian
species. To understand the complex physiological functions of each
convertase within a cellular context it is necessary to comprehensively
define its tissue distribution and cohabitation with other members of the
family. Previous studies demonstrated the distinct distribution of PC1,
PC2, and furin mRNAs in the pituitary and brain, suggesting a unique
function for each enzyme. In the present study, the mRNA tissue
distributions of the two most recent and homologous members, PC5 and PACE4,
were analyzed in rat pituitary and brain using in situ hybridization
histochemistry. In the pituitary, the anterior lobe exhibited moderate
levels of PC5 and high levels of PACE4 mRNAs. The intermediate lobe showed
low levels of PC5 expression, while PACE4 mRNA levels were undetectable.
PACE4 transcripts were detected throughout cells of the neural lobe
suggesting expression in pituicytes. In the brain, PC5 expression was more
restricted than PACE4. PC5 mRNA was detected only in neuronal cells,
whereas PACE4 mRNA was expressed in both neuronal and glial cells. In areas
that are rich in neuropeptides such as cortex, hippocampus, and
hypothalamus, mRNA levels of PC5 were high but PACE4 were low or
undetectable. In regions, such as the amygdaloid body and thalamus,
distinct but complementary distributions of PC5 and PACE4 mRNAs were
observed. The medial habenular and cerebellar Purkinje cells expressed very
high levels of PACE4 mRNA. The present data strongly suggest unique
tissue-specific functions of PC5 and PACE4.
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