Localization of two distinct type III phosphatidylinositol 4-kinase enzymemRNAs in the rat

Citation
A. Zolyomi et al., Localization of two distinct type III phosphatidylinositol 4-kinase enzymemRNAs in the rat, AM J P-CELL, 278(5), 2000, pp. C914-C920
Citations number
39
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cell & Developmental Biology
Journal title
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
ISSN journal
0363-6143 → ACNP
Volume
278
Issue
5
Year of publication
2000
Pages
C914 - C920
Database
ISI
SICI code
0363-6143(200005)278:5<C914:LOTDTI>2.0.ZU;2-8
Abstract
Inositol lipid kinases generate polyphosphoinositides, important regulators of several cellular functions. We have recently cloned two distinct phosph atidylinositol (PI) 4-kinase enzymes, the 210-kDa PI4KIII alpha and the 110 -kDa PI4KIII beta, from bovine tissues. In the present study, the distribut ion of mRNAs encoding these two enzymes was analyzed by in situ hybridizati on histochemistry in the rat. PI4KIIIa was found predominantly expressed in the brain, with low expression in peripheral tissues. PI4KIII beta was mor e uniformly expressed being also present in various peripheral tissues. Wit hin the brain, PI4KIII beta showed highest expression in the gray matter, e specially in neurons of the olfactory bulb and the hippocampus, but also ga ve a signal in the white matter indicating its presence in glia. PI4KIII al pha was highly expressed in neurons, but lacked a signal in the white matte r and the choroid plexus. Both enzymes showed expression in the pigment lay er and nuclear layers as well as in the ganglion cells of the retina. In a 17-day-old rat fetus, PI4KIII beta was found to be more widely distributed and PI4KIII alpha was primarily expressed in neurons. These results indicat e that PI4KIII beta is more widely expressed than PI4KIII alpha, and that t he two enzymes are probably coexpressed in many neurons. Such expression pa ttern and the conservation of these two proteins during evolution suggest t heir nonredundant functions in mammalian cells.