In:
American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 278, No. 5 ( 2000-05-01), p. C914-C920
Abstract:
Inositol lipid kinases generate polyphosphoinositides, important regulators of several cellular functions. We have recently cloned two distinct phosphatidylinositol (PI) 4-kinase enzymes, the 210-kDa PI4KIIIα and the 110-kDa PI4KIIIβ, from bovine tissues. In the present study, the distribution of mRNAs encoding these two enzymes was analyzed by in situ hybridization histochemistry in the rat. PI4KIIIα was found predominantly expressed in the brain, with low expression in peripheral tissues. PI4KIIIβ was more uniformly expressed being also present in various peripheral tissues. Within the brain, PI4KIIIβ showed highest expression in the gray matter, especially in neurons of the olfactory bulb and the hippocampus, but also gave a signal in the white matter indicating its presence in glia. PI4KIIIα was highly expressed in neurons, but lacked a signal in the white matter and the choroid plexus. Both enzymes showed expression in the pigment layer and nuclear layers as well as in the ganglion cells of the retina. In a 17-day-old rat fetus, PI4KIIIβ was found to be more widely distributed and PI4KIIIα was primarily expressed in neurons. These results indicate that PI4KIIIβ is more widely expressed than PI4KIIIα, and that the two enzymes are probably coexpressed in many neurons. Such expression pattern and the conservation of these two proteins during evolution suggest their nonredundant functions in mammalian cells.
Type of Medium:
Online Resource
ISSN:
0363-6143
,
1522-1563
DOI:
10.1152/ajpcell.2000.278.5.C914
Language:
English
Publisher:
American Physiological Society
Publication Date:
2000
detail.hit.zdb_id:
1477334-X
SSG:
12
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