Localization of mRNAs for subfamily of guanine nucleotide-exchange proteins (GEP) for ARFs (ADP-ribosylation factors) in the brain of developing and mature rats under normal and postaxotomy conditions.
ADP-ribosylation factors (ARFs) play important roles in vesicular trafficking and cytoskeletal regulation and its activation depends on guanine nucleotide-exchange proteins (GEPs). By way of in situ hybridization histochemistry, the localization of mRNAs for subfamily members of low-molecular-weight ARF-GEPs in the rat brain was studied at embryonic and postnatal stages. In the embryonic brain, the gene expression for msec7-1 was distinct in the ventricular zone while that for msec7-1, -3 and EFA6 in the mantle zone. In early postnatal brain, the expression for msec7-1, -2, -3 and EFA6 was seen widely in various loci of the gray matter with different intensity, and the expression of msec7-1 and -2 mRNAs was evident in the cerebellar external granule cell layer. In the adult brain, the gene expression for the four ARF-GEPs decreased more or less in most gray matter and the distinct expression was maintained mainly in the hippocampal and dentate neuronal layers and cerebellar cortex. The expression of EFA6 mRNA was also evident in the molecular layer of the hippocampus and dentate gyrus. No obvious gene expression for cytohesin-4 and ARF-GEP100 was detected in the brain at any stages of development. The present findings suggest that ARF-GEPs are differentially involved in some processes essential to neuronal differentiation and maturation in association with ARFs.
Suzuki
Ichiro
I
Division of Histology, Department of Cell Biology, Graduate School of Medicine, Tohoku University, 2-1 Seiryo-machi, Aoba-ku, 980-8575, Sendai, Japan.
Owada
Yuji
Y
Suzuki
Ryoji
R
Yoshimoto
Takashi
T
Kondo
Hisatake
H
D020727:ADP-Ribosylation Factors / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D019771:Axotomy; D001483:Base Sequence; D001921:Brain / Q000196:embryology / Q000254:growth & development / Q000378:metabolism*; D015815:Cell Adhesion Molecules / Q000096:biosynthesis / Q000235:genetics; D005260:Female; D005326:Fetal Proteins / Q000096:biosynthesis / Q000235:genetics; D020690:GTPase-Activating Proteins; D005786:Gene Expression Regulation; D020662:Guanine Nucleotide Exchange Factors / Q000096:biosynthesis / Q000235:genetics*; D006624:Hippocampus / Q000196:embryology / Q000254:growth & development / Q000378:metabolism; D006801:Humans; D007002:Hypoglossal Nerve / Q000254:growth & development / Q000378:metabolism; D061228:Hypoglossal Nerve Injuries; D017403:In Situ Hybridization; D008297:Male; D008969:Molecular Sequence Data; D009416:Nerve Regeneration / Q000235:genetics; D009419:Nerve Tissue Proteins / Q000096:biosynthesis / Q000235:genetics*; D010445:Peptide Elongation Factors / Q000096:biosynthesis / Q000235:genetics*; D012333:RNA, Messenger / Q000032:analysis* / Q000235:genetics; D051381:Rats; D012183:Retrograde Degeneration / Q000235:genetics; D017385:Sequence Homology; D013045:Species Specificity
C404511:CYTH4 protein, human; D015815:Cell Adhesion Molecules; C491661:Cyth 1 protein, rat; C491662:Cyth3 protein, rat; D005326:Fetal Proteins; D020690:GTPase-Activating Proteins; D020662:Guanine Nucleotide Exchange Factors; C504483:IQSEC1 protein, human; C000588810:IQSEC1 protein, rat; D009419:Nerve Tissue Proteins; C109970:PSD protein, human; D010445:Peptide Elongation Factors; C504475:Psd protein, rat; D012333:RNA, Messenger; C066755:Sec7 guanine nucleotide exchange factors; C102474:cytohesin-2; D020727:ADP-Ribosylation Factors