Distribution of the protein kinase C substrates MARCKS and MRP in the postnatal developing rat brain.
The myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP) are both membrane-associated phosphoproteins that interact with calmodulin and filamentous actin in a protein kinase C phosphorylation-dependent manner. In the present study, we examined MARCKS and MRP gene expression in the postnatal (P) rat brain (1, 7, 14, 21, and 90 days after birth) by using quantitative in situ hybridization. At P1, MRP expression was high in neocortex, striatum, thalamus, cerebellar cortex, and hippocampus (CA1-CA3, hilus, and granule cell layer) but low in brainstem and, between P7 and P14, exhibited a dramatic decline in each of these regions except hippocampal CA1 and granule cell layers. Between P14 and P21, MRP expression increased in white matter regions including the corpus callosum, fimbria/fornix, and cerebellar deep white matter. At P90 (adult), MRP remained strongly expressed in the olfactory bulb, medial habenula, hippocampal CA1, and the inner two-thirds of granule cell layer, temporal, and entorhinal cortices, the corpus callosum and fimbria/fornix, and cerebellar white matter. At P1, MARCKS was strongly expressed in the majority of brain regions except the brainstem, which subsequently declined gradually to approximate adult levels by P14. Between P14 and P21, MARCKS expression declined gradually in the hilus, remained elevated in hippocampal CA1, CA3, and granule cell layers, and increased dramatically in the corpus callosum and fimbria/fornix. At P90, MARCKS expression declined in hippocampal CA3 and hilus and remained strongly expressed in hippocampal CA1 and granule cell layers, regions of the olfactory bulb, the medial habenula, temporal cortex, and cerebellar granule and Purkinje cells. Expression of both MARCKS and MRP in regions undergoing neuronal proliferation, migration, and neurite outgrowth suggest a common role in these developmental events, whereas differences in expression during development and in the adult brain provide evidence of differential regulation.
McNamara
R K
RK
Department of Psychiatry, University of Florida College of Medicine, Gainesville 32610-0256, USA. rkm@mail.med.upenn.edu
Lenox
R H
RH
D000375:Aging / Q000378:metabolism*; D000818:Animals; D000831:Animals, Newborn / Q000254:growth & development / Q000378:metabolism*; D001921:Brain / Q000254:growth & development / Q000378:metabolism*; D017403:In Situ Hybridization; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D011493:Protein Kinase C / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D051381:Rats / Q000254:growth & development / Q000378:metabolism*; D017207:Rats, Sprague-Dawley; D013379:Substrate Specificity; D014018:Tissue Distribution; D033921:Vesicular Transport Proteins
D047908:Intracellular Signaling Peptides and Proteins; C000619712:Marcks protein, rat; C512942:Marcksl1 protein, rat; D008565:Membrane Proteins; D011506:Proteins; D033921:Vesicular Transport Proteins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D011493:Protein Kinase C