Abstract
Subplate cells are among the first generated neurons in the mammalian cerebral cortex and have been implicated in the establishment of cortical wiring. In rodents some subplate neurons persist into adulthood. Here we would like to highlight several converging findings which suggest a novel secretory function of subplate neurons during cortical development. Throughout the postnatal period in rodents, subplate neurons have highly developed rough endoplasmic reticulum (ER) and are under an ER stress condition. By comparing gene expression between subplate and layer 6, we found that several genes encoding secreted proteins are highly expressed in subplate neurons. One of these secreted proteins, neuroserpin, encoded by the serpini1 gene, is localized to the ER in subplate cells. We propose that subplate might influence cortical circuit formation through a transient secretory function.
Highlights
All eukaryotic cells contain a discernible amount of rough endoplasmic reticulum (ER) because it is needed for the synthesis of plasma membrane proteins and proteins of the extracellular matrix (Depierre and Dallner, 1975)
The section were incubated in 2% normal goat serum (NGS) diluted in Tris-buffered saline (TBS; 50 mM Tris buffer, 0.09% NaCl, pH 7.4) for blocking, and incubated for 2 h at room temperature (RT) with mouse anti-KDEL antibody (1:500, Abcam) as anti-immunoglobulin heavy chain-binding protein (BiP) (Okiyoneda et al, 2004) and rabbit anti-neuroserpin antibody (1:200, Abcam) in 1% NGS diluted in TBS
Plentiful Nissl substance was observed in layer 2/3 and subplate neurons (Figure 1A), suggesting that these neurons produce a large amount of proteins at P8
Summary
All eukaryotic cells contain a discernible amount of rough endoplasmic reticulum (ER) because it is needed for the synthesis of plasma membrane proteins and proteins of the extracellular matrix (Depierre and Dallner, 1975). Plasma cells produce antibodies, which circulate in the bloodstream, and pancreatic acinar cells synthesize digestive enzymes, which are transported to the intestine. In both types of cells, a large part of the cytosol is filled with rough ER. When cells synthesize secretory proteins in amounts that exceed the capacity of the folding apparatus, unfolded proteins accumulate in the rough ER To alleviate such an overstretched functional state, eukaryotic cells activate a series of self-defense mechanisms referred to collectively as the ER stress response ( called the unfolded protein response) (Schroder and Kaufman, 2005). ER stress response is especially observed physiologically for dedicated secretory cells, such as plasma cells, pancreatic acinar cells, and pancreatic beta cells, where high levels of secreted protein synthesis require a highly evolved mechanism to properly fold, process and secrete them (Wu and Kaufman, 2006; Kondo et al, 2011)
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