Aging‐dependent expression of synapse‐related proteins in the mouse brain

Abstract

A synapse is a cell adhesion structure that permits a neuron to pass a chemical or electrical signal to another neuron. They connect neurons and form neural networks that are essential for brain functions, such as learning and memory. At a chemical synapse, the presynapse and the postsynapse are connected by cell adhesion molecules. The presynapse contains synaptic vesicles and their release machinery, whereas the postsynapse contains postsynaptic densities and receptors for the neurotransmitters. Many proteins constituting a synapse have been identified, but their life-span expression profiles remain elusive. Here, we investigated the expression levels of representative synapse-related proteins by Western blot using the extranuclear supernatant fraction of the brains of mice at various ages. These proteins were classified into seven groups depending on their expression profiles during the embryonic stage, those from postnatal day 6 (P6) to P30, and those after P90. The expression levels of the majority of the proteins were gradually increased from the embryonic stage and then decreased at P14 or P30. After P90, the expression levels were not markedly changed or, in some proteins, increased. These results indicate that the expression levels of the synapse-related proteins are regulated orderly in an aging-dependent manner.

Developmental gene expression patterns in the brain and liver of Xenopus tropicalis during metamorphosis climax

“…In addition, Na + channel β-4 subunit and unphosphorylated tubulin β 3 class III proteins increase in the mouse brain during the postnatal and perinatal period, respectively (Fanarraga, L., Avila, J., & Zabala, J.C., 1999;Zhou, Zhang, Liu, Zhang, & Jiao, 2012). KCC2 mRNA and five synapse-related proteins are upregulated in the postnatal period (Clayton et al, 1998;Shiotani et al, 2017), and we showed their developmental regulation in the Xenopus tadpole brain during metamorphosis climax. The reduced expression level in the brain of hypothyroid rodents and the accumulation of mRNA stimulated by THs have been demonstrated for myelin-associated glycoprotein (Rodriguez-Peña et al, 1993), myelin basic protein (Ibarrola & Rodríguez-Peña, 1997), Na + ,K + -ATPase α2 (Chaudhury, Bajpai, & Bhattacharya, 1996) and neurofilament light and medium genes (Ghosh, Rahaman, & Sarkar, 1999).…”

“…The synapse plays a pivotal role in chemical and electrical signal transmission from one neuron to another to maintain the functions of the nervous system including learning, memory and locomotion. The developmental levels of synapse-related proteins in the mouse brain have been reported (Shiotani et al, 2017), including several proteins that peak at P14 when TH levels are at their maximum. qRT-PCR analysis was conducted to examine the developmental expression profiles of five synapse-related genes, necl-1, necl-2, nectin-1, nectin-3 and PSD-95.…”

Localization of nectin‐2α at the boundary between the adjacent somata of the clustered cholinergic neurons and its regulatory role in the subcellular localization of the voltage‐gated A‐type K+ channel Kv4.2 in the medial habenula

“…They were characterized as follows. Rat anti‐nectin‐2α/δ monoclonal Ab (mAb) (RRID:AB_590848) recognized 56‐kDa and 68‐kDa bands in Western blotting of mouse heart and brain (Aoki et al, ; Miyata et al, ; Shiotani et al, ). Specificity was verified by Western blotting of the wild‐type and nectin‐2 ‐deficient mouse hearts and cultured astrocytes and by immunohistochemistry on the wild‐type and nectin‐2 ‐deficient mouse hearts and brains (Miyata et al, ; Satomi‐Kobayashi et al, ).…”

“…Specificity was verified by Western blotting of the wild‐type and nectin‐2 ‐deficient mouse hearts and cultured astrocytes and by immunohistochemistry on the wild‐type and nectin‐2 ‐deficient mouse hearts and brains (Miyata et al, ; Satomi‐Kobayashi et al, ). Rat anti‐nectin‐3 mAb (RRID:AB_592587) recognized a 90‐kDa band in Western blotting of mouse brain (Miyata et al, ; Satoh‐Horikawa et al, 2000; Shiotani et al, ). Specificity was verified by Western blotting of the wild‐type and nectin‐3 ‐deficient mouse brains and by immunohistochemistry on the wild‐type and nectin‐3 ‐deficient mouse brains (Honda et al, ).…”

“…Specificity was verified by Western blotting of the wild‐type and nectin‐3 ‐deficient mouse brains and by immunohistochemistry on the wild‐type and nectin‐3 ‐deficient mouse brains (Honda et al, ). Rabbit anti‐Necl‐1 polyclonal Ab (pAb) recognized a 45‐kDa band in Western blotting of mouse brain (Kakunaga et al, ; Shiotani et al, ). Specificity was verified by Western blotting of the cultured wild‐type L cells and the cultured L cells stably expressing mouse Necl‐1 (Kakunaga et al, ).…”