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Physiology, Biochemistry, and Pathology of Neuromuscular Transmission
Published in Marc H. De Baets, Hans J.G.H. Oosterhuis, Myasthenia Gravis, 2019
Synapsin I projects to the cytoplasmic domain, and may serve a role as a link between vesicles and cytoskeletal elements.39 Phosphorylation decreases the binding between synapsin I and synaptic vesicles. Nervous stimulation may unlock synapsin I from the vesicles, thereby liberating the vesicles for movement to release sites.40
The Calcium-Calmodulin System
Published in Enrique Pimentel, Handbook of Growth Factors, 2017
CaM kinase I is involved in the phosphorylation of a specific serine residue in a collagenase-resistant domain of synapsin I, a synaptic vesicle associated protein that is involved in the regulation of neurotransmitter release. The enzyme was purified from bovine brain using synapsin I as substrate.169 CaM kinase I contains sequences that are autophosphorylated on threonine in the presence of Ca2+ and calmodulin, but the possible role of these autophosphorylations is not known. Also unknown is the function of the phosphorylation of synapsin I as well as the phosphorylation of another substrate of the same kinase, protein IB.
Composition of The Chromaffin Cell
Published in Stephen W. Carmichael, Susan L. Stoddard, The Adrenal Medulla 1986 - 1988, 2017
Stephen W. Carmichael, Susan L. Stoddard
Romano, Nichols, Greengard et al. (1987) characterized synapsin I in PC12 cells; the molecule was immunochemically similar to that molecule in the brain. Chronic nerve growth factor treatment of the PC12 cells induces a significant increase in the total amount of synapsin I relative to total cell protein.
Potential neuroprotective role of astroglial exosomes against smoking-induced oxidative stress and HIV-1 replication in the central nervous system
Published in Expert Opinion on Therapeutic Targets, 2018
Sabina Ranjit, Benjamin J. Patters, Kelli A. Gerth, Sanjana Haque, Sanjeev Choudhary, Santosh Kumar
Several studies report that glial cells protect neurons from oxidative stress via release of exosomes carrying protective molecules and proteins. Astrocyte-derived exosomes are known to provide neuroprotection against oxidative damage by transfer of prion protein, a cell surface glycoprotein, which acts as a sensor for oxidative stress [80]. Synapsin I, an oligomannose-carrying glycoprotein that promotes neurite outgrowth and neuronal survival under stress conditions, is also found to be packaged by exosomes released from astrocytes [81]. Another report suggests a mechanism by which astrocytes provide antioxidant protection is by secreting exosomes containing heat shock proteins (e.g. HSP70) [82]. HSP70 rescues oxidative damage by preventing protein misfolding and aggregation or by inhibiting the factors that promote apoptosis and inflammation [83]. Frohlich et al. (2014) have reported that exosomes from oligodendrocytes protect neurons under ischemic conditions by transporting the antioxidant enzymes SOD1 and catalase [15]. These findings suggest a therapeutic role of exosomes in combating oxidative stress, inflammation, and the subsequent neuronal damage. Consistent with this hypothesis, exosomes artificially loaded with catalase have been shown to rescue oxidative damage and promote neuroprotection in both in vitro and in vivo models of Parkinson’s disease [16].
RLIPostC protects against cerebral ischemia through improved synaptogenesis in rats
Published in Brain Injury, 2018
Yingli Wang, Zhaohui Zhang, Lei Zhang, Haoran Yang, Zhiqiang Shen
Synapsin 1 (Syn1) is a member of the synapsin gene family, which plays an important role in the regulation of synaptogenesis. Here, we detected the effects of RLIPostC treatment on the expression of Syn1 at day 14 after MCAO by western blotting. The results showed that RLIPostC treatment significantly upregulated the expression of Syn1 (p < 0.05, Figure 4(a)) compared to the control group. Interestingly, although there was no statistical difference, the expression of Syn1 in the RLIPostC treatment group was higher than that in the sham group (p = 0.32).
Flavanol-rich lychee fruit extract substantially reduces progressive cognitive and molecular deficits in a triple-transgenic animal model of Alzheimer disease
Published in Nutritional Neuroscience, 2021
Xiao Chen, Benhong Xu, Luling Nie, Kaiwu He, Li Zhou, Xinfeng Huang, Peter Spencer, Xifei Yang, Jianjun Liu
To explore the modulation of synaptic proteins by Oligonol, we used Western-blot analysis to determine the expression of synapsin I, synapsin II, synaptophysin, post-synaptic density protein PSD 93 and PSD 95 (Figure 3). The expressions of synapsin I, synaptophysin and PSD 93 in WT and 3×Tg-AD did not differ, but the mean levels of synapsin II and PSD95 were significantly lower in the 3×Tg-AD group. 3×Tg-AD mice treated with high-dose Oligonol showed mean levels of synapsin II and PSD 95 significantly higher than in Oligonol-untreated 3×Tg-AD mice.