Much less is known about the and subunits GlyR subunit

Much less is known about the α3 and α4 subunits. GlyR α3 subunit immunoreactive synapses are concentrated in discrete bands across the IPL; besides, bipolar, amacrine and ganglion cells have been suggested to express it (Haverkamp et al., 2003, Wässle et al., 2009). In fact, All amacrine express α3β GlyR (Wässle et al., 2009). However, physiological recordings demonstrated that bipolar cells do not express the α3 subunit (Ivanova et al., 2006). Interestingly, the inner retina from knockout mice appears intact regardless of the absence of α2, α3 or both subunits expression (Nobles et al., 2012; Zhang et al., 2105). Here we found a very low proportion of the α3 subunit at early postnatal ages (around 12%); however, it exhibited a considerably increased expression at P15-adult, which may represent its participation in maturing connectivity. In this respect, there is evidence that glycine signaling plays a key role in synapses and networks formation in spinal cord and retina (Xu and Tian, 2008). Regarding the expression of the α4 subunit in the developing retina, it represented a very low proportion of all GlyR subunits at P7 (2.5%), which was associated to the relatively low mRNA levels. Despite that, this protein showed a remarkable increase from P15 to the adult in which α4 reached its highest expression (16% of the total alpha subunits). In accordance with this, relatively low α4 immunoreactivity has been detected at the IPL in the adult mouse retina (Heinze et al., 2007, Wässle et al., 2009). Thus, our results might suggest that similar to the α3 subunit, the α4 subunit also participates in the establishment of specific synapses. In relation to the β subunit, expression of mRNA β subunit was found since early postnatal ages, reaching maximum levels at P15- adult, which suggests that about one-third of the GlyR expressed through all stages studied are heteromeric receptors. In this regard, besides the high expression of α1β GlyR in the inner retina, All amacrine express α3β GlyR, and narrow and wide field amacrine cells express α2β GlyR (Wässle et al., 2009). The use of GSK2578215A australia is a good tool to analyze the expression of proteins; however, the use of antibodies depends on their commercial availability, and different sources can lead to some kind of diverse results due to their characteristics and dissimilar specificity. Thus, we could not analyze the protein expression of the β subunit due to the difficulties in its commercial availability of its antibodies. In spite of that, the qPCR results agreed considerably with those of the protein expression of the other GlyR subunits.
Conclusions
Conflict of interest
Acknowledgements We thank Miss Viridiana Acosta for helping in the western blot analysis. This research was partially supported by the PAPIIT/UNAM project IG200216 and FIS/IMSS/PROT/G15/1401 from The Mexican Institute of Social Security (IMSS).
Introduction Despite great advances in the understanding and treatment of heart failure, the disease remains a leading cause of death worldwide [1], [2]. Heart failure is structurally characterized by pathologic hypertrophy of the myocardium which temporarily preserves pump function and reduces ventricular wall stress. However, prolonged cardiac hypertrophy can cause arrhythmias, dilated cardiomyopathy and heart failure [3], [4]. In contrast to physiological hypertrophy, pathological hypertrophy is characterized by accumulation of interstitial collagen and cell death, both of which contribute to increased risk for myocardial infarction, arrhythmia and sudden death. Therefore, it would be of great therapeutic interest to prevent pathological hypertrophy. Glycine is a major amino acid in mammals and other animals. It plays an important role in metabolism, growth, development, immunity, cytoprotection, and survival [5], [6]. Recent studies have shown a few beneficial effects of glycine on cardiomyocytes under ischemia-reperfusion (I/R) conditions. For example, 3mM glycine increases the cell viability of isolated rat hearts after I/R [7]. Infusion of glycine into animal donor hearts is good for right ventricular function after transplantation [8]. Glycine can inhibit the LPS induced increase in cytosolic Ca2+ concentration and tumor necrosis factor-α (TNF-α) production in cardiomyocytes by activating a glycine receptor (glyR) [9]. The antioxidant N-2-mercaptopropionyl glycine has been reported to attenuate cardiac hypertrophy induced by TAC in mice [10]. However, whether glycine has an impact on cardiac hypertrophy is unknown.