Other structural proteins analyzed were RRBP1, kinectin, and CKAP4. A common feature of these proteins is their coiled-coil domains that form luminal bridges and flat scaffolds. These proteins are implicated in shaping, cisternae stacking, and cytoskeletal interactions. RRBP1 and kinectin are ER integral membrane proteins. The former plays a role in polysome assembly and therefore in protein biosynthesis as well as expansion of the Golgi Protease Inhibitor Cocktail (EDTA-Free, 100X in DMSO) complex ; also, it has been shown that is an inductor of membrane biogenesis. Kinectin is a receptor for kinesin, which is involved in cellular component transport along microtubules. Both RRBP1 and kinectin were upregulated in the pathological groups studied. These results could indicate that modeling of the ER structure occurs as a possible consequence of UPR activation in ER stress conditions. Moreover, the upregulation of RRBP1 may influence the enhancement of protein synthesis necessary in some UPR pathways. In addition, we found a direct relationship between this protein and the stress protein XBP1 in the DCM group, giving evidence about the existence of a specific relationship between stress and structure. Besides, we found a solid inverse relationship between RRBP1 and LV function parameters EF and FS. These parameters are related to the ventricular remodeling that occurs in HF patients. This ventricular remodeling implies the activation of several pathways including inflammation and fibrosis that need a production of their related proteins. RRBP1 has a relevant role in protein synthesis and particularly it has been shown that is a crucial step in cardiac remodeling throughout increasing procollagen synthesis, necessary to develop the fibrosis processes in maladaptive cardiac remodeling. In addition, there is evidence supporting structural modifications under stress conditions. Tumarovs��ka et al. reported the dilation of ER cisternae in induced ER stress in isolated cardiomyocytes. Taking into account these findings and altogether with the results obtained in our study, we Mupirocin conclude that alterations in various UPR molecules as a consequence of ER stress may influence the architecture of the ER and alter its structure since we have observed changes in some of the proteins involved in forming and organizing the ER.