Mechanotransduction Mechanisms of Hypertrophy and Performance with Resistance Exercise
Peter M. Tiidus, Rebecca E. K. MacPherson, Paul J. LeBlanc, Andrea R. Josse in The Routledge Handbook on Biochemistry of Exercise, 2020
Besides the mechanism of increasing ribosome assembly and translation initiation, the activation of early immediate genes from MAPK further regulates increases in ribosomal biogenesis (14, 161). Thus, the short-term activation post exercise to increase indices and assembly of ribosomal proteins for protein synthesis also activates translational capacity. This increase in ribosome biogenesis from mechanical overload appears to be partially mTOR independent (60, 175) and suggestive of ERK/MAPK involvement. Importantly, the MAPK pathway appears necessary for the maintenance of muscle mass via ERK and c-Jun N-terminal kinases (JNK) by sensitizing and integrating contraction and IGF-1 mediated stimuli into muscle hypertrophy (61, 111, 154). Although it is clear now that increased ribosome biogenesis from chronic resistance exercise supports enhanced translational capacity (14, 45), in vitro data suggest ribosome biogenesis alone is not the sole determinant of IGF-1-mediation of muscle hypertrophy (33). Finally, like satellite cell responses to resistance training, the expansion of ribosome biogenesis following chronic resistance exercise appears to be genetically determined, since recent data suggest older individuals who experience the greatest hypertrophy to a resistance training programme have faster ribosome biogenesis responses early in the training programme (159).
Translation and Post-Translational Modifications During Aging
Alvaro Macieira-Coelho in Molecular Basis of Aging, 2017
Ribosomes are cellular organelles that comprise at least 4 types of rRNA and about 80 proteins, and are the pivotal link where the language of nucleic acids is translated into a growing chain of amino acids. In the case of ribosomal proteins, the amino acid sequences of about 35 proteins out of a total of about 80 have been determined. However, the exact roles of the various rRNAs, the proteins, and their mutual interactions in determining the activity, efficiency, and accuracy of the ribosomes is not very well understood at present. Several studies have been performed on the age-related changes in the number of ribosomes, their thermal stability, their binding to aminoacyl-tRNA, the levels of ribosomal proteins and rRNAs, the sensitivity to aminoglycoside antibiotics, and the fidelity of ribosomes (Table 2).
Nonhistone Nuclear Phosphoproteins
Lubomir S. Hnilica in Chromosomal Nonhistone Proteins, 2018
Two-dimensional electrophoretic analyses showed that proteins from both ribosomal sub-units were present in nucleolar preribosomal particles.123,124 Among the proteins present in the preribosomal particles were the two proteins previously shown to be highly phosphorylated, B23 and C23. Olson et al.125 found that approximately 19 proteins including B23 and C23 were phosphorylated in vivo. Four of these were ribosomal proteins, but they were different from the proteins phosphorylated in cytoplasmic ribosomes. These results suggested that phosphorylation of proteins of the nucleolar preribosomes is independent of phosphorylation of cytoplasmic ribosomal proteins. It was also proposed that protein phosphorylation is involved in the maturation process of preribosomal particles.
Diversity of neuropsychiatric manifestations in systemic lupus erythematosus
Published in Immunological Medicine, 2020
Ribosomes are organelles of protein synthesis and are composed of ribosomal protein–RNA complexes. Ribosomal P protein refers to three types of phosphorylated proteins present on the 60S subunit of eukaryotic ribosomes. It is also known as the neuronal surface P antigen (NSPA) due to their expression on the neuronal cell surface in the cerebral cortex, hippocampus and amygdala [23]. P antigen consists of the highly conserved carboxy-terminal residues of three ribosomal phosphoproteins, P0 (38 kDa), P1 (19 kDa) and P2 (17 kDa) [24]. Anti-ribosomal P protein antibodies recognize all these proteins [25], increase cellular calcium influx and induce cell death [26]. Passive transfer experiments in mice have shown that anti-ribosomal P protein antibodies isolated from SLE patients induce olfactory abnormalities [27], depression-like manifestations [28] and memory impairment [29]. In addition, ribosomal P proteins are expressed on the surfaces of peripheral blood monocytes. Binding of anti-ribosomal P protein antibody to monocytes increases the production of proinflammatory cytokines, such as tumour necrosis factor-α and interleukin (IL)-6 from monocytes [30]. Since these cytokines contribute to the BBB breach, the association between anti-ribosomal P antibodies and BBB breach has recently been considered.
Exploitation of the antifungal and antibiofilm activities of plumbagin against Cryptococcus neoformans
Published in Biofouling, 2022
Weidong Qian, Wenjing Wang, Jianing Zhang, Yuting Fu, Qiming Liu, Xinchen Li, Ting Wang, Qian Zhang
As shown in Figure 7, 19 DEGs involved in ribosome biogenesis were observed in plumbagin-treated C. neoformans H99 cells in the biofilm and planktonic state. Ribosomes are composed of structural components encoded by ribosomal protein (RP) genes and are the sophisticated molecular machines for protein synthesis as directed by the genetic information encoded by mRNAs. In this study, 12 and seven DEGs in the plumbagin-treated C. neoformans H99 cells were downregulated in the biofilm and planktonic states, respectively. Moreover, the downregulated expression levels of RPL27 (ribosomal protein L27), RPL17, RPL22, RPL2, RPL9B, RPL30 and UBI1 genes in the C. neoformans H99 biofilm state were similar to those in the corresponding planktonic state. In contrast, the expression of RPL39, NOP1, MRPS18 and NOG2 were downregulated in the biofilm state, but were unaltered in the planktonic state.
Cerebrospinal fluid proteomics reveal potential protein targets of JiaWeiSiNiSan in preventing chronic psychological stress damage
Published in Pharmaceutical Biology, 2021
Han-Zhang Wang, Wu-Long Luo, Ning-Xi Zeng, Hui-Zhen Li, Ling Li, Can Yan, Li-Li Wu
Ribosomal proteins are closely related to complex functions – coordinating protein biosynthesis to maintain homeostasis and survival in cells. Many ribosomal proteins have secondary functions independent of their involvement in protein biosynthesis. Many of these proteins act as cell proliferation regulators and, in some cases, as inducers of cell death. Some scholars (Hetman and Slomnicki 2019) have suggested that ribosome biogenesis disorder may lead to insufficient proliferation and/or loss of neural precursor cells and apoptosis of immature neurons. In this study, a total of 35 differential proteins co-regulated by CUMS and JWSNS were screened, among which 8 were ribosome proteins, represented by Rps14, Rps4x and Rps12. They were highly co-expressed in the CUMS group, and their expression was reduced by JWSNS. These ribosomal proteins are highly differentiated and are key nodes in the protein interaction network, indicating that they are important proteins involved in the stress damage regulation of JWSNS. Consistent with our results, Hiroaki et al. (Hori et al. 2018) found that the ribosome gene was up-regulated in depression, bipolar disorder and schizophrenia and was associated with stress susceptibility in the analysis of gene expression profiles in human peripheral blood.
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