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Signal transduction and exercise
Published in Adam P. Sharples, James P. Morton, Henning Wackerhage, Molecular Exercise Physiology, 2022
Brendan Egan, Adam P. Sharples
Mature mRNA is translated into protein by ribosomes. Ribosomes consist of a small 40S and a large 60S subunit of rRNA (ribosomal RNA) that join together to create an 80S ribosome. Ribosomes are controlled by ribosomal proteins, which are regulated especially by the mTOR signalling pathways. In the late 1990s, it was noted that translational regulators were modulated in hypertrophying muscles (74), and subsequent research has shown that activation of translation via the mTOR pathway is a key mechanism by which exercise increases MPS (in a later section, we provide more discussion on the role of MPS in aerobic and resistance exercise adaptations). Protein translation occurs in three stages: initiation, where the ribosome and mRNA are assembled;elongation, where the mRNA is read by the ribosome and translated into an amino acid chain; andtermination.
Diamond–Blackfan Anemia
Published in Dongyou Liu, Handbook of Tumor Syndromes, 2020
Homozygous mutation in the ribosomal protein (RP) genes is likely lethal to embryos, as only heterozygous pathogenic variants are observed in DBA-affected individuals. Heterozygous germline RP mutations occur in about 70% of cases and demonstrate autosomal dominant inheritance, in which one copy of the altered gene in each cell is sufficient to cause the disorder. While 40%–45% of patients with autosomal dominant DBA inherit the pathogenic variant from a parent, 55%–60% of patients appear to evolve from a de novo mutation (with neither parent possessing pathogenic variant nor showing clinical evidence of the disorder). A few DBA cases are caused by mutations in TSR2 on chromosome Xp11.2 and GATA1 on Xp11.23, which indicate maternal inheritance. Further, about 30% of DBA cases appear to contain mutations in other unidentified genes [1].
Nonhistone Nuclear Phosphoproteins
Published in Lubomir S. Hnilica, 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.
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.
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.