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Adult Ocular and Orbital (Ocular Adnexa) Tumors
Published in Pat Price, Karol Sikora, Treatment of Cancer, 2020
P.N. Plowman, Rachel Lewis, J.L. Hungerford
Inactivating mutations in BAP1, a tumor suppressor gene located on chromosome 3p, are found in approximately 47% of primary uveal melanoma and 84% of metastatic uveal melanoma cases, consistent with the association between BAP1 mutations and poor prognosis.16 Mutations in splicing factor 3B subunit 1 (SF3B1), involved in pre-messenger RNA splicing, while associated with more favorable prognostic features than BAP1 mutations, are also found in cases of delayed metastasis, with a median of 8.2 years.16,17EIF1AX encodes for eukaryotic translation initiation factor 1A. These mutations are mutually exclusive from BAP1 and SF3B1 and are associated with a longer disease-free survival and a more favorable prognosis.
Familial Chordoma
Published in Dongyou Liu, Handbook of Tumor Syndromes, 2020
Alexandra Suttman, Sydney T. Grob, Jean M. Mulcahy Levy
TSC1 and TSC2 encode for the proteins hamartin and tuberin, respectively. Together they form a complex that is thought to function as a “tumor suppressor” with roles in cellular signaling and cell growth and proliferation. Alteration and/or inactivation of the hamartin-tuberin protein complex results in unregulated activation of mTOR pathway, which is crucial for cell-cycle regulation [19]. Increased mTOR activity results in phosphorylation of S6 ribosomal protein and eukaryotic translation initiation factor 4E (eIF-4E). This results in the abnormal growth of multiple tissues including facial angiofibroma, cardiac rhabdomyoma, subependymal nodules, and subependymal giant cell astrocytomas, which are all clinical characteristics of patients with TSC [20].
Translation
Published in Paul Pumpens, Single-Stranded RNA Phages, 2020
The MS2 RNA-programmed in vitro protein synthesis was employed by examination of small peptides that inhibited translation by targeting the specific sites of ribosomal RNA within the ribosome and not only accelerated production of new antibiotics but also provided new tools for ribosomal research (Llano-Sotelo et al. 2009). Such peptides were selected by a principally novel approach when a heptapeptide phage-display library was screened for the affinity to the h18 pseudoknot of 16S rRNA, which played a central role in functions of the ribosome decoding center and was directly involved in controlling the accuracy of the aminoacyl-tRNA selection (Ogle et al. 2001). As a result, two of the selected peptides could interfere efficiently with both bacterial and eukaryotic translation.
EIF3B promotes cancer progression in pancreatic cancer
Published in Scandinavian Journal of Gastroenterology, 2021
Hanzhang Zhu, Yuqiang Shan, Ke Ge, Jun Lu, Wencheng Kong, Changku Jia
Eukaryotic Translation Initiation Factor 3 Subunit B (EIF3B) is the RNA-binding component of the eIF-3 complex and critical for several steps in the initiation of protein synthesis [8]. Aberrances in EIF3B have been characterized in several human cancers. Chai et al. performed the systematic profiling of the eIF3 subunits in glioma and suggested that eIF3i exhibited prognostic value in IDH-mutant lower grade glioma [9]. Wang et al. showed that shRNA-mediated knockdown of EIF3B in human ovarian cancer cells significantly suppressed cell proliferation and induced apoptosis [10]. Tian et al. uncovered that EIF3B correlated with advanced disease stage and poor prognosis in non-small cell lung cancer via promoting proliferation and inhibiting apoptosis [11]. Consistently, Choi et al. demonstrated that silencing EIF3B promoted apoptosis in osteosarcoma cells as well [12]. Zhang et al. proposed that EIF3B displayed prognostic value in clear cell renal cell carcinoma and served as a potential therapeutic target [13]. Xu et al. reported that EIF3B accelerated the progression of esophageal squamous cell carcinoma by activating the β-catenin signaling pathway [14]. In colon cancer cells, Wang et al. provided evidences that RNAi-mediated silencing of EIF3B inhibited cell proliferation [15], and similar observation was noticed in glioblastoma cells [16]. However, the expression status and mechanistic involvement of EIF3B in pancreatic cancer are still elusive currently. Here we started with analyzing clinical tumor samples to address this question.
Unpacking the genetic etiology of uveal melanoma
Published in Expert Review of Ophthalmology, 2020
Sophie Thornton, Helen Kalirai, Karen Aughton, Sarah E. Coupland
Eukaryotic translation initiation factor 1A X-linked (EIF1AX) located on Xp22.12 encodes an essential eukaryotic translation protein required for ribosome dissociation and stabilizing the binding of Met-tRNA to 40 S ribosomal subunits. EIF1AX mutations in UM occur across hotspots on exons 1 and 2 at a frequency of 14–34% [39,45,87,89,92], generally occurring only in D3-UM cases. Mutations in EIF1AX are associated with a more favorable prognosis and play a protective role to prevent metastasis even when taking into consideration clinical and histological risk factors [88,92]. Although they were initially thought to be mutually exclusive of SF3B1 mutations [93], a targeted sequencing study identified two rare cases of D3-UM that harbored both SF3B1 and EIF1AX mutations, as well as two cases of EIF1AX mutant M3-UM [57]. In the two UM cases showing both SF3B1 and EIF1AX mutations, metastatic death occurred within 5 years of the diagnosis of the primary UM [57].
Maytansine-bearing antibody-drug conjugates induce in vitro hallmarks of immunogenic cell death selectively in antigen-positive target cells
Published in OncoImmunology, 2019
Maxine Bauzon, Penelope M. Drake, Robyn M. Barfield, Brandon M. Cornali, Igor Rupniewski, David Rabuka
An ER stress response has been shown to precede cell surface calreticulin exposure. A central aspect of this stress response is a global reduction in protein synthesis mediated via phosphorylation of eukaryotic translation initiation factor 2A (EIF2A), a regulatory component of the ternary complex that brings the initiator Met-tRNAi to the 40S ribosomal subunit.39 A number of studies have demonstrated that EIF2A is phosphorylated in the context of ICD. 7,15,40,41 Accordingly, we asked whether the target cell lines used in our study – BT474 and BJAB – increased the phosphorylation of EIF2A after treatment with free maytansine (100 nM). Indeed, as determined by immunoblotting, induction of phosphorylated EIF2A was observed in both cell lines as early as 16 h post-maytansine treatment (Figure 5).