Identification of a novel actin isoform in hepatocellular carcinoma

Chang, Ko‐Wei; Yang, Pei-Yin; Lai, Hsin-Yu; Yeh, Ta‐Sen; Chen, Tse–Ching; Yeh, Chau‐Ting

doi:10.1016/j.hepres.2006.05.003

Cited by 25 publications

(21 citation statements)

References 14 publications

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“…Less is known about ACTBM (also known as kappa actin). Kappa actins are also associated with cancer; expression is increased hepatocellular carcinoma[12]. ACTBM has been mapped to the subcellular locations of cytoskeleton, cytosol, extracellular space, vesicles and exosomes (IPA).…”

Section: Discussionmentioning

confidence: 99%

Proteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer’s disease

Nayak²,

et al. 2017

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Rapidly progressive Alzheimer’s disease (rpAD) is a particularly aggressive form of Alzheimer’s disease, with a median survival time of 7–10 months after diagnosis. Why these patients have such a rapid progression of Alzheimer’s disease is currently unknown. To further understand pathological differences between rpAD and typical sporadic Alzheimer’s disease (sAD) we used localized proteomics to analyze the protein differences in amyloid plaques in rpAD and sAD. Label-free quantitative LC-MS/MS was performed on amyloid plaques microdissected from rpAD and sAD patients (n=22 for each patient group) and protein expression differences were quantified. On average, 913±30 (mean±SEM) proteins were quantified in plaques from each patient and 279 of these proteins were consistently found in plaques from every patient. We found significant differences in protein composition between rpAD and sAD plaques. We found that rpAD plaques contained significantly higher levels of neuronal proteins (p=0.0017) and significantly lower levels of astrocyte proteins (p=1.08x10−6). Unexpectedly, cumulative protein differences in rpAD plaques did not suggest accelerated typical sAD. Plaques from patients with rpAD were particularly abundant in synaptic proteins, especially those involved in synaptic vesicle release, highlighting the potential importance of synaptic dysfunction in the accelerated development of plaque pathology in rpAD. Combined, our data provides new direct evidence that amyloid plaques do not all have the same protein composition and that the proteomic differences in plaques could provide important insight into the factors that contribute to plaque development. The cumulative protein differences in rpAD plaques suggest rpAD may be a novel subtype of Alzheimer’s disease.

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Section: Discussionmentioning

confidence: 99%

Proteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer’s disease

Nayak²,

et al. 2017

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“…Indeed, the association of ACTB with a wide range of cancer types (liver, renal, colorectal, gastric, pancreatic, esophageal, lung, breast, prostate, and ovarian cancers and leukemia, melanoma, and lymphoma) has been explained [34] and that of ACTBL2 in some hepatocellular carcinoma has been reported [35]. However, the combined effects of ACTB, ACTBL2, and either RPeL27 or RPeL43 in malignant transformation of human cells are unclear.…”

Section: Discussionmentioning

confidence: 99%

Human Ribosomal Proteins RPeL27, RPeL43, and RPeL41 Are Upregulated in Nasopharyngeal Carcinoma Cell Lines

Sim

Chan

et al. 2016

Disease Markers

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Apart from their canonical role in ribosome biogenesis, there is increasing evidence of ribosomal protein genes' involvement in various cancers. A previous study by us revealed significant differential expression of three ribosomal protein genes (RPeL27, RPeL41, and RPeL43) between cell lines derived from tumor and normal nasopharyngeal epithelium. However, the results therein were based on a semiquantitative assay, thus preliminary in nature. Herein, we provide findings of a deeper analysis of these three genes in the context to nasopharyngeal carcinoma (NPC) tumorigenesis. Their expression patterns were analyzed in a more quantitative manner at transcript level. Their protein expression levels were also investigated. We showed results that are contrary to previous report. Rather than downregulation, these genes were significantly overexpressed in NPC cell lines compared to normal control at both transcript and protein levels. Nevertheless, their association with NPC has been established. Immunoprecipitation pulldown assays indicate the plausible interaction of either RPeL27 or RPeL43 with POTEE/TUBA1A and ACTB/ACTBL2 complexes. In addition, RPeL43 is shown to bind with MRAS and EIF2S1 proteins in a NPC cell line (HK1). Our findings support RPeL27, RPeL41, and RPeL43 as potential markers of NPC and provide insights into the interaction targets of RPeL27 and RPeL43 proteins.

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“…Cytoskeleton or cytoskeleton-associated proteins were most represented in this analysis, and most of these were actin-related (Table IB). We identified several actin isoforms in the virus preparations, including a recently described novel actin isoform called ␤-actin-like protein 2 (-actin) (54). In Table IB, although only -actin was identified with a non-degenerate peptide sequence, peptides corresponding to other actin isoforms, including ␣-actin and ␤-actin, were present in the sample (supplemental Table 1, A and B).…”

Section: Proteomics Analysis Of Rsv Particlesmentioning

confidence: 98%

Protein Analysis of Purified Respiratory Syncytial Virus Particles Reveals an Important Role for Heat Shock Protein 90 in Virus Particle Assembly

Radhakrishnan

Yeo

Brown

et al. 2010

Molecular & Cellular Proteomics

119

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In this study, we used imaging and proteomics to identify the presence of virus-associated cellular proteins that may play a role in respiratory syncytial virus (RSV) maturation. Fluorescence microscopy of virus-infected cells revealed the presence of virus-induced cytoplasmic inclusion bodies and mature virus particles, the latter appearing as virus filaments. In situ electron tomography suggested that the virus filaments were complex structures that were able to package multiple copies of the virus genome. The virus particles were purified, and the protein content was analyzed by one-dimensional nano-LC MS/ MS. In addition to all the major virus structural proteins, 25 cellular proteins were also detected, including proteins associated with the cortical actin network, energy pathways, and heat shock proteins (HSP70, HSC70, and HSP90). Representative actin-associated proteins, HSC70, and HSP90 were selected for further biological validation. The presence of ␤-actin, filamin-1, cofilin-1, HSC70, and HSP90 in the virus preparation was confirmed by immunoblotting using relevant antibodies. Immunofluorescence microscopy of infected cells stained with antibodies against relevant virus and cellular proteins confirmed the presence of these cellular proteins in the virus filaments and inclusion bodies. The relevance of HSP90 to virus infection was examined using the specific inhibitors 17-N-Allylamino-17-demethoxygeldanamycin. Although virus protein expression was largely unaffected by these drugs, we noted that the formation of virus particles was inhibited, and virus transmission was impaired, suggesting an important role for HSP90 in virus maturation. This study highlights the utility of proteomics in facilitating both our understanding of the role that cellular proteins play during RSV maturation and, by extrapolation, the identification of new potential targets for antiviral therapy. Molecular & Cellular Proteomics 9:1829 -1848, 2010. Respiratory syncytial virus (RSV)1 belongs to the paramyxovirus group of viruses, and it is the most important respiratory virus causing lower respiratory tract infection in young children and neonates. The mature RSV particle comprises a ribonucleoparticle (RNP) core formed by the interaction between the viral genomic RNA (vRNA), the nucleocapsid (N) protein (42 kDa), the phospho (P) protein (35 kDa), and the large (L) protein (250 kDa). The RNP core is visualized by electron microscopy as a strand of repeating N protein subunits that form a herringbone-like structure of ϳ10 -20 nm in diameter (1). Although the minimal functional polymerase activity requires an association between the N, P, and L proteins and the virus genome vRNA (2-4), additional viral proteins called the M2-1 protein (22 kDa), M2-2 protein, and M protein (28 kDa) regulate the activity of the polymerase (5-8). The virus is surrounded by a lipid envelope that is formed from the host cell during the budding process in which the three virus membrane proteins are inserted. The G protein (90 kDa) mediates attachment of...

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Identification of a novel actin isoform in hepatocellular carcinoma

Cited by 25 publications

References 14 publications

Proteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer’s disease

Proteomic differences in amyloid plaques in rapidly progressive and sporadic Alzheimer’s disease

Human Ribosomal Proteins RPeL27, RPeL43, and RPeL41 Are Upregulated in Nasopharyngeal Carcinoma Cell Lines

Protein Analysis of Purified Respiratory Syncytial Virus Particles Reveals an Important Role for Heat Shock Protein 90 in Virus Particle Assembly

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