The Expression Pattern of Heterogeneous Nuclear Ribonucleoprotein R in Rat Retina

Peng, Zheng-Yu; Huang, Jia; Lee, Shu-Chen; Shi, Yongliang; Chen, Xianhua; Xu, Ping

doi:10.1007/s11064-008-9878-3

Cited by 4 publications

(3 citation statements)

References 24 publications

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“…For example, HNRNPR is a member of the hnRNP protein family. It reacts with SF3A2 protein and hence, is involved in the formation of SF3a complex/ U2 mnRNP [9]. In turn, DDX46 protein, belonging to group DExH/D helicases, forms a bridge between U1 and U2 mnRNP, thus forming a presplisosome [12].…”

Section: Resultsmentioning

confidence: 99%

Changed Profile of Expression of Splicing Regulator Genes in Response to Exercise

et al. 2009

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Intensive exercise triggers the cascade processes of body adaptation, including modulation of splisosome functioning, and can lead to modification of its activity and choice of alternative exons. We studied the effect of exercise of the maximum aerobic power on activation of transcription of genes involved in the splicing process. Short-term exercise resulted in a significant increase of mRNA expression of genes encoding proteins involved in the formation of precatalytic splisosome: DDX17, DDX46, HNRNPR, PRPF4B, and SRPK2. The role of the detected regulators in initiation of splisosome assembly under conditions of maximally intensive exercise is discussed.

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Section: Resultsmentioning

confidence: 99%

Changed Profile of Expression of Splicing Regulator Genes in Response to Exercise

et al. 2009

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“…hnRNP R and hnRNP Q are multi-functional, RNA-binding proteins containing three RNA recognition motifs, one acidic rich domain and an RGG domain [21, 38]. Despite being widely expressed in neuronal tissue little is known about these hnRNP in the context of neurodegenerative diseases [44]. The two proteins have high sequence homology with sequence alignment of their canonical isoforms showing that they are 81.2% identical at the amino acid level [37].…”

Section: Discussionmentioning

confidence: 99%

Heterogeneous nuclear ribonucleoproteins R and Q accumulate in pathological inclusions in FTLD-FUS

Gittings

Foti

Benson

et al. 2019

acta neuropathol commun

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Frontotemporal lobar degeneration (FTLD) is pathologically subdivided based on the presence of particular pathological proteins that are identified in inclusion bodies observed post-mortem. The FTLD-FUS subgroup is defined by the presence of the fused in sarcoma protein (FUS) in pathological inclusions. FUS is a heterogeneous nuclear ribonucleoprotein (hnRNP) protein and a member of the FET (FUS, EWS, TAF15) protein family. It shuttles between the nucleus and cytoplasm, and has been implicated in many cellular functions including translation, splicing, and RNA transport. EWS, TAF15 and the nuclear import receptor transportin have been shown to co-accumulate with FUS in neuronal inclusions specifically in FTLD-FUS, with transportin-positive inclusions most frequently observed. Here, we report the identification of hnRNP R and hnRNP Q in neuronal cytoplasmic and intranuclear inclusions in the frontal cortex and hippocampus of FTLD-FUS patients, as frequently as transportin. hnRNP R and hnRNP Q were not found in the characteristic pathological inclusions observed in FTLD-TDP (subtypes A-C). Additionally, we studied the expression of hnRNP R in the frontal and temporal cortices from patients with FTLD and found significantly increased expression of the heterogeneous nuclear ribonucleoprotein R in several FTLD disease groups. Our identification of the frequent presence of hnRNP R and hnRNP Q in FTLD-FUS inclusions suggests a potential role for these hnRNPs in FTLD-FUS pathogenesis and supports the role of dysfunctional RNA metabolism in FTLD.Electronic supplementary materialThe online version of this article (10.1186/s40478-019-0673-y) contains supplementary material, which is available to authorized users.

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“…Mouse epididymal tissues were prepared for the protein extraction or fixed by 4% paraformaldehyde/PBS as described previously [21]. The surgery of unilateral-castrated or bilateral castrated animals was performed as described previously [22].…”

Section: Methodsmentioning

confidence: 99%

Dephosphorylated NSSR1 Is Induced by Androgen in Mouse Epididymis and Phosphorylated NSSR1 Is Increased during Sperm Maturation

et al. 2011

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NSSR1 (Neural salient serine/arginine rich protein 1, alternatively SRp38) is a newly identified RNA splicing factor and predominantly expressed in neural tissues. Here, by Western blot analysis and immunofluorescent staining, we showed that the expression of dephosphorylated NSSR1 increased significantly during development of the caput epididymis. In adult mice, phosphorylated NSSR1 was mainly expressed in the apical side of epithelial cells, and dephosphorylated NSSR1 in caput epididymis was upregulated in a testosterone dependent manner. In addition, subcellular immunoreactive distribution of NSSR1 varied in different regions of the epididymis. With respect to the sperm, phosphorylated NSSR1 was detected in the mid-piece of the tail as well as the acrosome. Furthermore, NSSR1 was released from the sperm head during the capacitation and acrosome reaction. These findings for the first time provide the evidence for the potential roles of NSSR1 in sperm maturation and fertilization.

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The Expression Pattern of Heterogeneous Nuclear Ribonucleoprotein R in Rat Retina

Cited by 4 publications

References 24 publications

Changed Profile of Expression of Splicing Regulator Genes in Response to Exercise

Changed Profile of Expression of Splicing Regulator Genes in Response to Exercise

Heterogeneous nuclear ribonucleoproteins R and Q accumulate in pathological inclusions in FTLD-FUS

Dephosphorylated NSSR1 Is Induced by Androgen in Mouse Epididymis and Phosphorylated NSSR1 Is Increased during Sperm Maturation

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