Academic literature on the topic 'HnRNP A2/B1'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'HnRNP A2/B1.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Journal articles on the topic "HnRNP A2/B1"
1
Shi, Stephanie T., Guann-Yi Yu, and Michael M. C. Lai. "Multiple Type A/B Heterogeneous Nuclear Ribonucleoproteins (hnRNPs) Can Replace hnRNP A1 in Mouse Hepatitis Virus RNA Synthesis." Journal of Virology 77, no. 19 (2003): 10584–93. http://dx.doi.org/10.1128/jvi.77.19.10584-10593.2003.
Full textAbstract:
ABSTRACT Heterogeneous nuclear ribonucleoprotein (hnRNP) A1 has previously been shown to bind mouse hepatitis virus (MHV) RNA at the 3′ end of both plus and minus strands and modulate MHV RNA synthesis. However, a mouse erythroleukemia cell line, CB3, does not express hnRNP A1 but still supports MHV replication, suggesting that alternative proteins can replace hnRNP A1 in cellular functions and viral infection. In this study, we set out to identify these proteins. UV cross-linking experiments revealed that several CB3 cellular proteins similar in size to hnRNP A1 interacted with the MHV RNA. These proteins were purified by RNA affinity column with biotinylated negative-strand MHV leader RNA and identified by mass spectrometry to be hnRNP A2/B1, hnRNP A/B, and hnRNP A3, all of which belong to the type A/B hnRNPs. All of these proteins contain amino acid sequences with strong similarity to the RNA-binding domains of hnRNP A1. Some of these hnRNPs have previously been shown to replace hnRNP A1 in regulating RNA splicing. These proteins displayed MHV RNA-binding affinity and specificity similar to those of hnRNP A1. hnRNP A2/B1, which is predominantly localized to the nucleus and shuttles between the nucleus and the cytoplasm, was shown to relocalize to the cytoplasm in MHV-infected CB3 cells. Furthermore, overexpression of hnRNP A/B in cells enhanced MHV RNA synthesis. Our findings demonstrate that the functions of hnRNP A1 in MHV RNA synthesis can be replaced by other closely related hnRNPs, further supporting the roles of cellular proteins in MHV RNA synthesis.
2
Wang, Tong-Hong, Chin-Chuan Chen, Yuan-Chao Hsiao, et al. "Heterogeneous Nuclear Ribonucleoproteins A1 and A2 Function in Telomerase-Dependent Maintenance of Telomeres." Cancers 11, no. 3 (2019): 334. http://dx.doi.org/10.3390/cancers11030334.
Full textAbstract:
The A/B subfamily of heterogeneous nuclear ribonucleoproteins (hnRNPs A/B), which includes hnRNP A1, A2/B1, and A3, plays an important role in cell proliferation. The simultaneous suppression of hnRNP A1/A2, but not the suppression of hnRNP A1 or A2 alone, has been shown to inhibit cell proliferation and induce apoptosis in cancer cells, but not in mortal normal cells. However, the molecular basis for such a differential inhibition of cell proliferation remains unknown. Here, we show that the simultaneous suppression of hnRNP A1 and hnRNP A2 resulted in dysfunctional telomeres and induced DNA damage responses in cancer cells. The inhibition of apoptosis did not alleviate the inhibition of cell proliferation nor the formation of dysfunctional telomeres in cancer cells depleted of hnRNP A1/A2. Moreover, while proliferation of mortal normal fibroblasts was not sensitive to the depletion of hnRNP A1/A2, the ectopic expression of hTERT in normal fibroblasts rendered these cells sensitive to proliferation inhibition, which was associated with the production of dysfunctional telomeres. Our study demonstrates that hnRNP A1 and A2 function to maintain telomeres in telomerase-expressing cells only, suggesting that the maintenance of functional telomeres in telomerase-expressing cancer cells employs factors that differ from those used in the telomerase-negative normal cells.
3
Gu, Wenchao, Xiwen Gao, Linxun Wang, et al. "The Expression of hnRNP A2/B1 in Benign and Malignant Lung Lesions and Its Early Diagnosis Value in NSCLC." Contrast Media & Molecular Imaging 2022 (October 5, 2022): 1–6. http://dx.doi.org/10.1155/2022/5687245.
Full textAbstract:
Lung cancer in its occurrence and development of different stages exist different biological behavior changes. This paper studies the expression of heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1 in benign and malignant lung lesions and its early diagnosis value of nonsmall-cell lung cancer (NSCLC), aiming to provide reference for the early diagnosis and therapy of NSCLC. Some lung surgery specimens are selected from January 2021 to March 2022. All cases received no radiotherapy and chemotherapy before surgery, including 90 sufferers with benign lung lesions as the contrast set. hnRNP A2/B1 expressions are measured for comparison. The experimental results show that for lung cancer sufferers, the positive expression of hnRNP A2/B1 in their malignant lesion tissue is notoriously higher than that in their benign lesion tissue, and hnRNP A2/B1 is differently expressed in different differentiation and in different stages.
4
Maslyanskiy, Aleksey, Natalya Lazareva, Polina Olinek, et al. "Anti-hnRNP B1 (RA33) Autoantibodies Are Associated with the Clinical Phenotype in Russian Patients with Rheumatoid Arthritis and Systemic Sclerosis." Journal of Immunology Research 2014 (2014): 1–7. http://dx.doi.org/10.1155/2014/516593.
Full textAbstract:
Heterogeneous nuclear ribonucleoproteins (hnRNPs) are potent autoantigenic targets in systemic autoimmune rheumatic diseases (SARD). Loss of tolerance to the RA33 complex consisting of hnRNP A2 and its alternatively spliced variants B1 and B2 has been the interest of rheumatologists. A novel ELISA for the detection of anti-hnRNP B1 autoantibodies has been developed to investigate the prevalence thereof in 397 patients with SARD, including patients with rheumatoid arthritis (RA), spondyloarthropathy (SPA), juvenile chronic arthritis, systemic lupus erythematosus (SLE), systemic sclerosis (SSc), and Sjögren’s syndrome (SS), in comparison to 174 controls. Anti-hnRNP B1 autoantibodies were significantly more prevalent in patients with SARD than controls (47/397, 11.8% versus 2/174, 1.1%;P<0.001). In particular, anti-hnRNP B1 were found more frequently in the disease cohorts than in the controls and were present in 24/165 (14.5%) patients with RA, 6/58 (10.3%) SPA, 11/65 (16.9%) SSc, and 4/50 (8.0%) SLE. In RA patients, anti-hnRNP B1 autoantibodies correlated significantly with C-reactive protein levels and erythrocyte sedimentation rate, while in patients with SSc it was associated with features of arterial wall stiffness and presence of hypertension. Anti-hnRNP B1 autoantibodies occur in SARD and seem to be correlated with distinct clinical characteristics in patients with RA and SSc.
5
Hernández-Díaz, Iván, Teresa Giraldez, Silvia Morales, et al. "Heterogeneous nuclear ribonucleoprotein A2/B1 is a tissue-specific aldosterone target gene with prominent induction in the rat distal colon." American Journal of Physiology-Gastrointestinal and Liver Physiology 304, no. 2 (2013): G122—G131. http://dx.doi.org/10.1152/ajpgi.00130.2012.
Full textAbstract:
The steroid hormone aldosterone enhances transepithelial Na+ reabsorption in tight epithelia and is crucial to achieve extracellular volume homeostasis and control of blood pressure. One of the main transport pathways regulated by aldosterone involves the epithelial Na+ channel (ENaC), which constitutes the rate-limiting step of Na+ reabsorption in parts of the distal nephron and the collecting duct, the distal colon, and sweat and salivary glands. Although these epithelial tissues share the same receptor for aldosterone (mineralocorticoid receptor, MR), and the same transport system (ENaC), it has become clear that the molecular mechanisms involved in the modulation of channel activity are tissue-specific. Recent evidence suggests that aldosterone controls transcription and also translation of ENaC subunits in some cell types. A possible pathway for translational regulation is binding of regulatory proteins to ENaC subunit mRNAs, such as the heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1). In this study, we examined whether hnRNP A2/B1 is an aldosterone-target gene in vivo. Our data show that physiological levels of aldosterone markedly induce hnRNP A2/B1 expression in an early and sustained manner in the late distal colon epithelium but not in other aldosterone-target tissues. The effect depends on MR but not on glucocorticoid receptor activity. We also demonstrate that the genomic region upstream of hnRNP A2/B1 contains aldosterone-responsive elements involved in the control of gene expression. We hypothesize that hnRNP A2/B1 is involved in the tissue-specific regulation of ENaC biosynthesis and may coordinate the response of other genes relevant for transepithelial Na+ reabsorption by aldosterone.
6
Bozinovic, Ksenija, Taghi Manshouri, Sean M. Post, et al. "Altered Expression and Mutation Analysis Of Heterogeneous Nuclear Ribonucleoprotein k In Bone Marrow Of Primary Myelofibrosis Patients." Blood 122, no. 21 (2013): 5272. http://dx.doi.org/10.1182/blood.v122.21.5272.5272.
Full textAbstract:
Abstract The heterogeneous nuclear ribonucleoproteins (hnRNPs) are RNA/DNA-binding proteins that consist of several family members: A1, A2, B1, C2 and K. hnRNPs have been implicated in numerous cellular processes and when dysregulated, have been suggested to impact tumorigenesis. hnRNP A2/B1 is overexpressed in some lung cancers and has been suggested to be a useful early detection marker for lung carcinoma. hnRNP K has been reported to associate with colon cancer and directly interacts with DNA, RNA, and proteins to regulate gene expression in numerous cellular processes involved in mitogenic responses and tumorigenesis. Loss of hnRNP K expression results in defects in differentiation and apoptosis, and increased hnRNP K expression has been associated with loss of apoptosis and an increase in cellular proliferation. To explore the possibility of altered hnRNP K expression or mutations in primary myelofibrosis, we isolated mRNA from primary blood or bone marrow mononuclear cells from patients with myelofibrosis (n=62) and healthy controls (n=19). We examined hnRNP K levels and determined that hnRNP K is significantly overexpressed in myelofibrosis (p= <0.0001). Sequencing of the hnRNP K locus revealed a single nucleotide alteration (A-to-G) one allele of intron 5 in 43% of myelofibrosis patients (n= 21) In contrast, only one out of 11 control samples harbored this alteration ((x2 p = 0.05). At present, we are investigating whether G allele is a mutation or a SNP. Furthermore, western blotting indicates an increase in phosphorylation of serine-248 in myelofibrosis patients. Together, these data suggest altered hnRNP K expression and mutations in myelofibrosis that might play a significant role in myeloproliferation and hematopoietic differentiation in myelofibrosis patients. Given the significant impact that hematopoietic differentiation has on leukemogenesis, it is imperative to decipher Disclosures: No relevant conflicts of interest to declare.
7
Jung, Youngseob, Ji-Young Seo, Hye Guk Ryu, Do-Yeon Kim, Kyung-Ha Lee, and Kyong-Tai Kim. "BDNF-induced local translation of GluA1 is regulated by HNRNP A2/B1." Science Advances 6, no. 47 (2020): eabd2163. http://dx.doi.org/10.1126/sciadv.abd2163.
Full textAbstract:
The AMPA receptor subunit GluA1 is essential for induction of synaptic plasticity. While various regulatory mechanisms of AMPA receptor expression have been identified, the underlying mechanisms of GluA1 protein synthesis are not fully understood. In neurons, axonal and dendritic mRNAs have been reported to be translated in a cap-independent manner. However, molecular mechanisms of cap-independent translation of synaptic mRNAs remain largely unknown. Here, we show that GluA1 mRNA contains an internal ribosome entry site (IRES) in the 5′UTR. We also demonstrate that heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1 interacts with GluA1 mRNA and mediates internal initiation of GluA1. Brain-derived neurotrophic factor (BDNF) stimulation increases IRES-mediated GluA1 translation via up-regulation of HNRNP A2/B1. Moreover, BDNF-induced GluA1 expression and dendritic spine density were significantly decreased in neurons lacking hnRNP A2/B1. Together, our data demonstrate that IRES-mediated translation of GluA1 mRNA is a previously unidentified feature of local expression of the AMPA receptor.
8
Barnett, S. F., T. A. Theiry, and W. M. LeStourgeon. "The core proteins A2 and B1 exist as (A2)3B1 tetramers in 40S nuclear ribonucleoprotein particles." Molecular and Cellular Biology 11, no. 2 (1991): 864–71. http://dx.doi.org/10.1128/mcb.11.2.864-871.1991.
Full textAbstract:
The six "core" proteins of HeLa cell 40S nuclear ribonucleoprotein particles (hnRNP particles) package 700-nucleotide lengths of pre-mRNA into a repeating array of regular particles. We have previously shown that the C proteins exist as anisotropic tetramers of (C1)3C2 in 40S hnRNP particles and that each particle probably contains three such tetramers. We report here that proteins A2 and B1 also exist in monoparticles as (A2)3B1 tetramers and that each monoparticle contains at least three such tetramers. Proteins A2 and B1 dissociate from isolated monoparticles as a stable tetramer upon nuclease digestion. In low-salt gradients, the tetramers sediment at 6.8S, which is consistent with a mass of 145 kDa. In 200 mM salt, the concentration which dissociates these proteins from RNA, only 4.2S dimers exist in solution. Tetramers of (A2)3B1 possess the ability to package multiples of 700 nucleotides of RNA in vitro into an array of regular, 22.5-nm 43S particles. Unlike the in vitro assembly of intact 40S hnRNP, the (A2)3B1 tetramers assemble by means of a highly cooperative process. These findings indicate that the (A2)3B1 tetramers play a major role in hnRNP assembly and they further support the contention that 40S monoparticles are regular structures composed of three copies of three different tetramers, i.e., 3[(A1)3B2, (A2)3B1, (C1)3C2].
9
Barnett, S. F., T. A. Theiry, and W. M. LeStourgeon. "The core proteins A2 and B1 exist as (A2)3B1 tetramers in 40S nuclear ribonucleoprotein particles." Molecular and Cellular Biology 11, no. 2 (1991): 864–71. http://dx.doi.org/10.1128/mcb.11.2.864.
Full textAbstract:
The six "core" proteins of HeLa cell 40S nuclear ribonucleoprotein particles (hnRNP particles) package 700-nucleotide lengths of pre-mRNA into a repeating array of regular particles. We have previously shown that the C proteins exist as anisotropic tetramers of (C1)3C2 in 40S hnRNP particles and that each particle probably contains three such tetramers. We report here that proteins A2 and B1 also exist in monoparticles as (A2)3B1 tetramers and that each monoparticle contains at least three such tetramers. Proteins A2 and B1 dissociate from isolated monoparticles as a stable tetramer upon nuclease digestion. In low-salt gradients, the tetramers sediment at 6.8S, which is consistent with a mass of 145 kDa. In 200 mM salt, the concentration which dissociates these proteins from RNA, only 4.2S dimers exist in solution. Tetramers of (A2)3B1 possess the ability to package multiples of 700 nucleotides of RNA in vitro into an array of regular, 22.5-nm 43S particles. Unlike the in vitro assembly of intact 40S hnRNP, the (A2)3B1 tetramers assemble by means of a highly cooperative process. These findings indicate that the (A2)3B1 tetramers play a major role in hnRNP assembly and they further support the contention that 40S monoparticles are regular structures composed of three copies of three different tetramers, i.e., 3[(A1)3B2, (A2)3B1, (C1)3C2].
10
Zech, Veronika F. E., Margit Dlaska, Alexandar Tzankov, and Wolfgang Hilbe. "Prognostic and diagnostic relevance of hnRNP A2/B1, hnRNP B1 and S100 A2 in non-small cell lung cancer." Cancer Detection and Prevention 30, no. 5 (2006): 395–402. http://dx.doi.org/10.1016/j.cdp.2006.04.009.
Full textDissertations / Theses on the topic "HnRNP A2/B1"
1
Peebles, Katherine Anne. "HnRNP A2/B1 expression in neoplastic mouse lung cells /." Connect to full text via ProQuest. IP filtered, 2005.
Find full textAbstract:
Thesis (Ph.D. in Pharmaceutical Sciences) -- University of Colorado at Denver and Health Sciences Center, 2005.<br>Typescript. Includes bibliographical references (leaves 153-171). Free to UCDHSC affiliates. Online version available via ProQuest Digital Dissertations;
2
Griffith, Brian Nelson. "Differential binding of hnRNP K, L and A2/B1 to an exonic splicing silencer element located within exon 12 of glucose-6-phosphate dehydrogenase mRNA." Morgantown, W. Va. : [West Virginia University Libraries], 2006. https://eidr.wvu.edu/etd/documentdata.eTD?documentid=4811.
Full textAbstract:
Thesis (Ph. D.)--West Virginia University, 2006.<br>Title from document title page. Document formatted into pages; contains xi, 183 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
3
Nai-JhuDing and 丁乃筑. "Studying the role of hnRNP Q1 and hnRNP A2/B1 in Aurora-A translation." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/74480634540075209707.
Full textAbstract:
碩士<br>國立成功大學<br>生物資訊與訊息傳遞研究所<br>100<br>Aurora-A is a serine/threonine kinase that involved in centrosome maturation, mitotic entry, spindle assembly and chromosome segregation. Dysregulation of Aurora-A results in centrosome amplification, cytokinesis failure, aneuploidy, and finally leads to tumor formation. It was reported that Aurora-A is overexpressed in a lot of cancers. Our previously studies indicated that EGF can translational up-regulate the expression of Aurora-A through a specific 5’-untranslated region (5’UTR). In addition, hnRNP Q1 and hnRNP A2/B1 may participate the translational regulation of Aurora-A mRNA. In this study, we investigate the role of hnRNP Q1 and hnRNP A2/B1 in translational regulating Aurora-A. The expression pattern of Aurora-A mRNA isoforms in human colorectal cancer was firstly confirmed by real-time PCR. In vivo translation assay and ribosomal protein S6-immunoprecipitation assay showed that hnRNP Q1 can increase the translation efficiency of Aurora-A, however hnRNP A2/B1 plays an opposite role. The biotin pull-down assay indicates hnRNP Q1 and hnRNP A2/B1 prefers to interact with different region of Aurora-A 5’UTR. BIAcore assay confirmed the Aurora-A 5’UTR-binding domain of hnRNP Q1. The expression of Aurora-A and hnRNP Q presents a positive correlation in clinical human colorectal cancer specimens by RT-PCR analysis. Taken together, our results suggest that hnNRP Q1 and hnRNP A2/B1 may translationally regulate Aurora-A mRNA through its 5’UTR.
4
Leal, Graciano. "Regulation of hnRNP A2/B1 and hnRNP K by synaptic activity and BDNF in the hippocampus." Doctoral thesis, 2014. http://hdl.handle.net/10316/24128.
Full textAbstract:
Tese de doutoramento em Biociências, apresentada à Faculdade de Ciências e Tecnologia da Universidade de Coimbra<br>Synaptic plasticity describes the process by which connections between neurons, or synapses, change in strength. By definition, it is a functional term referring to an increase or decrease in synaptic efficacy, which is accompanied by structural changes at synapses.Long-term potentiation (LTP) is the most studied form of synaptic plasticity and it has been widely recognized that synaptic changes that underpin certain forms of learning and memory may be similar to those involved in the expression of LTP.
Some of the structural, biochemical and functional modifications at the synapse associated with synaptic plasticity require activity-dependent transport and translation of dendritic-localized mRNAs, with concomitant alterations in the synaptic proteome. It is becoming evident that dendritic protein synthesis has a crucial role in several forms of synaptic plasticity, including brain-derived neurotrophic factor (BDNF)-mediated LTP. Dendritic transcripts required for local protein synthesis are transported in a repressed state along the microtubule cytoskeleton as components of large messenger ribonucleoprotein complexes (mRNPs). In order to be transported, dendritic mRNAs must contain a cis-acting element in their sequence that is recognized by specific RNA binding proteins that, together with other factors, form a functional mRNP granule that engage with motor proteins for the transport. When they reach their destination, usually in, or in the vicinity of activated synapses, the translational-block is relieved and the mRNAs are translated upon neuronal activation. Among the molecular components of neuronal mRNPs, there are several members of the heterogeneous nuclear ribonucleoprotein (hnRNP) family of proteins. hnRNP A2/B1 is one of the best described trans-acting factor involved in the transport of dendritic-localized mRNAs in neurons, but whether this is a constitutive or a regulated process is unknown. hnRNP K is another member of the hnRNP family of proteins present in neuronal mRNPs, but the function of hnRNP K in neurons, and whether this protein plays a role in dendritic mRNA metabolism, remains to be determined.
Here we show that both hnRNP A2/B1 and hnRNP K accumulate in dendrites and at the synapse following neuronal activation in hippocampal neurons. Importantly, the activity-dependent delivery of hnRNP A2/B1 into synaptic sites requires BDNF. In addition, we observed that this neurotrophin also upregulates the dendritic and synaptic levels of hnRNP K and hnRNP A2/B1 in primary cultures of hippocampal neurons.
Previous studies from our laboratory identified several transcripts associated with hnRNP K in cultured hippocampal neurons, including mRNAs coding for proteins with roles in synaptic plasticity such as GluA1, GluN1, BDNF and CaMKIIẞ. In addition, we demonstrated that the neurotrophin BDNF induces the release of these transcripts from the hnRNPK-containing mRNPs in hippocampal neurons. Herein we show that BDNF also promotes the dissociation of hnRNPK-bound mRNAs locally at the synapse. These results suggest a key role for hnRNP K in the local translation of several proteins that contribute to the late phase of LTP. Accordingly, we demonstrate that hnRNP K-associated mRNAs are differentially regulated during high-frequency stimulation (HFS)-induced LTP in the perforant path-dentate gyrus synapse in live anesthetized rats. Importantly, we show that this form of synaptic potentiation requires TrkB (tropomyosin-related kinase B) signaling. Although our results indicate that BDNF induces the release of the transcripts bound to mRNPs containing hnRNP K, at this time point it is not possible to rule out the contribution of other RNA-binding proteins that were found to co-immunoprecipitate with hnRNP K in a proteomic screen.
Altogether, our data support the evidence available pointing to a prominent role of hnRNP A2/B1 in the delivery of transcripts into dendritic domains and suggest that this process is regulated by synaptic activity and by the neurotrophin BDNF. Furthermore, we show that BDNF is required for the activity-induced synaptic delivery of hnRNP A2/B1. We also show that hnRNP K is another hnRNP that is likely to have a major role in the regulation of local mRNA metabolism in dendrites. Ourresults show that hnRNP K and hnRNP K-associated mRNAs are regulated by synaptic activity and BDNF, both in vitro and in vivo,and suggest hnRNP K as an important regulator of neuronal function, in particularin BDNF-induced plasticity events.<br>A plasticidade sináptica descreve um processo no qual a força da interacção entre neurónios, ou sinapses, é alterada. Por definição, é um termo funcional que se refere ao aumento ou decréscimo na eficácia sináptica, sendo acompanhado por alterações estruturais nas sinapses.A potenciação sináptica de longa duração (LTP) é a forma mais estudada de plasticidade sináptica e tem sido amplamente reconhecido que as alterações sinápticas responsáveis por certas formas de aprendizagem e memória podem ser semelhantes aquelas em que a expressão da LTP se baseia.
Algumas das modificações estruturais, bioquímicas e funcionais nas sinapses associadas à plasticidade sináptica dependem do transporte e da tradução de RNAs mensageiros (mRNAs) localizados nas dendrites, em resposta à actividade sináptica, com a concomitante alteração local do proteoma. É cada vez mais evidente que a síntese de proteínas nas dendrites desempenha um papel crucial em diversas formas de plasticidade sináptica, incluindo na potenciação de longa duração mediada pelo BDNF (factor neurotrófico derivado do cérebro).
Os transcritos dendríticos são transportados ao longo dos microtúbulos, numa forma em que a tradução está bloqueada, como componentes de complexos ribonucleoproteicos mensageiros (mRNPs). Para serem transportados, os mRNAs necessitam de conter na sua sequência um elemento cis-acting que é reconhecido por proteínas que ligam RNA e que, juntamente com outros factores, formam um complexo funcional que se liga a proteínas motoras para o transporte. Quando chegam ao seu destino, normalmente em sinapses ou na imediação de sinapses activadas, o bloqueio da tradução é libertado e os mRNAs são traduzidos após activação neuronal. Entre os constituintes moleculares que compõem os mRNPs em neurónios estão vários membros da família de proteínas hnRNP (ribonucleoproteinas nucleares heterogéneas).A proteína hnRNP A2/B1 é um dos mais bem descritos factores trans-acting envolvidos no transporte de mRNAs ao longo das dendrites em neurónios, contudo não se sabe se este é um processo constitutivo ou regulado. A hnRNP K também está presente em mRNPs em neurónios mas a sua função, e se desempenha algum papel no metabolismo de mRNAs nas dendrites, ainda está por determinar.
Neste trabalho mostramos que tanto a hnRNP A2/B1 como a hnRNP K se acumulam nas dendrites e nas sinapses após actividade sináptica em neurónios do hipocampo em cultura. Verificou-se também que o endereçamento de hnRNP A2/B1 para a sinapse em resposta à actividade neuronal depende de BDNF. De acordo com estes resultados, a estimulação de neurónios do hipocampo com BDNF também aumentou os níveis de hnRNP K e hnRNP A2/B1 nas dendrites e nas sinapses.
Estudos anteriores realizados no nosso laboratório identificaram diversos transcritos associados com a hnRNP K em neurónios do hipocampo, incluindo mRNAs que codificam proteínas importantes para a plasticidade sináptica como GluA1, GluN1, BDNF e CaMKIIẞ. De seguida verificou-se também que a neurotrofina BDNF induz a libertação desses transcritos de mRNPs que contêm hnRNP K em neurónios do hipocampo. Neste trabalho mostrámos que o BDNF também promove a dissociação dos mRNAs associados à hnRNP K localmente na sinapse. Estes resultados sugerem um papel fundamental da hnRNP K na tradução local de várias proteínas que contribuem para a fase tardia da LTP. De acordo com estas evidências experimentais, demonstrámos que os mRNAs associados à hnRNP K são regulados diferencialmente durante a potenciação de longa duração (LTP) induzida pela estimulação de alta frequência nas sinapses da via perforante-giro dentado em ratos vivos anestesiados. Demonstrámos também que esta forma de potenciação sináptica requer a activação dos receptores TrkB. Apesar de os resultados obtidos indicarem que o BDNF induz a libertação dos transcritos associados a mRNPs contendo a hnRNP K, não é possível excluir a contribuição de outras ribonucleoproteínas que co-imunoprecipitaram com a hnRNP K num estudo de proteómica efectuado.
No seu conjunto, os resultados obtidos apoiam o modelo que propõe uma função para a hnRNP A2/B1 na entrega de transcritos em regiões específicas das dendrites e sugerem que este é um processo regulado pela actividade sináptica e pelo BDNF. Demonstrámos também que a acumulação de hnRNP A2/B1 na sinapse após actividade sináptica depende de BDNF. A hnRNP K é outra hnRNP que parece desempenhar um papel crucial na regulação do metabolismo do mRNA localmente nas dendrites. Os nossos resultados demonstram que a interacção entre a hnRNP K e os mRNAs a ela associados é regulada pela actividade sináptica e pelo BDNF, tanto in vitro como in vivo, o que sugere a hnRNP K como um importante regulador da função neuronal, em particular em fenómenos de plasticidade sináptica induzidos pelo BDNF.
5
Wang, Hsin Ju, and 王馨茹. "Investigation of the role of NP in hnRNP A2/B1-mediated miRNA biogenesis." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/74580343168277538398.
Full textAbstract:
碩士<br>長庚大學<br>醫學生物技術暨檢驗學系<br>102<br>Influenza A virus infection frequently causes respiratory disease. Our research group observed that NP can interact directly with a glycine- rich motif of heterogeneous nuclear ribonucleoproteins (hnRNP A2/B1). In addition, NP and hnRNP A2/B1 colocalize in the nuclei of virus-infected cells early in the infection process. The RNA recognition motif of hnRNP A2/B1 exhibits greater than 80% similarity with hnRNP A1, which can modulate miRNA biogenesis. A previous study indicated that hnRNP A2/B1 can interact with the terminal loop of miR-7-1. Another research demonstrated that miR-7-1 positively regulate virus replication by targeting immune genes. In view of previous researches, we predicted NP modulated miRNA by interacting with hnRNP A2/B1. Thus, we chose miR-7-1 as our taget based on previous reports. Our research indicated that： (1) hnRNP A2/B1 may positively regulate
miR-7-1 biogenesis. MiR-7-1 will decrease when knockdown hnRNP A2/B1, and miR-7-1 will increase when over express hnRNP A2/B1. (2) NP may positively regulate miR-7-1 through hnRNP A2/B1. A pri-miR-7-1 RNA pull-down assay revealed that NP and hnRNP A2/B1 were enhanced as the NP-Flag plasmid expressed. (3) hnRNP A2/B1 may positively regulate miR-7-1 in A/WSN/33 virus-infected cell. MiR-7-1 decreased when hnRNP A2/B1-inhibited A549 cells were infected with A/WSN/33.
6
Chang, Cheng Kai, and 張程凱. "Interaction of influenza viral nucleoprotein with hnRNP A2/B1 and its impacts on viral replication." Thesis, 2018. http://ndltd.ncl.edu.tw/handle/484y48.
Full textAbstract:
博士<br>長庚大學<br>生物醫學研究所<br>106<br>Viral host interaction contributes to both viral replication and host defense mechanisms during infection. A cellular protein, heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1, was found to interact with influenza A virus NP protein by antibody precipitation assay and MALDI-TOF identification. The interaction was further confirmed by means of co-immunoprecipitation. In vitro binding assay using a series of truncated forms of hnRNP A2 recombinant proteins revealed that glycine-rich domain (GRD) in C-terminus of hnRNP A2 was responsible for the interaction. In vivo immunoprecipitation assay also demonstrated F412 and R422 residues and tail loop domain of NP contributed to the interaction between NP and hnRNP A2/B1. hnRNP A2/B1 was found colocalized with NP in the nuclei of virus-infected cells at 4-6 hrs post-infection under confocal microscopy. Influenza viral RNP activity decreased in hnRNP A2/B1 silence cell which means hnRNP A2/B1 play as a positive regulator for viral RNA replication. This finding demonstrated cellular protein hnRNP A2/B1 can modulate viral RNA synthesis through binding to influenza viral protein NP.
Book chapters on the topic "HnRNP A2/B1"
1
Tockman, Melvyn S., Tatyana A. Zhukov, Yener S. Erozan, William H. Westra, Jun Zhou, and James L. Mulshine. "Antigen Retrieval Improves hnRNP A2/B1 Immunohistochemical Localization in Premalignant Lesions of the Lung." In Clinical and Biological Basis of Lung Cancer Prevention. Birkhäuser Basel, 1998. http://dx.doi.org/10.1007/978-3-0348-8924-7_21.
Full textConference papers on the topic "HnRNP A2/B1"
1
Tauler, Jordi, Jessica Siegler, Xiaoguang Sun, Liliana Moreno-Vinasco, and Joe GN Garcia. "Abstract 352: hnRNP A2/B1 regulates S1PR3 expression in lung cancer." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-352.
Full text
2
Fritsch, R., D. Eselboeck, B. Jahn-Schmid, et al. "FRI0086 Characterisation of ra33 (hnrnp-a2/b1)- autoreactive t cells in sle-patients." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.1228.
Full text
3
Vasiljevic, J., C. Niehage, D. Vasiljevic та ін. "hnRNP A2/B1 as a novel post-transcriptional regulator of insulin expression in β-cells". У Diabetes Kongress 2018 – 53. Jahrestagung der DDG. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1641820.
Full text
4
Sieghart, D., P. Studenic, M. Grundhuber, et al. "P006 ANTI-RA33 (HNRNP-A2/B1) autoantibodies are associated with the therapeutic response to methotrexate in patients with rheumatoid arthritis." In 38th European Workshop for Rheumatology Research, 22–24 February 2018, Geneva, Switzerland. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-ewrr2018.32.
Full text