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Journal articles on the topic 'HnRNP A2/B1'

Author: Grafiati

Published: 4 September 2021

Last updated: 21 June 2025

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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].

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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.

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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].

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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.

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11

Satoh, H., H. Ishikawa, H. Kamma, Y. T. Yamashita, and K. Sekizawa. "HnRNP A2/B1 Proteins in Nontumorous Alveolar Cells." Lung 181, no. 4 (2003): 219–25. http://dx.doi.org/10.1007/s00408-003-1024-z.

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12

Coppola, Antonina, Patrizia Cancemi, Laura Tomasello, et al. "Anti-Inflammatory Action of Heterogeneous Nuclear Ribonucleoprotein A2/B1 in Patients with Autoimmune Endocrine Disorders." Journal of Clinical Medicine 9, no. 1 (2019): 9. http://dx.doi.org/10.3390/jcm9010009.

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Our previous studies documented that human fibroblast-limbal stem cells (f-LSCs) possess immunosuppressive capabilities, playing a role in regulating T-cell activity. This study highlights the molecular activities by which human f-LSCs can attenuate the inflammatory responses of self-reactive peripheral blood mononuclear cells (PBMCs) collected from patients with autoimmune endocrine diseases (AEDs). Anti-CD3 activated PBMCs from twenty healthy donors and fifty-two patients with AEDs were cocultured on f-LSC monolayer. 2D-DIGE proteomic experiments, mass spectrometry sequencing and functional in vitro assays were assessed in cocultured PBMCs. We identified the downmodulation of several human heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1) isoforms in healthy and AED activated PBMCs upon f-LSC interaction. The reduction of hnRNPA2/B1 protein expression largely affected the cycling ki67+, CD25+, PD-1+ reactive cells and the double marked CD8+/hnRNPA2B1+ T cell subset. Anti-PD1 blocking experiments evoked hnRNPA2/B1 overexpression, attributing putative activation function to the protein. hnRNPA2/B2 transient silencing inverted immunopolarization of the self-reactive PBMCs from AEDs toward a M2/Th2-type background. Pharmacological inhibition and co-immunoprecipitation experiments demonstrated the involvement of NF-ĸB in hnRNPA2/B activity and turnover. Our data indicate cardinal involvement of hnRNP A2/B1 protein in peripheral mechanisms of tolerance restoration and attenuation of inflammation, identifying a novel immunoplayer potentially targetable in all AEDs.

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Ishikawa, F., M. J. Matunis, G. Dreyfuss, and T. R. Cech. "Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n." Molecular and Cellular Biology 13, no. 7 (1993): 4301–10. http://dx.doi.org/10.1128/mcb.13.7.4301-4310.1993.

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HeLa cell nuclear proteins that bind to single-stranded d(TTAGGG)n, the human telomeric DNA repeat, were identified and purified by a gel retardation assay. Immunological data and peptide sequencing experiments indicated that the purified proteins were identical or closely related to the heterogeneous nuclear ribonucleoproteins (hnRNPs) A1, A2-B1, D, and E and to nucleolin. These proteins bound to RNA oligonucleotides having r(UUAGGG) repeats more tightly than to DNA of the same sequence. The binding was sequence specific, as point mutation of any of the first 4 bases [r(UUAG)] abolished it. The fraction containing D and E hnRNPs was shown to bind specifically to a synthetic oligoribonucleotide having the 3' splice site sequence of the human beta-globin intervening sequence 1, which includes the sequence UUAGG. Proteins in this fraction were further identified by two-dimensional gel electrophoresis as D01, D02, D1*, and E0; intriguingly, these members of the hnRNP D and E groups are nuclear proteins that are not stably associated with hnRNP complexes. These studies establish the binding specificities of these D and E hnRNPs. Furthermore, they suggest the possibility that these hnRNPs could perhaps bind to chromosome telomeres, in addition to having a role in pre-mRNA metabolism.

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Ishikawa, F., M. J. Matunis, G. Dreyfuss, and T. R. Cech. "Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n." Molecular and Cellular Biology 13, no. 7 (1993): 4301–10. http://dx.doi.org/10.1128/mcb.13.7.4301.

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HeLa cell nuclear proteins that bind to single-stranded d(TTAGGG)n, the human telomeric DNA repeat, were identified and purified by a gel retardation assay. Immunological data and peptide sequencing experiments indicated that the purified proteins were identical or closely related to the heterogeneous nuclear ribonucleoproteins (hnRNPs) A1, A2-B1, D, and E and to nucleolin. These proteins bound to RNA oligonucleotides having r(UUAGGG) repeats more tightly than to DNA of the same sequence. The binding was sequence specific, as point mutation of any of the first 4 bases [r(UUAG)] abolished it. The fraction containing D and E hnRNPs was shown to bind specifically to a synthetic oligoribonucleotide having the 3' splice site sequence of the human beta-globin intervening sequence 1, which includes the sequence UUAGG. Proteins in this fraction were further identified by two-dimensional gel electrophoresis as D01, D02, D1*, and E0; intriguingly, these members of the hnRNP D and E groups are nuclear proteins that are not stably associated with hnRNP complexes. These studies establish the binding specificities of these D and E hnRNPs. Furthermore, they suggest the possibility that these hnRNPs could perhaps bind to chromosome telomeres, in addition to having a role in pre-mRNA metabolism.

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15

Somberg, Monika, Xiaomin Zhao, Monika Fröhlich, Magnus Evander, and Stefan Schwartz. "Polypyrimidine Tract Binding Protein Induces Human Papillomavirus Type 16 Late Gene Expression by Interfering with Splicing Inhibitory Elements at the Major Late 5′ Splice Site, SD3632." Journal of Virology 82, no. 7 (2008): 3665–78. http://dx.doi.org/10.1128/jvi.02140-07.

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ABSTRACT We have initiated a screen for cellular factors that can induce human papillomavirus type 16 (HPV-16) late gene expression in human cancer cells. We report that the overexpression of polypyrimidine tract binding protein (PTB), also known as heterologous nuclear ribonucleoprotein I (hnRNP I), induces HPV-16 late gene expression in cells transfected with subgenomic HPV-16 plasmids or with full-length HPV-16 genomes and in persistently HPV-16-infected cells. In contrast, other hnRNPs such as hnRNP B1/A2, hnRNP F, and hnRNP Q do not induce HPV-16 late gene expression. PTB activates SD3632, the only 5′ splice site on the HPV-16 genome that is used exclusively by late mRNAs. PTB interferes with splicing inhibitory sequences located immediately upstream and downstream of SD3632, thereby activating late gene expression. One AU-rich PTB-responsive element was mapped to a 198-nucleotide sequence located downstream of SD3632. The deletion of this element induced HPV-16 late gene expression in the absence of PTB. Our results suggest that the overexpression of PTB interferes with cellular factors that interact with the inhibitory sequences. One may speculate that an increase in PTB levels or a reduction in the concentration of a PTB antagonist is required for the activation of HPV-16 late gene expression during the viral life cycle.

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Liu, Ting-Yuan, Yu-Chia Chen, Yuh-Jyh Jong, et al. "Muscle developmental defects in heterogeneous nuclear Ribonucleoprotein A1 knockout mice." Open Biology 7, no. 1 (2017): 160303. http://dx.doi.org/10.1098/rsob.160303.

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Heterogeneous ribonucleoprotein A1 (hnRNP A1) is crucial for regulating alternative splicing. Its integrated function within an organism has not, however, been identified. We generated hnRNP A1 knockout mice to study the role of hnRNP A1 in vivo . The knockout mice, hnRNP A1 −/− , showed embryonic lethality because of muscle developmental defects. The blood pressure and heart rate of the heterozygous mice were higher than those of the wild-type mice, indicating heart function defects. We performed mouse exon arrays to study the muscle development mechanism. The processes regulated by hnRNP A1 included cell adhesion and muscle contraction. The expression levels of muscle development-related genes in hnRNP A1 +/− mice were significantly different from those in wild-type mice, as detected using qRT-PCR. We further confirmed the alternative splicing patterns of muscle development-related genes including mef2c , lrrfip1 , usp28 and abcc9 . Alternative mRNA isoforms of these genes were increased in hnRNP A1 +/− mice compared with wild-type mice. Furthermore, we revealed that the functionally similar hnRNP A2/B1 did not compensate for the expression of hnRNP A1 in organisms. In summary, our study demonstrated that hnRNP A1 plays a critical and irreplaceable role in embryonic muscle development by regulating the expression and alternative splicing of muscle-related genes.

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Han, Siew Ping, Lexie R. Friend, John H. Carson, et al. "Differential Subcellular Distributions and Trafficking Functions of hnRNP A2/B1 Spliceoforms." Traffic 11, no. 7 (2010): 886–98. http://dx.doi.org/10.1111/j.1600-0854.2010.01072.x.

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Thibault, Patricia A., Aravindhan Ganesan, Subha Kalyaanamoorthy, Joseph-Patrick W. E. Clarke, Hannah E. Salapa, and Michael C. Levin. "hnRNP A/B Proteins: An Encyclopedic Assessment of Their Roles in Homeostasis and Disease." Biology 10, no. 8 (2021): 712. http://dx.doi.org/10.3390/biology10080712.

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: The hnRNP A/B family of proteins is canonically central to cellular RNA metabolism, but due to their highly conserved nature, the functional differences between hnRNP A1, A2/B1, A0, and A3 are often overlooked. In this review, we explore and identify the shared and disparate homeostatic and disease-related functions of the hnRNP A/B family proteins, highlighting areas where the proteins have not been clearly differentiated. Herein, we provide a comprehensive assembly of the literature on these proteins. We find that there are critical gaps in our grasp of A/B proteins’ alternative splice isoforms, structures, regulation, and tissue and cell-type-specific functions, and propose that future mechanistic research integrating multiple A/B proteins will significantly improve our understanding of how this essential protein family contributes to cell homeostasis and disease.

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Huang, Yan, Jingjing Chen, Juan Pan, et al. "A2/B1 Promotes NRF2 mRNA Stability and Inhibits Ferroptosis and Cell Proliferation in Breast Cancer Cells." BioMed Research International 2023 (April 14, 2023): 1–12. http://dx.doi.org/10.1155/2023/2620738.

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Breast cancer is a highly harmful malignant tumor, which poses a great threat to women’s body and mind, and the mortality rate ranks second among all women’s diseases. The incidence rate accounts for 7-10% of various malignant tumors in the whole body, second only to uterine cancer in women, and has become the main cause of threatening women’s health. Advanced breast cancer is often considered an incurable disease. The family of heterogeneous nuclear ribonucleoprotein complexes is composed of about 20 hnRNP proteins with molecular weights ranging from 32 to 120 kDa, and they are named according to their molecular weights. Among them, hnRNPA2 and hnRNPB1 are the two most important members of the hnRNP family, both derived from the same gene on chromosome 7p15. Therefore, research to understand the molecular mechanism and process of breast cancer progression has an important role in promoting the current medical research on breast cancer treatment methods. Therefore, studying the mechanism of tumorigenesis is the key to tumor prevention and treatment. Therefore, this paper proposes that A2/B1 promotes the stability of NRF2 mRNA and inhibits ferroptosis and cell proliferation in breast cancer cells. The article mainly introduces the disease diagnosis method based on artificial neural network and its neural network algorithm. In the experimental part, the activity of hnRNP A2/B1 on cancer cells is deeply studied. The results show that the absorbance of the MTT method increases continuously with the extension of the culture time, and the maximum reaches 1.2. This fully shows that its absorption capacity is very strong, especially after 24 hours, the absorption rate rises from 0.6 to 0.9, which shows that 24 hours is the best absorption time. And it can also be found that hnRNPA2/B1 has a significant inhibitory effect on breast cancer cells; it can reduce the effect on breast cancer cell cycle and apoptosis.

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Nyhan, Michelle J., Shereen M. El Mashad, Tracey R. O’Donovan, et al. "VHLGenetic Alteration in CCRCC Does Not Determine De-Regulation of HIF, CAIX, hnRNP A2/B1 and Osteopontin." Analytical Cellular Pathology 33, no. 3-4 (2010): 121–32. http://dx.doi.org/10.1155/2010/562491.

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Background: von Hippel–Lindau (VHL) tumour suppressor gene inactivation is associated with clear cell renal cell carcinoma (CCRCC) development. The VHL protein (pVHL) has been proposed to regulate the expression of several proteins including Hypoxia Inducible Factor-α (HIF-α), carbonic anhydrase (CA)IX, heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1 and osteopontin. pVHL has been characterized in vitro, however, clinical studies are limited. We evaluated the impact of VHL genetic alterations on the expression of several pVHL protein targets in paired normal and tumor tissue.Methods: TheVHLgene was sequenced in 23 CCRCC patients andVHLtranscript levels were evaluated by real-time RT-PCR. Expression of pVHL’s protein targets were determined by Western blotting in 17 paired patient samples.Results: VHL genetic alterations were identified in 43.5% (10/23) of CCRCCs. HIF-1α, HIF-2α and CAIX were up-regulated in 88.2% (15/17), 100% (17/17) and 88.2% (15/17) of tumors respectively and their expression is independent ofVHLstatus. hnRNP A2/B1 and osteopontin expression was variable in CCRCCs and had no association withVHLgenetic status.Conclusion: As expression of these proposed pVHL targets can be achieved independently ofVHLmutation (and possibly by hypoxia alone), these data suggests that other pVHL targets may be more crucial in renal carcinogenesis.

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Garayoa, Mercedes, Yan-Gao Man, Alfredo Martínez, Frank Cuttitta, and James L. Mulshine. "Downregulation of hnRNP A2/B1 Expression in Tumor Cells under Prolonged Hypoxia." American Journal of Respiratory Cell and Molecular Biology 28, no. 1 (2003): 80–85. http://dx.doi.org/10.1165/rcmb.4880.

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McKay, Stewart J., and Howard Cooke. "hnRNP A2/B1 binds specifically to single stranded vertebrate telomeric repeat TTAGGGn." Nucleic Acids Research 20, no. 24 (1992): 6461–64. http://dx.doi.org/10.1093/nar/20.24.6461.

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Tauler, Jordi, Enrique Zudaire, Huaitian Liu, Joanna Shih, and James L. Mulshine. "hnRNP A2/B1 Modulates Epithelial-Mesenchymal Transition in Lung Cancer Cell Lines." Cancer Research 70, no. 18 (2010): 7137–47. http://dx.doi.org/10.1158/0008-5472.can-10-0860.

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Mizukami, Katsuyoshi, Hiroshi Kamma, Masanori Ishikawa, and Gideon Dreyfuss. "Immunohistochemical study of the hnRNP A2 and B1 in the rat forebrain." NeuroReport 11, no. 14 (2000): 3099–102. http://dx.doi.org/10.1097/00001756-200009280-00012.

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Liu, Yichen, Yan Gao, Yan Wu, Yonghong Wu, Hangyan Wang, and Chenggang Zhang. "Histochemical Mapping of hnRNP A2/B1 in Rat Brain After Ischemia–Reperfusion Insults." Journal of Histochemistry & Cytochemistry 58, no. 8 (2010): 695–705. http://dx.doi.org/10.1369/jhc.2010.955021.

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Nguyen, Eric D., Maggie M. Balas, April M. Griffin, Justin T. Roberts, and Aaron M. Johnson. "Global profiling of hnRNP A2/B1-RNA binding on chromatin highlights LncRNA interactions." RNA Biology 15, no. 7 (2018): 901–13. http://dx.doi.org/10.1080/15476286.2018.1474072.

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He, Fang, Amy Krans, Brian D. Freibaum, J. Paul Taylor, and Peter K. Todd. "TDP-43 suppresses CGG repeat-induced neurotoxicity through interactions with HnRNP A2/B1." Human Molecular Genetics 23, no. 19 (2014): 5036–51. http://dx.doi.org/10.1093/hmg/ddu216.

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Cho, See-Wun, Ken-ichi Suzuki, Yoshiaki Miura, et al. "Novel role of hnRNP-A2/B1 in modulating aryl hydrocarbon receptor ligand sensitivity." Archives of Toxicology 89, no. 11 (2014): 2027–38. http://dx.doi.org/10.1007/s00204-014-1352-1.

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DANGLI, Amalia, Angeliki PLOMARITOGLOU, Efrosini BOUTOU, Neratzoula VASSILIADOU, Haralampos M. MOUTSOPOULOS, and Apostolia GUIALIS. "Recognition of subsets of the mammalian A/B-type core heterogeneous nuclear ribonucleoprotein polypeptides by novel autoantibodies." Biochemical Journal 320, no. 3 (1996): 761–67. http://dx.doi.org/10.1042/bj3200761.

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The structurally related A/B-type core heterogeneous nuclear ribonucleoprotein (hnRNP) polypeptides of 34–39 kDa (A1, A2, B1 and B2) belong to a family of RNA-binding proteins that are major components of 40 S hnRNP complexes. By two-dimensional gel electrophoresis and peptide mapping analysis we compared each member of the A/B-type core proteins in the human and rat liver cells. This comparison revealed the unique presence in rat cells of major protein species, referred to as mBx polypeptides, that appeared as three charge isoforms at a position corresponding to the minor HeLa B1b protein spot. In addition, clear differences in the ratios of the A1 polypeptide to the A1b isoform were observed. The detection, in sera of patients with rheumatic autoimmune diseases, of two novel autoantibody specificities, one recognizing solely B2 protein and the second both the B2 and mBx polypeptides, helped to identify mBx proteins as new A/B-type hnRNP components, immunologically related to B2 protein. A common immunoreactive V8 protease peptide of approx. 17 kDa has been identified in B2 and mBx hnRNP polypeptides. mBx protein species are identified in cells of murine origin, and have a ubiquitous tissue distribution and developmental appearance.

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Val, S., S. Jeong, M. Poley, et al. "MP5: STABLE ISOTOPE LABELED BY AMINO ACID IN CULTURE (SILAC) STRATEGY TO ANALYZE HUMAN MIDDLE EAR EPITHELIAL CELLS (HMEEC) SECRETOME IN RESPONSE TO NTHI LYSATES: EVIDENCE OF THE IMPLICATION OF EXOSOMES IN OTITIS MEDIA." Journal of Investigative Medicine 64, no. 3 (2016): 806.2–806. http://dx.doi.org/10.1136/jim-2016-000080.17.

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Purpose of StudyThis study aimed at characterizing the secretome of HMEEC-1 and to evaluate its regulation in response to NTHi lysates and better understand the pathogenesis of Otitis Media (OM).Methods UsedHMEEC-1 were labeled with heavy isotopes of arginine and lysine to obtain a spike-in standard that was mixed with the conditions of interest (control or treated 24 hrs, secretions recovered 24 hrs or 48 hrs) and separated by SDS-PAGE. Peptides generated by in-gel digestion were analyzed by LC-MS/MS. Middle ear effusions (MEEs) from patients having chronic OM were analyzed to validate the results obtained with HMEEC.Summary of Results767 proteins were detected by MS in HMEEC secretions. The more abundant proteins detected were components of the extracellular matrix, proteins implicated in the innate immune response, and surprisingly proteins implicated in the processing and packaging of RNA. These proteins were heterogenous nuclear ribonucleoproteins A2/B1 (hnRNPA2B1) and K (hnRNPK) enriched at the 24 hrs time point (1.99 and 1.78 fold change respectively) and Q at 48 hrs (hnRNPQ, fold change 4.76) in response to NTHi lysates. We then hypothesized that these proteins were implicated in the packaging of miRNAs in exosomes in response to NTHi lysates. An exosome marker assay showed the presence of exosomes in both the cell secretions and MEEs. A western blot analysis of MEE exosome proteins showed the presence of hnRNPs as in cell secretions. Finally, a Nanostring chip assay demonstrated the presence of 8 miRNA in MEEs, mostly reported to be produced by epithelial cells and neutrophils.ConclusionsWe characterized the secretome of HMEEC in response to NTHi lysates treatment that show a potential implication of exosomes in the pathogenesis of OM. We demonstrated the presence of exosomes in HMEEC secretions and MEEs, transporting miRNAs packaged by hnRNP proteins.

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Ma, Kit Wan, Shannon W. N. Au, and Mary M. Y. Waye. "Over-expression of SUMO-1 induces the up-regulation of heterogeneous nuclear ribonucleoprotein A2/B1 isoform B1 (hnRNP A2/B1 isoform B1) and uracil DNA glycosylase (UDG) in hepG2 cells." Cell Biochemistry and Function 27, no. 4 (2009): 228–37. http://dx.doi.org/10.1002/cbf.1562.

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Travina, Aleksandra O., Nadya V. Ilicheva, Alexey G. Mittenberg, Sergey V. Shabelnikov, Anastasia V. Kotova, and Olga I. Podgornaya. "The Long Linker Region of Telomere-Binding Protein TRF2 Is Responsible for Interactions with Lamins." International Journal of Molecular Sciences 22, no. 7 (2021): 3293. http://dx.doi.org/10.3390/ijms22073293.

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Telomere-binding factor 2 (TRF2) is part of the shelterin protein complex found at chromosome ends. Lamin A/C interacts with TRF2 and influences telomere position. TRF2 has an intrinsically disordered region between the ordered dimerization and DNA-binding domains. This domain is referred to as the long linker region of TRF2, or udTRF2. We suggest that udTRF2 might be involved in the interaction between TRF2 and lamins. The recombinant protein corresponding to the udTRF2 region along with polyclonal antibodies against this region were used in co-immunoprecipitation with purified lamina and nuclear extracts. Co-immunoprecipitation followed by Western blots and mass spectrometry indicated that udTRF2 interacts with lamins, preferably lamins A/C. The interaction did not involve any lamin-associated proteins, was not dependent on the post-translation modification of lamins, nor did it require their higher-order assembly. Besides lamins, a number of other udTRF2-interacting proteins were identified by mass spectrometry, including several heterogeneous nuclear ribonucleoproteins (hnRNP A2/B1, hnRNPA1, hnRNP A3, hnRNP K, hnRNP L, hnRNP M), splicing factors (SFPQ, NONO, SRSF1, and others), helicases (DDX5, DHX9, and Eif4a3l1), topoisomerase I, and heat shock protein 71, amongst others. Some of the identified interactors are known to be involved in telomere biology; the roles of the others remain to be investigated. Thus, the long linker region of TRF2 (udTRF2) is a regulatory domain responsible for the association between TRF2 and lamins and is involved in interactions with other proteins.

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Wang, G., Q. Xiao, and Q. Xu. "4 Stem cell differentiation to smooth muscle cells is regulated by HnRNP A2/B1." Heart 97, no. 20 (2011): e7-e7. http://dx.doi.org/10.1136/heartjnl-2011-300920b.4.

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Hatfield, Jodie T., Joseph A. Rothnagel, and Ross Smith. "Characterization of the mouse hnRNP A2/B1/B0 gene and identification of processed pseudogenes." Gene 295, no. 1 (2002): 33–42. http://dx.doi.org/10.1016/s0378-1119(02)00800-4.

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Kozu, Tomoko, Birgit Henrich, and Klaus P. Schäfer. "Structure and expression of the gene (HNRPA2B1) encoding the human hnRNP protein A2/B1." Genomics 25, no. 2 (1995): 365–71. http://dx.doi.org/10.1016/0888-7543(95)80035-k.

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Matsui, Miwa, Hisashi Horiguchi, Hiroshi Kamma, Masachika Fujiwara, Rieko Ohtsubo, and Takesaburo Ogata. "Testis- and developmental stage-specific expression of hnRNP A2/B1 splicing isoforms, B0a/b." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1493, no. 1-2 (2000): 33–40. http://dx.doi.org/10.1016/s0167-4781(00)00154-8.

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Kamma, Hiroshi, Mitsuo Fujimoto, Masachika Fujiwara, et al. "Interaction of hnRNP A2/B1 Isoforms with Telomeric ssDNA and the in Vitro Function." Biochemical and Biophysical Research Communications 280, no. 3 (2001): 625–30. http://dx.doi.org/10.1006/bbrc.2000.4173.

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Kamma, Hiroshi, Hisashi Horiguchi, Lili Wan, et al. "Molecular Characterization of the hnRNP A2/B1 Proteins: Tissue-Specific Expression and Novel Isoforms." Experimental Cell Research 246, no. 2 (1999): 399–411. http://dx.doi.org/10.1006/excr.1998.4323.

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Zhou, Jun, D. C. Allred, Ingalill Avis, et al. "Differential Expression of the Early Lung Cancer Detection Marker, Heterogeneous Nuclear Ribonucleoprotein-A2/B1 (hnRNP-A2/B1) in Normal Breast and Neoplastic Breast Cancer." Breast Cancer Research and Treatment 66, no. 3 (2001): 217–24. http://dx.doi.org/10.1023/a:1010631915831.

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Bilodeau, Patricia S., Jeffrey K. Domsic, Akila Mayeda, Adrian R. Krainer, and C. Martin Stoltzfus. "RNA Splicing at Human Immunodeficiency Virus Type 1 3′ Splice Site A2 Is Regulated by Binding of hnRNP A/B Proteins to an Exonic Splicing Silencer Element." Journal of Virology 75, no. 18 (2001): 8487–97. http://dx.doi.org/10.1128/jvi.75.18.8487-8497.2001.

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ABSTRACT The synthesis of human immunodeficiency virus type 1 (HIV-1) mRNAs is a complex process by which more than 30 different mRNA species are produced by alternative splicing of a single primary RNA transcript. HIV-1 splice sites are used with significantly different efficiencies, resulting in different levels of mRNA species in infected cells. Splicing of Tat mRNA, which is present at relatively low levels in infected cells, is repressed by the presence of exonic splicing silencers (ESS) within the two tat coding exons (ESS2 and ESS3). These ESS elements contain the consensus sequence PyUAG. Here we show that the efficiency of splicing at 3′ splice site A2, which is used to generate Vpr mRNA, is also regulated by the presence of an ESS (ESSV), which has sequence homology to ESS2 and ESS3. Mutagenesis of the three PyUAG motifs within ESSV increases splicing at splice site A2, resulting in increased Vpr mRNA levels and reduced skipping of the noncoding exon flanked by A2 and D3. The increase in Vpr mRNA levels and the reduced skipping also occur when splice site D3 is mutated toward the consensus sequence. By in vitro splicing assays, we show that ESSV represses splicing when placed downstream of a heterologous splice site. A1, A1B, A2, and B1 hnRNPs preferentially bind to ESSV RNA compared to ESSV mutant RNA. Each of these proteins, when added back to HeLa cell nuclear extracts depleted of ESSV-binding factors, is able to restore splicing repression. The results suggest that coordinate repression of HIV-1 RNA splicing is mediated by members of the hnRNP A/B protein family.

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Ishikawa, Kinya, and Yoshitaka Nagai. "Molecular Mechanisms and Future Therapeutics for Spinocerebellar Ataxia Type 31 (SCA31)." Neurotherapeutics 16, no. 4 (2019): 1106–14. http://dx.doi.org/10.1007/s13311-019-00804-6.

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AbstractSpinocerebellar ataxia type 31 (SCA31) is one of the autosomal-dominant neurodegenerative disorders that shows progressive cerebellar ataxia as a cardinal symptom. This disease is caused by a 2.5- to 3.8-kb-long complex pentanucleotide repeat containing (TGGAA)n, (TAGAA)n, (TAAAA)n, and (TAAAATAGAA)n in an intron of the gene called BEAN1 (brain expressed, associated with Nedd4). By comparing various pentanucleotide repeats in this particular locus among control Japanese and Caucasian populations, it was found that (TGGAA)n was the only sequence segregating with SCA31, strongly suggesting the pathogenicity of (TGGAA)n. The complex repeat also lies in an intron of another gene, TK2 (thymidine kinase 2), which is transcribed in the opposite direction, indicating that the complex repeat is bi-directionally transcribed as noncoding repeats. In SCA31 human brains, (UGGAA)n, the BEAN1 transcript of SCA31 mutation was found to form abnormal RNA structures called RNA foci in cerebellar Purkinje cell nuclei. Subsequent RNA pulldown analysis disclosed that (UGGAA)n binds to RNA-binding proteins TDP-43, FUS, and hnRNP A2/B1. In fact, TDP-43 was found to co-localize with RNA foci in human SCA31 Purkinje cells. To dissect the pathogenesis of (UGGAA)n in SCA31, we generated transgenic fly models of SCA31 by overexpressing SCA31 complex pentanucleotide repeats in Drosophila. We found that the toxicity of (UGGAA)n is length- and expression level–dependent, and it was dampened by co-expressing TDP-43, FUS, and hnRNP A2/B1. Further investigation revealed that TDP-43 ameliorates (UGGAA)n toxicity by directly fixing the abnormal structure of (UGGAA)n. This led us to propose that TDP-43 acts as an RNA chaperone against toxic (UGGAA)n. Further research on the role of RNA-binding proteins as RNA chaperones may provide a novel therapeutic strategy for SCA31.

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Gordon, Heather, Lara Ajamian, Fernando Valiente-Echeverrìa, Kathy Lévesque, William F. Rigby, and Andrew J. Mouland. "Depletion of hnRNP A2/B1 overrides the nuclear retention of the HIV-1 genomic RNA." RNA Biology 10, no. 11 (2013): 1714–25. http://dx.doi.org/10.4161/rna.26542.

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Deng, Jinmu, Song Chen, Feng Wang, et al. "Effects of hnRNP A2/B1 Knockdown on Inhibition of Glioblastoma Cell Invasion, Growth and Survival." Molecular Neurobiology 53, no. 2 (2015): 1132–44. http://dx.doi.org/10.1007/s12035-014-9080-3.

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Eom, Ha-Young, Hye-Ran Kim, Hwan-Young Kim, et al. "Mitochondrial DNA copy number and hnRNP A2/B1 protein: Biomarkers for direct exposure of benzene." Environmental Toxicology and Chemistry 30, no. 12 (2011): 2762–70. http://dx.doi.org/10.1002/etc.675.

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Kasim, Mumtaz, Edgar Benko, Aline Winkelmann, et al. "Shutdown of Achaete-scute Homolog-1 Expression by Heterogeneous Nuclear Ribonucleoprotein (hnRNP)-A2/B1 in Hypoxia." Journal of Biological Chemistry 289, no. 39 (2014): 26973–88. http://dx.doi.org/10.1074/jbc.m114.579391.

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Chang, Cheng-Kai, Chi-Jene Chen, Chih-Ching Wu, Shiau-Wen Chen, Shin-Ru Shih, and Rei-Lin Kuo. "Cellular hnRNP A2/B1 interacts with the NP of influenza A virus and impacts viral replication." PLOS ONE 12, no. 11 (2017): e0188214. http://dx.doi.org/10.1371/journal.pone.0188214.

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Jing, Guang-Jun, Dong-Hui Xu, Song-Lin Shi, et al. "Aberrant expression and localization of hnRNP-A2/B1 is a common event in human gastric adenocarcinoma." Journal of Gastroenterology and Hepatology 26, no. 1 (2010): 108–15. http://dx.doi.org/10.1111/j.1440-1746.2010.06482.x.

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Kamma, Hiroshi, Hiroaki Satoh, Miwa Matusi, WenWen Wu, Masachika Fujiwara, and Hisashi Horiguchi. "Characterization of hnRNP A2 and B1 using monoclonal antibodies: intracellular distribution and metabolism through cell cycle." Immunology Letters 76, no. 1 (2001): 49–54. http://dx.doi.org/10.1016/s0165-2478(00)00318-7.

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Prahl, Magdalena, Anna Vilborg, Carina Palmberg, Hans Jörnvall, Charlotte Asker, and Klas G. Wiman. "The p53 target protein Wig-1 binds hnRNP A2/B1 and RNA Helicase A via RNA." FEBS Letters 582, no. 15 (2008): 2173–77. http://dx.doi.org/10.1016/j.febslet.2008.04.065.

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QU, XIAO-HAN, JIN-LU LIU, XIN-WEN ZHONG, XI LI, and QI-GANG ZHANG. "Insights into the roles of hnRNP A2/B1 and AXL in non-small cell lung cancer." Oncology Letters 10, no. 3 (2015): 1677–85. http://dx.doi.org/10.3892/ol.2015.3457.

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