Heterogeneous nuclear ribonucleoprotein (hnRNP) A2/B1 is involved in the synthesis of RNA. Its expression is up-regulated in many tumor cell lines. In this study, we investigated the distribution of hnRNP A2/B1 in the nuclear matrix, including its co-localization with expression products of related genes. Results from 2-DE PAGE and MS showed that hnRNP A2/B1 is involved with components of nuclear matrix proteins of SK-N-SH cells, and that its expression level is down-regulated after retinoic acid (RA) treatment. Protein immunoblotting results further confirm the existence of hnRNP A2/B1 in the nuclear matrix, as well as its down-regulation after RA treatment. Immunofluorescence microscopy observation showed that hnRNP A2/B1 localized in nuclear matrix of SK-N-SH cells and its distribution regions were altered after RA treatment. Laser scanning confocal microscopy observation showed that hnRNP A2/B1 co-localized with c-Myc, c-Fos, P53, and Rb in SK-N-SH cells. The co-localized region was altered as a result of RA treatment. Our data proved that hnRNP A2/B1 is a nuclear matrix protein and can be up-regulated in human neuroblastoma. The expression and distribution of hnRNP A2/B1 can affect the differentiation of SK-N-SH cells, as well as its co-localization with related oncogenes and tumor suppressor genes.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/jcb.23063 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Exosome-delivered NR2F1-AS1 and NR2F1 drive phenotypic transition from dormancy to proliferation in treatment-resistant prostate cancer via stabilizing hormonal receptors.
J Nanobiotechnology
December 2024
Department of Urology, Guangzhou Women and Children's Medical Center, National Children's Medical Center for South Central Region, Guangzhou Medical University, Guangzhou, Guangdong, China.
Cancer cells acquire the ability to reprogram their phenotype in response to targeted therapies, yet the transition from dormancy to proliferation in drug-resistant cancers remains poorly understood. In prostate cancer, we utilized high-plasticity mouse models and enzalutamide-resistant (ENZ-R) cellular models to elucidate NR2F1 as a key factor in lineage transition and ENZ resistance. Depletion of NR2F1 drives ENZ-R cells into a relative dormancy state, characterized by reduced proliferation and heightened drug resistance, while NR2F1 overexpression yields contrasting outcomes.
View Article and Find Full Text PDFC9orf72-linked arginine-rich dipeptide repeats aggravate pathological phase separation of G3BP1.
Proc Natl Acad Sci U S A
December 2024
Structural Biology Brussels, Bio-engineering Department, Vrije Universiteit Brussel, Elsene 1050, Belgium.
Article Synopsis
- * R-DPRs bind much stronger to the protein G3BP1 than RNA does, promoting the formation of cellular droplets through a process called liquid-liquid phase separation (LLPS), and these droplets can eventually aggregate harmful proteins linked to ALS.
- * Differences in pathology between two types of R-DPRs, poly-GR and poly-PR, suggest that poly-GR primarily targets G3BP1 in stress granules, rather than NPM1 in nucleoli, indicating
Higher isoform of hnRNPA1 confer Temozolomide resistance in U87MG & LN229 glioma cells.
J Neurooncol
January 2025
Molecular Cancer Genetics and Signal Transduction Laboratory, Dr. B.R Ambedkar Center for Biomedical Research, University of Delhi, North Campus, Gate No. 1, Vishwavidyalaya Marg, Mall Road, 44, AH2, Delhi, 110007, India.
Background: Gliblastoma is a malignant brain tumor; despite available treatment modalities, the tumor reoccurrence rate persist in the currently prescribed Temozolomide chemotherapy. Study aimed to study the inquisitive role of RNA binding splice factor protein hnRNPA1 in promoting glioma resistance against Temozolomide drug and therapeutic insights.
Methods: In this study two non-expressing O-methylguanine-DNA methyltransferase (MGMT) glioma cell lines U87MG & LN229.
Intrinsically disordered regions and RNA binding domains contribute to protein enrichment in biomolecular condensates in Xenopus oocytes.
Sci Rep
November 2024
Department of Molecular Biology, Cell Biology & Biochemistry, Brown University, Providence, RI, 02912, USA.
Proteins containing both intrinsically disordered regions (IDRs) and RNA binding domains (RBDs) can phase separate in vitro, forming bodies similar to cellular biomolecular condensates. However, how IDR and RBD domains contribute to in vivo recruitment of proteins to biomolecular condensates remains poorly understood. Here, we analyzed the roles of IDRs and RBDs in L-bodies, biomolecular condensates present in Xenopus oocytes.
View Article and Find Full Text PDFOptical characterization of molecular interaction strength in protein condensates.
Mol Biol Cell
December 2024
Max Planck Institute for the Science of Light, Erlangen, Germany, 91058.
Biomolecular condensates have been identified as a ubiquitous means of intracellular organization, exhibiting very diverse material properties. However, techniques to characterize these material properties and their underlying molecular interactions are scarce. Here, we introduce two optical techniques-Brillouin microscopy and quantitative phase imaging (QPI)-to address this scarcity.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!