Research Advances in the Biological Functions of RBM3

Long Feiyu

doi:doi:10.11648/j.ijacm.20251302.13

Research Article |

| Peer-Reviewed

Research Advances in the Biological Functions of RBM3

Long Feiyu^*

Published in International Journal of Anesthesia and Clinical Medicine (Volume 13, Issue 2)

Received: 21 July 2025 Accepted: 31 July 2025 Published: 13 August 2025

Views: Downloads:

Download PDF

Share This Article

Twitter
Linked In
Facebook

Abstract

In clinical research, "hypothermia therapy" (at 32-34°C) has been proven to be an effective method for alleviating neurological deficits in neonatal hypoxic-ischemic encephalopathy and adult acute brain injury. Even deeper levels of hypothermia have been used in heart and transplant surgeries. However, "hypothermia therapy" in clinical settings cannot avoid many life-threatening side effects. Its effects go far beyond what was initially observed under hypothermic conditions. RNA-binding motif protein 3 (RBM3), a critical cold shock protein, has revealed significance extending far beyond its initial discovery in hypothermia. Induced by diverse stressors-notably mild hypothermia-RBM3 orchestrates complex post-transcriptional processes, modulating mRNA stability, translation, alternative splicing, and phase separation. It further regulates multiple cellular physiological processes, including neuroprotection, tumorigenesis, anti-apoptosis, and cell cycle progression. This review outlines RBM3’s structure and distribution in humans and synthesizes recent advances in understanding its multifaceted biological functions.

Published in	International Journal of Anesthesia and Clinical Medicine (Volume 13, Issue 2)
DOI	10.11648/j.ijacm.20251302.13
Page(s)	76-81
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2025. Published by Science Publishing Group

Keywords

RNA-Binding Motif Protein 3, Neuroprotection, Cancer

1. Introduction

Hibernating animals adapt to cold environments through tolerance to reduced blood flow, energy consumption, and body temperature while maintaining tissue oxygenation and metabolic homeostasis

[1, 2]

. Over the past two decades, studies identified that mammals produce specific proteins during hypothermia that decelerate cellular metabolism. Termed cold shock proteins (CSPs), these regulators influence cell proliferation, neuronal differentiation/maturation, axonal guidance, and synaptic remodeling

[3-5]

. RBM3 is a key CSP member. Clinically, therapeutic hypothermia (32-34°C) mitigates neurological deficits in neonatal hypoxic-ischemic encephalopathy

[6]

and adult acute brain injury

[7]

, with deeper hypothermia used in cardiac and transplant surgeries

[8]

. However, this therapy carries life-threatening complications

[9]

. Thus, CSPs like RBM3 represent promising targets for mimicking hypothermia’s benefits. Beyond cold adaptation, RBM3 exerts cytoprotective functions under endogenous and environmental stressors at normothermia

[10]

and participates in tumorigenesis

[11]

. This review summarizes recent advances in RBM3’s biological roles.

2. Structural Features and Spatiotemporal Distribution of RBM3

RBM3, encoded on chromosome Xp11.2

[12]

, comprises 157 amino acids. Its N-terminus harbors two highly conserved RNA recognition motifs (RRM1 and RRM2), which mediate RNA processing, splicing, export, stability, packaging, and degradation

[55]

. The C-terminal arginine-glycine-rich domain (RGG) governs protein localization, DNA damage response, mRNA translation, and synaptic plasticity

[56]

, placing RBM3 within the glycine-rich protein (GRP) family.

As a cold shock protein, RBM3 is induced by hypothermia, hypoxia, and mild stress

[13]

. In mammals, RBM3 peaks neonatally but declines markedly in most brain regions during adulthood, except neurogenic niches like the subventricular (SVZ) and subgranular zones (SGZ)

[14, 15]

. The spatial distribution of RBM3 in major organs varies across species. In humans, RBM3 expression is minimal or absent in the thyroid and heart

[16]

. In hibernating animals, such as black bears and squirrels, RBM3 is upregulated in muscle, liver, and heart tissues

[17-19]

. At the subcellular level, RBM3 primarily localizes to the nucleus due to its RGG domain, which serves as a nuclear localization signal facilitating nucleocytoplasmic shuttling

[20]

. Within the nucleus, RBM3 regulates gene transcription or binds specific mRNAs for post-transcriptional modulation. Under physiological or stress conditions, RBM3 shuttles between the nucleus and cytoplasm to exert its biological functions

[21]

3. Biological Functions of RBM3

3.1. Neuroprotection

Mild hypothermia’s neuroprotective effects are closely linked to RBM3, It is mainly manifested in the following aspects:

1) RBM3 is highly expressed in immature mouse neurons and widely distributed.

2) Its mRNA/protein levels increase significantly in neurons at 32-34°C.

3) Higher RBM3 correlates with reduced neuronal apoptosis.

4) RBM3 knockdown diminishes neuroprotection.

5) Hypothermia-induced RBM3 upregulation or normothermic overexpression attenuates apoptosis

[22]

Thus, RBM3 acts as a mediator of hypothermic neuroprotection and a potential therapeutic target to circumvent clinical complications.

In prion-diseased and Alzheimer’s models, RBM3 overexpression preserves synaptic structure (dendritic spine density, synaptic protein levels) and function, prolongs survival, and ameliorates behavioral deficits and neuroinflammation

[23]

. Conversely, RBM3 knockout suppresses synaptogenesis and accelerates disease

[24]

. After acute brain/spinal cord injury, RBM3 redistributes spatiotemporally

[25]

. In rat spinal cord injury (SCI) models, RBM3-positive cells increase dynamically, peaking at 1 day

[26]

or 5 days

[25]

post-injury—discrepancies possibly arising from surgical variability. Both studies support RBM3 upregulation and its critical role in SCI. RBM3 overexpression promotes axonal regeneration and functional recovery in SCI models.

Although RBM3 is recognized as a potent neuroprotective protein, its mechanisms remain incompletely understood. RBM3 binds the 3'UTR of YAP1 mRNA to regulate YAP1 expression, coordinating neurogenesis during cold stress

[28]

. Bastide et al. found that RBM3 interacts with RTN3 mRNA, enhancing its expression. RTN3, as a downstream effector of RBM3, mediates neuroprotection

[27]

. Post hypoxic-ischemic brain injury, RBM3 stimulates neuronal differentiation in the SVZ and SGZ and promotes neural stem/progenitor cell proliferation via the IMP2-IGF2 pathway

[29, 30]

. Additionally, RBM3 modulates apoptosis through multiple pathways, such as inhibiting MAPK signaling to counteract rotenone-induced neurotoxicity

[53]

and suppressing PARP cleavage in hypothermia-mediated neuroprotection

[15]

. In summary, RBM3 plays a pivotal role in neuroprotection, warranting further investigation.

3.2. Cancer

RBM3 regulates protein synthesis and post-transcriptional gene expression, including RNA splicing, transport, surveillance, decay, and translation. Its expression correlates with tumor malignancy and staging, positioning it as a proto-oncogene in cancer development.

3.2.1. Colorectal Cancer

Colorectal cancer (CRC) is the fourth most common human malignancy. High RBM3 expression correlates with favorable CRC prognosis

[31]

, while its loss associates with poor outcomes

[32]

, suggesting RBM3 as a potential prognostic marker. Mechanistically, RBM3 upregulation in HCT116 and DLD1 colon cancer cells enhances β-catenin signaling via GSK3β activation, promoting cancer stem cell activity

[33]

. Thus, RBM3 is a promising therapeutic target in CRC.

3.2.2. Prostate Cancer

High RBM3 expression associates with poorly differentiated, aggressive tumors and independently predicts early recurrence

[34]

. RBM3 knockdown reduces cell viability and increases chemosensitivity

[35]

, aligning with its pro-survival role. However, its prognostic value remains debated. One study showed RBM3 inhibits CD44 variant splicing, impairing cancer stemness and tumorigenesis

[36]

. These findings suggest cancer-type-specific RBM3 effects

[37]

, necessitating further exploration.

3.2.3. Bladder Cancer

In urothelial bladder cancer, low RBM3 expression correlates with higher tumor grade and independently predicts reduced survival

[38]

. Elevated RBM3 associates with lower lymph node metastasis risk

[39]

. A small-scale study found RBM3 deficiency predicts poorer 5-year survival in early-stage patients

[40]

3.2.4. Breast Cancer

RBM3 is overexpressed in breast cancer

[41]

, where it modulates tumor progression via miRNA-mediated protein regulation

[42]

. X chromosome-linked RBM genes (RBMX, RBM3, RBM10) correlate with pro-apoptotic Bax expression

[41]

. While some studies link high RBM3 to favorable prognosis

[43]

, others associate it with poor outcomes, possibly via ARPC2 3'UTR binding

[44]

. LncRNA-LINC0009 also regulates RBM3 to promote triple-negative breast cancer proliferation and invasion

[45]

3.2.5. Other Cancers

In gastric cancer, high RBM3 correlates with reduced p53 expression and better prognosis

[46]

. In melanoma, metastatic tumors show RBM3 downregulation, while nuclear RBM3 in primary tumors associates with prolonged survival

[47]

. RBM3 inversely correlates with MCM3, a poor prognostic marker, further supporting its favorable role

[48]

Overall, most studies position RBM3 as a favorable prognostic biomarker across cancers. However, conflicting findings underscore the need for further research into its tumor-specific roles.

3.3. Other Functions

3.3.1. Apoptosis Regulation

Early studies showed hypothermia (32°C) induces RBM3, protecting neurons from toxicant-induced apoptosis

[15]

. In breast cancer, RBM3 correlates with Bax expression

[41]

. Ferry et al. reported RBM3 overexpression inhibits apoptosis and necrosis in myoblasts, enhancing cell survival

[49]

, suggesting therapeutic potential in muscle atrophy. Under serum starvation, RBM3 rescues apoptosis by restoring translation efficiency

[16]

. Feng et al. found RBM3 increases survival of LPS-treated pulmonary microvascular endothelial cells

[50]

Mechanistically, RBM3 binds NF90 to suppress PERK-eIF2α-CHOP signaling, mitigating ER stress-induced apoptosis

[51]

. It also upregulates Bcl-2 and inhibits caspases

[49]

and blocks UV-induced p38/JNK activation

[52]

. Collectively, RBM3 exerts cytoprotection across cell types.

3.3.2. mRNA Transcription and Translation

RBM3 binds and modulates mRNA translation, notably stabilizing COX-2, IL-8, and VEGF mRNAs

[54]

. It enhances translation via:

1) RNA-independent binding to 60S ribosomal subunits;

2) Increasing polysome formation;

3) Promoting eIF4E phosphorylation

[56]

;

4) RBM3 also regulates translation via microRNAs.

3.3.3. MicroRNA Biogenesis

Hypothermia-induced RBM3 alters miRNA levels to promote translation. It binds 70-nt pre-miRNAs, broadly regulating miRNA processing via Dicer

[58]

. Paradoxically, RBM3 knockdown upregulates thermosensitive immune-related miRNAs, preventing hyperthermia pathology

[59]

. While RBM3’s miRNA regulatory role is clear, precise mechanisms require further study.

3.3.4. Cell Cycle

RBM3 regulates G2/M transition, linking it to tumor biology. RBM3 knockout induces mitotic defects in NIH3T3 fibroblasts and HCT116 cells

[57]

. RBM3-deficient mouse embryonic fibroblasts exhibit G2 arrest

[60]

, confirming its necessity for mitosis. This may explain why RBM3-high tumors show better chemosensitivity and prognosis

[61]

3.3.5. Inflammation

High circulating RBM3 reduces systemic inflammation during extracorporeal circulation

[62]

. In murine acute lung injury models, RBM3 overexpression enhances endothelial cell survival post-LPS but disrupts tight junctions

[50]

. RBM3 knockout exacerbates sepsis-induced lung injury and mortality via NF-κB/NLRP3

[63]

, highlighting its emerging role in inflammation.

4. Summary

This review outlines RBM3’s roles in neuroprotection, cancer, apoptosis, mRNA regulation, cell cycle, and inflammation. As a cold shock protein, RBM3’s neuroprotective effects are well-documented but require clinical validation. Before targeting RBM3 for hypothermia-mimetic therapies, further clinical studies are needed.

In cancer, RBM3’s duality as both a favorable and unfavorable prognostic marker necessitates deeper exploration of its stage- and context-dependent roles. Its anti-apoptotic and cell cycle functions intersect with neuroprotection and tumorigenesis, positioning RBM3 as a multifaceted "protective molecule." Emerging roles in inflammation underscore its therapeutic potential. Elucidating RBM3’s precise mechanisms and signaling pathways may pave the way for personalized therapies across diverse diseases.

Abbreviations

RBM3	RNA-Binding Motif Protein 3
CSPs	Cold Shock Proteins
RRM	RNA Recognition Motifs
GRP	Glycine-Rich Protein
SVZ	Subventricular
SGZ	Subgranular Zones
SCI	Spinal Cord Injury
CRC	Colorectal Cancer

Author Contributions

Feiyu Long is the sole author. The author read and approved the final manuscript.

Conflicts of Interest

The author declares no conflicts of interest.

References

[1]	Frerichs KU, Kennedy C, Sokoloff L, et al. Local cerebral blood flow during hibernation, a model of natural tolerance to "cerebral ischemia" [J]. J Cereb Blood Flow Metab, 1994, 14(2): 193-205.
[2]	Frerichs KU, Hallenbeck JM. Hibernation in ground squirrels induces state and species-specific tolerance to hypoxia and aglycemia: an in vitro study in hippocampal slices [J]. J Cereb Blood Flow Metab, 1998, 18(2): 168-175.
[3]	Lin AC, Holt CE. Local translation and directional steering in axons [J]. EMBO J, 2007, 26(16): 3729-3736.
[4]	Ratti A, Fallini C, Cova L, et al. A role for the ELAV RNA-binding proteins in neural stem cells: stabilization of Msi1 mRNA [J]. J Cell Sci, 2006, 119(Pt 7): 1442-1452.
[5]	Steward O, Schuman EM. Protein synthesis at synaptic sites on dendrites [J]. Annu Rev Neurosci, 2001, 24: 299-325.
[6]	Committee on Fetus and Newborn, Papile LA, Baley JE, et al. Hypothermia and neonatal encephalopathy [J]. Pediatrics, 2014, 133(6): 1146-1150.
[7]	Yenari MA, Han HS. Neuroprotective mechanisms of hypothermia in brain ischaemia [J]. Nat Rev Neurosci, 2012, 13(4): 267-278.
[8]	Lampe JW, Becker LB. State of the art in therapeutic hypothermia [J]. Annu Rev Med, 2011, 62: 79-93.
[9]	Choi HA, Badjatia N, Mayer SA. Hypothermia for acute brain injury--mechanisms and practical aspects [J]. Nat Rev Neurol, 2012, 8(4): 214-222.
[10]	Lleonart ME. A new generation of proto-oncogenes: cold-inducible RNA binding proteins [J]. Biochim Biophys Acta, 2010, 1805(1): 43-52.
[11]	Zhou RB, Lu XL, Zhang CY, et al. RNA binding motif protein 3: a potential biomarker in cancer and therapeutic target in neuroprotection [J]. Oncotarget, 2017, 8(13): 22235-22250.
[12]	Derry JM, Kerns JA, Francke U. RBM3, a novel human gene in Xp11.23 with a putative RNA-binding domain [J]. Hum Mol Genet, 1995, 4(12): 2307-2311.
[13]	Yang H, Rao JN, Wang JY. Posttranscriptional Regulation of Intestinal Epithelial Tight Junction Barrier by RNA-binding Proteins and microRNAs [J]. Tissue Barriers, 2014, 2(1): e28320.
[14]	Pilotte J, Cunningham BA, Edelman GM, et al. Developmentally regulated expression of the cold-inducible RNA-binding motif protein 3 in euthermic rat brain [J]. Brain Res, 2009, 1258: 12-24.
[15]	Chip S, Zelmer A, Ogunshola OO, et al. The RNA-binding protein RBM3 is involved in hypothermia induced neuroprotection [J]. Neurobiol Dis, 2011, 43(2): 388-396.
[16]	Wellmann S, Truss M, Bruder E, et al. The RNA-binding protein RBM3 is required for cell proliferation and protects against serum deprivation-induced cell death [J]. Pediatr Res, 2010, 67(1): 35-41.
[17]	Fedorov VB, Goropashnaya AV, Tøien Ø, et al. Modulation of gene expression in heart and liver of hibernating black bears (Ursus americanus) [J]. BMC Genomics, 2011, 12: 171.
[18]	Fedorov VB, Goropashnaya AV, Tøien Ø, et al. Elevated expression of protein biosynthesis genes in liver and muscle of hibernating black bears (Ursus americanus) [J]. Physiol Genomics, 2009, 37(2): 108-118.
[19]	Williams DR, Epperson LE, Li W, et al. Seasonally hibernating phenotype assessed through transcript screening [J]. Physiol Genomics, 2005, 24(1): 13-22.
[20]	Rzechorzek NM, Connick P, Patani R, et al. Hypothermic Preconditioning of Human Cortical Neurons Requires Proteostatic Priming [J]. EBioMedicine, 2015, 2(6): 528-535.
[21]	Thandapani P, O'Connor TR, Bailey TL, et al Defining the RGG/RG motif [J]. Mol Cell, 2013, 50(5): 613-623.
[22]	Al-Astal HI, Massad M, AlMatar M, et al. Cellular Functions of RNA-Binding Motif Protein 3 (RBM3): Clues in Hypothermia, Cancer Biology and Apoptosis [J]. Protein Pept Lett, 2016, 23(9): 828-835.
[23]	Peretti D, Bastide A, Radford H, et al. RBM3 mediates structural plasticity and protective effects of cooling in neurodegeneration [J]. Nature, 2015, 518(7538): 236-239.
[24]	Ma T, Trinh MA, Wexler AJ, et al. Suppression of eIF2α kinases alleviates Alzheimer's disease-related plasticity and memory deficits [J]. Nat Neurosci, 2013, 16(9): 1299-1305.
[25]	Cui Z, Zhang J, Bao G, et al. Spatiotemporal profile and essential role of RBM3 expression after spinal cord injury in adult rats [J]. J Mol Neurosci, 2014, 54(2): 252-263.
[26]	Zhao W, Xu D, Cai G, et al. Spatiotemporal pattern of RNA-binding motif protein 3 expression after spinal cord injury in rats [J]. Cell Mol Neurobiol, 2014, 34(4): 491-499.
[27]	Bastide A, Peretti D, Knight JR, et al. RTN3 Is a Novel Cold-Induced Protein and Mediates Neuroprotective Effects of RBM3 [J]. Curr Biol, 2017, 27(5): 638-650.
[28]	Xia W, Su L, Jiao J. Cold-induced protein RBM3 orchestrates neurogenesis via modulating Yap mRNA stability in cold stress [J]. J Cell Biol, 2018, 217(10): 3464-3479.
[29]	Yan J, Goerne T, Zelmer A, et al. The RNA-Binding Protein RBM3 Promotes Neural Stem Cell (NSC) Proliferation Under Hypoxia [J]. Front Cell Dev Biol, 2019, 7: 288.
[30]	Zhu X, Yan J, Bregere C, et al. RBM3 promotes neurogenesis in a niche-dependent manner via IMP2-IGF2 signaling pathway after hypoxic-ischemic brain injury [J]. Nat Commun, 2019, 10(1): 3983.
[31]	Hjelm B, Brennan DJ, Zendehrokh N, et al. High nuclear RBM3 expression is associated with an improved prognosis in colorectal cancer [J]. Proteomics Clin Appl, 2011, 5(11-12): 624-635.
[32]	Melling N, Simon R, Mirlacher M, et al. Loss of RNA-binding motif protein 3 expression is associated with right-sided localization and poor prognosis in colorectal cancer [J]. Histopathology, 2016, 68(2): 191-198.
[33]	Venugopal A, Subramaniam D, Balmaceda J, et al. RNA binding protein RBM3 increases β-catenin signaling to increase stem cell characteristics in colorectal cancer cells [J]. Mol Carcinog, 2016, 55(11): 1503-1516.
[34]	Grupp K, Wilking J, Prien K, et al. High RNA-binding motif protein 3 expression is an independent prognostic marker in operated prostate cancer and tightly linked to ERG activation and PTEN deletions [J]. Eur J Cancer, 2014, 50(4): 852-861.
[35]	Zeng Y, Kulkarni P, Inoue T, et al. Down-regulating cold shock protein genes impairs cancer cell survival and enhances chemosensitivity [J]. J Cell Biochem, 2009, 107(1): 179-188.
[36]	Zeng Y, Wodzenski D, Gao D, et al. Stress-response protein RBM3 attenuates the stem-like properties of prostate cancer cells by interfering with CD44 variant splicing [J]. Cancer Res, 2013, 73(13): 4123-4133.
[37]	Thomas C, Gustafsson JÅ. The different roles of ER subtypes in cancer biology and therapy [J]. Nat Rev Cancer, 2011, 11(8): 597-608.
[38]	Boman K, Segersten U, Ahlgren G, et al. Decreased expression of RNA-binding motif protein 3 correlates with tumour progression and poor prognosis in urothelial bladder cancer [J]. BMC Urol, 2013, 13: 17.
[39]	Florianova L, Xu B, Traboulsi S, et al. Evaluation of RNA-binding motif protein 3 expression in urothelial carcinoma of the bladder: an immunohistochemical study [J]. World J Surg Oncol, 2015, 13: 317.
[40]	Boman K, Andersson G, Wennersten C, et al. Podocalyxin-like and RNA-binding motif protein 3 are prognostic biomarkers in urothelial bladder cancer: a validatory study [J]. Biomark Res, 2017, 5: 10.
[41]	Martínez-Arribas F, Agudo D, Pollán M, et al. Positive correlation between the expression of X-chromosome RBM genes (RBMX, RBM3, RBM10) and the proapoptotic Bax gene in human breast cancer [J]. J Cell Biochem, 2006, 97(6): 1275-1282.
[42]	Dresios J, Aschrafi A, Owens GC, et al. Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters microRNA levels, and enhances global protein synthesis [J]. Proc Natl Acad Sci USA, 2005, 102(6): 1865-1870.
[43]	Jögi A, Brennan DJ, Rydén L, et al. Nuclear expression of the RNA-binding protein RBM3 is associated with an improved clinical outcome in breast cancer [J]. Mod Pathol, 2009, 22(12): 1564-1574.
[44]	Chen P, Yue X, Xiong H, et al. RBM3 upregulates ARPC2 by binding the 3'UTR and contributes to breast cancer progression [J]. Int J Oncol, 2019, 54(4): 1387-1397.
[45]	Tian Y, Xia S, Ma M, et al. LINC00096 Promotes the Proliferation and Invasion by Sponging miR-383-5p and Regulating RBM3 Expression in Triple-Negative Breast Cancer [J]. Onco Targets Ther, 2019, 12: 10569-10578.
[46]	Ye F, Jin P, Cai X, et al. High RNA-Binding Motif Protein 3 (RBM3) Expression is Independently Associated with Prolonged Overall Survival in Intestinal-Type Gastric Cancer [J]. Med Sci Monit, 2017, 23: 6033-6041.
[47]	Jonsson L, Bergman J, Nodin B, et al. Low RBM3 protein expression correlates with tumour progression and poor prognosis in malignant melanoma: an analysis of 215 cases from the Malmö Diet and Cancer Study [J]. J Transl Med, 2011, 9: 114.
[48]	Nodin B, Fridberg M, Jonsson L, et al. High MCM3 expression is an independent biomarker of poor prognosis and correlates with reduced RBM3 expression in a prospective cohort of malignant melanoma [J]. Diagn Pathol, 2012, 7: 82.
[49]	Ferry AL, Vanderklish PW, Dupont-Versteegden EE. Enhanced survival of skeletal muscle myoblasts in response to overexpression of cold shock protein RBM3 [J]. Am J Physiol Cell Physiol, 2011, 301(2): C392-C402.
[50]	Feng J, Pan W, Yang X, et al. RBM3 Increases Cell Survival but Disrupts Tight Junction of Microvascular Endothelial Cells in Acute Lung Injury [J]. J Surg Res, 2021, 261: 226-235.
[51]	Zhu X, Zelmer A, Kapfhammer JP, et al. Cold-inducible RBM3 inhibits PERK phosphorylation through cooperation with NF90 to protect cells from endoplasmic reticulum stress [J]. FASEB J, 2016, 30(2): 624-634.
[52]	Zhuang RJ, Ma J, Shi X, et al. Cold-Inducible Protein RBM3 Protects UV Irradiation-Induced Apoptosis in Neuroblastoma Cells by Affecting p38 and JNK Pathways and Bcl2 Family Proteins [J]. J Mol Neurosci, 2017, 63(2): 142-151.
[53]	Yang HJ, Zhuang RJ, Li YB, et al. Cold-inducible protein RBM3 mediates hypothermic neuroprotection against neurotoxin rotenone via inhibition on MAPK signalling [J]. J Cell Mol Med, 2019, 23(10): 7010-7020.
[54]	Burd CG, Dreyfuss G. Conserved structures and diversity of functions of RNA-binding proteins. Science. 1994; 265(5172): 615-621.
[55]	Godin KS, Varani G. How arginine-rich domains coordinate mRNA maturation events. RNA Biol. 2007; 4(2): 69-75.
[56]	Smart F, Aschrafi A, Atkins A, et al. Two isoforms of the cold -inducible mRNA -binding protein RBM3 lo- calize to dendrites and promote translation [J]. J Neuro- chem, 2007, 101(5): 1367-1379.
[57]	Sureban SM, Ramalingam S, Natarajan G, et al. Translation regulatory factor RBM3 is a proto-oncogene that prevents mitotic catastrophe [J]. Oncogene, 2008, 27(33): 4544-4556.
[58]	Pilotte J, Dupont - Versteegden EE, Vanderklish PW. Widespread regulation of miRNA biogenesis at the Dic-er step by the cold - inducible RNA - binding protein, RBM3 [J]. PLoS One, 2011, 6(12): e28446.
[59]	Wong JJ, Au AY, Gao D, et al. RBM3 regulates temperature sensitive miR - 142 - 5p and miR - 143 (thermo-miRs), which target immune genes and control fever [J]. Nucleic Acids Res, 2016, 44(6): 2888-2897.
[60]	Matsuda A, Ogawa M, Yanai H, et al. Generation of mice deficient in RNA -binding motif protein 3 (RBM3) and characterization of its role in innate immune responses and cell growth [J].
[61]	Ehlen A, Nodin B, Rexhepaj E, et al. RBM3- regulat-ed genes promote DNA integrity and affect clinical out- come in epithelial ovarian cancer [J]. Transl Oncol, 2011, 4(4): 212-221.
[62]	Rosenthal LM, Tong G, Wowro S, et al. A Prospective Clinical Trial Measuring the Effects of Cardiopulmonary Bypass Under Mild Hypothermia on the Inflammatory Response and Regulation of Cold-Shock Protein RNA-Binding Motif 3. Ther Hypothermia Temp Manag. 2020; 10(1): 60-70.
[63]	Long F, Hu L, Chen Y, et al. RBM3 is associated with acute lung injury in septic mice and patients via the NF-κB/NLRP3 pathway. Inflamm Res. 2023; 72(4): 731-744.

Cite This Article

Plain Text BibTeX RIS

APA Style

Feiyu, L. (2025). Research Advances in the Biological Functions of RBM3. International Journal of Anesthesia and Clinical Medicine, 13(2), 76-81. https://doi.org/10.11648/j.ijacm.20251302.13

Copy | Download

ACS Style

Feiyu, L. Research Advances in the Biological Functions of RBM3. Int. J. Anesth. Clin. Med. 2025, 13(2), 76-81. doi: 10.11648/j.ijacm.20251302.13

Copy | Download

AMA Style

Feiyu L. Research Advances in the Biological Functions of RBM3. Int J Anesth Clin Med. 2025;13(2):76-81. doi: 10.11648/j.ijacm.20251302.13

Copy | Download

@article{10.11648/j.ijacm.20251302.13,
  author = {Long Feiyu},
  title = {Research Advances in the Biological Functions of RBM3
},
  journal = {International Journal of Anesthesia and Clinical Medicine},
  volume = {13},
  number = {2},
  pages = {76-81},
  doi = {10.11648/j.ijacm.20251302.13},
  url = {https://doi.org/10.11648/j.ijacm.20251302.13},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijacm.20251302.13},
  abstract = {In clinical research, "hypothermia therapy" (at 32-34°C) has been proven to be an effective method for alleviating neurological deficits in neonatal hypoxic-ischemic encephalopathy and adult acute brain injury. Even deeper levels of hypothermia have been used in heart and transplant surgeries. However, "hypothermia therapy" in clinical settings cannot avoid many life-threatening side effects. Its effects go far beyond what was initially observed under hypothermic conditions. RNA-binding motif protein 3 (RBM3), a critical cold shock protein, has revealed significance extending far beyond its initial discovery in hypothermia. Induced by diverse stressors-notably mild hypothermia-RBM3 orchestrates complex post-transcriptional processes, modulating mRNA stability, translation, alternative splicing, and phase separation. It further regulates multiple cellular physiological processes, including neuroprotection, tumorigenesis, anti-apoptosis, and cell cycle progression. This review outlines RBM3’s structure and distribution in humans and synthesizes recent advances in understanding its multifaceted biological functions.},
 year = {2025}
}

Copy | Download

TY  - JOUR
T1  - Research Advances in the Biological Functions of RBM3

AU  - Long Feiyu
Y1  - 2025/08/13
PY  - 2025
N1  - https://doi.org/10.11648/j.ijacm.20251302.13
DO  - 10.11648/j.ijacm.20251302.13
T2  - International Journal of Anesthesia and Clinical Medicine
JF  - International Journal of Anesthesia and Clinical Medicine
JO  - International Journal of Anesthesia and Clinical Medicine
SP  - 76
EP  - 81
PB  - Science Publishing Group
SN  - 2997-2698
UR  - https://doi.org/10.11648/j.ijacm.20251302.13
AB  - In clinical research, "hypothermia therapy" (at 32-34°C) has been proven to be an effective method for alleviating neurological deficits in neonatal hypoxic-ischemic encephalopathy and adult acute brain injury. Even deeper levels of hypothermia have been used in heart and transplant surgeries. However, "hypothermia therapy" in clinical settings cannot avoid many life-threatening side effects. Its effects go far beyond what was initially observed under hypothermic conditions. RNA-binding motif protein 3 (RBM3), a critical cold shock protein, has revealed significance extending far beyond its initial discovery in hypothermia. Induced by diverse stressors-notably mild hypothermia-RBM3 orchestrates complex post-transcriptional processes, modulating mRNA stability, translation, alternative splicing, and phase separation. It further regulates multiple cellular physiological processes, including neuroprotection, tumorigenesis, anti-apoptosis, and cell cycle progression. This review outlines RBM3’s structure and distribution in humans and synthesizes recent advances in understanding its multifaceted biological functions.
VL  - 13
IS  - 2
ER  -

Copy | Download

Author Information

Long Feiyu

Department of Anesthesiology, West China Hospital, Sichuan University, Chengdu, China

Contact Email

http://orcid.org/0000-0002-3845-293X

Download PDF

Submit an Article

Sections

Plain Text BibTeX RIS

APA Style

Feiyu, L. (2025). Research Advances in the Biological Functions of RBM3. International Journal of Anesthesia and Clinical Medicine, 13(2), 76-81. https://doi.org/10.11648/j.ijacm.20251302.13

Copy | Download

ACS Style

Feiyu, L. Research Advances in the Biological Functions of RBM3. Int. J. Anesth. Clin. Med. 2025, 13(2), 76-81. doi: 10.11648/j.ijacm.20251302.13

Copy | Download

AMA Style

Feiyu L. Research Advances in the Biological Functions of RBM3. Int J Anesth Clin Med. 2025;13(2):76-81. doi: 10.11648/j.ijacm.20251302.13

Copy | Download

@article{10.11648/j.ijacm.20251302.13,
  author = {Long Feiyu},
  title = {Research Advances in the Biological Functions of RBM3
},
  journal = {International Journal of Anesthesia and Clinical Medicine},
  volume = {13},
  number = {2},
  pages = {76-81},
  doi = {10.11648/j.ijacm.20251302.13},
  url = {https://doi.org/10.11648/j.ijacm.20251302.13},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijacm.20251302.13},
  abstract = {In clinical research, "hypothermia therapy" (at 32-34°C) has been proven to be an effective method for alleviating neurological deficits in neonatal hypoxic-ischemic encephalopathy and adult acute brain injury. Even deeper levels of hypothermia have been used in heart and transplant surgeries. However, "hypothermia therapy" in clinical settings cannot avoid many life-threatening side effects. Its effects go far beyond what was initially observed under hypothermic conditions. RNA-binding motif protein 3 (RBM3), a critical cold shock protein, has revealed significance extending far beyond its initial discovery in hypothermia. Induced by diverse stressors-notably mild hypothermia-RBM3 orchestrates complex post-transcriptional processes, modulating mRNA stability, translation, alternative splicing, and phase separation. It further regulates multiple cellular physiological processes, including neuroprotection, tumorigenesis, anti-apoptosis, and cell cycle progression. This review outlines RBM3’s structure and distribution in humans and synthesizes recent advances in understanding its multifaceted biological functions.},
 year = {2025}
}

Copy | Download

TY  - JOUR
T1  - Research Advances in the Biological Functions of RBM3

AU  - Long Feiyu
Y1  - 2025/08/13
PY  - 2025
N1  - https://doi.org/10.11648/j.ijacm.20251302.13
DO  - 10.11648/j.ijacm.20251302.13
T2  - International Journal of Anesthesia and Clinical Medicine
JF  - International Journal of Anesthesia and Clinical Medicine
JO  - International Journal of Anesthesia and Clinical Medicine
SP  - 76
EP  - 81
PB  - Science Publishing Group
SN  - 2997-2698
UR  - https://doi.org/10.11648/j.ijacm.20251302.13
AB  - In clinical research, "hypothermia therapy" (at 32-34°C) has been proven to be an effective method for alleviating neurological deficits in neonatal hypoxic-ischemic encephalopathy and adult acute brain injury. Even deeper levels of hypothermia have been used in heart and transplant surgeries. However, "hypothermia therapy" in clinical settings cannot avoid many life-threatening side effects. Its effects go far beyond what was initially observed under hypothermic conditions. RNA-binding motif protein 3 (RBM3), a critical cold shock protein, has revealed significance extending far beyond its initial discovery in hypothermia. Induced by diverse stressors-notably mild hypothermia-RBM3 orchestrates complex post-transcriptional processes, modulating mRNA stability, translation, alternative splicing, and phase separation. It further regulates multiple cellular physiological processes, including neuroprotection, tumorigenesis, anti-apoptosis, and cell cycle progression. This review outlines RBM3’s structure and distribution in humans and synthesizes recent advances in understanding its multifaceted biological functions.
VL  - 13
IS  - 2
ER  -

Copy | Download