Heterogeneous nuclear ribonucleoprotein U-actin complex derived from extracellular vesicles facilitates proliferation and migration of human coronary artery endothelial cells by promoting RNA polymerase II transcription

Wang, Han; Liu, Hengdao; Zhao, Xi; Chen, Xiaowei

doi:10.1080/21655979.2022.2066754

Cited by 5 publications

(4 citation statements)

References 93 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Through extracellular vesicles derived from embryonic stem cells, SAF-A is transferred into human coronary artery endothelial cells to combine with actin. The SAF-A-actin complex leads to enhanced RNA Pol II phosphorylation and its level on vascular endothelial growth factor ( VEGF ) promoter, upregulating VEGF expression ( 4 ) ( Fig. 2B ).…”

Section: Functions Of Saf-amentioning

confidence: 99%

“…Through consistent interaction with chromatin-associated RNAs, SAF-A forms oligomers to induce de-compaction of the large-scale human interphase chromatin structure ( 8 ). (B) During transcription initiation, SAF-A-actin interaction enhances RNA Pol II phosphorylation ( 4 ). Besides, SAF-A binds to elements within promoter regions to promote transcription ( 32 ).…”

Section: Figurementioning

confidence: 99%

“…SAF-A is widely expressed in various organs or tissues, such as bone marrow, lymphoid tissues, brain, heart, lung and kidney ( https://www.proteinatlas.org/ENSG00000153187-HNRNPU ). Due to its functional domains, SAF-A binds to both DNA (such as scaffold-attached region DNA) and RNA (such as chromatin-associated RNAs) and plays essential roles in several cellular processes such as chromatin structure regulation ( 3 ), transcription ( 4 ) and mitosis ( 5 ). The present review summarized the structure, multiple functions and clinical significance of SAF-A.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Biological functions and clinic significance of SAF‑A (Review)

Zhang,

Li,

et al. 2024

Biomed Rep

View full text Add to dashboard Cite

As one member of the heterogeneous ribonucleoprotein (hnRNP) family, scaffold attachment factor A (SAF-A) or hnRNP U, is an abundant nuclear protein. With RNA and DNA binding activities, SAF-A has multiple functions. The present review focused on the biological structure and different roles of SAF-A and SAF-A-related diseases. It was found that SAF-A maintains the higher-order chromatin organization via RNA and DNA, and regulates transcription at the initiation and elongation stages. In addition to regulating pre-mRNA splicing, mRNA transportation and stabilization, SAF-A participates in double-strand breaks and mitosis repair.Therefore, the aberrant expression and mutation of SAF-A results in tumors and impaired neurodevelopment. Moreover, SAF-A may play a role in the anti-virus system. In conclusion, due to its essential biological functions, SAF-A may be a valuable clinical prediction factor or therapeutic target. Since the role of SAF-A in tumors and viral infections may be controversial, more animal experiments and clinical assays are needed. Contents 1. Introduction 2. Materials and methods 3. The structure of SAF-A 4. Functions of SAF-A 5.

show abstract

Section: Functions Of Saf-amentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Biological functions and clinic significance of SAF‑A (Review)

Zhang,

Li,

et al. 2024

Biomed Rep

View full text Add to dashboard Cite

show abstract

“…hnRNP D0 was shown to decrease VEGF expression, whereas hnRNP U was shown to promote coronary endothelial proliferation and migration. 67,68 hnRNP K has been demonstrated to bind to endothelial uncoupling protein 2(UCP2) and reduce ROS production, 69 whereas hnRNP L is essential for endothelial cell survival under hypoxic conditions. 70 As there is no evidence in the literature describing the function of hnRNPs in brain endothelial cells, we postulate that the observed hnRNP expression changes indicate significant alteration of RNA metabolism including alternative splicing in BMVs.…”

Section: Upregulated Proteins -Severe Hypoglycemiamentioning

confidence: 99%

Acute severe hypoglycemia alters mouse brain microvascular proteome

Sakamuri,

Sure,

Oruganti

et al. 2023

J Cereb Blood Flow Metab

View full text Add to dashboard Cite

Hypoglycemia increases the risk related to stroke and neurodegenerative diseases, however, the underlying mechanisms are unclear. For the first time, we studied the effect of a single episode (acute) of severe (ASH) and mild (AMH) hypoglycemia on mouse brain microvascular proteome. After four-hour fasting, insulin was administered (i.p) to lower mean blood glucose in mice and induce ∼30 minutes of ASH (∼30 mg/dL) or AMH (∼75 mg/dL), whereas a similar volume of saline was given to control mice (∼130 mg/dL). Blood glucose was allowed to recover over 60 minutes either spontaneously or by 20% dextrose administration (i.p). Twenty-four hours later, the brain microvessels (BMVs) were isolated, and tandem mass tag (TMT)–based quantitative proteomics was performed using liquid chromatography-mass spectrometry (LC/MS). When compared to control, ASH significantly downregulated 13 proteins (p ≤ 0.05) whereas 23 proteins showed a strong trend toward decrease (p ≤ 0.10). When compared to AMH, ASH significantly induced the expression of 35 proteins with 13 proteins showing an increasing trend. AMH downregulated only 3 proteins. ASH-induced downregulated proteins are involved in actin cytoskeleton maintenance needed for cell shape and migration which are critical for blood-brain barrier maintenance and angiogenesis. In contrast, ASH-induced upregulated proteins are RNA-binding proteins involved in RNA splicing, transport, and stability. Thus, ASH alters BMV proteomics to impair cytoskeletal integrity and RNA processing which are critical for cerebrovascular function.

show abstract