Bves

Official Full Name

blood vessel epicardial substance

Synonyms

BVES; blood vessel epicardial substance; HBVES; POP1; POPDC1; popeye domain containing 1; MGC42413; POP 1; POPDC 1; Popeye domain containing protein 1; Popeye protein 1; OTTHUMP00000016910; OTTHUMP00000016911; OTTHUMP00000242208; popeye domain-containing protein 1; POP1C protein; zgc:86887

Cat.No.	Product Name	Price
CSC-DC001600	Panoply™ Human BVES Knockdown Stable Cell Line	Inquiry
CSC-SC001600	Panoply™ Human BVES Over-expressing Stable Cell Line	Inquiry

Cat.No.	Product Name	Price
AD01974Z	Human BVES adenoviral particles	Inquiry
LV06445L	human BVES (NM_147147) lentivirus particles	Inquiry

Cat.No.	Product Name	Price
SHG108361	shRNA set against Rat Bves(NM_001077590.1)	Inquiry
SHG108389	shRNA set against Mouse Bves(NM_024285.2)	Inquiry
SHH248498	shRNA set against Human BVES (NM_007073.4)	Inquiry
SHH248502	shRNA set against Mouse BVES (NM_024285.2)	Inquiry
SHH248506	shRNA set against Rat BVES (NM_001077590.1)	Inquiry
SHW000026	shRNA set against Chicken BVES (NM_001001299)	Inquiry
SHW006142	shRNA set against Danio rerio BVES (NM_001001847)	Inquiry
SHW014094	shRNA set against Danio rerio BVES (NM_001257162)	Inquiry
SHW014095	shRNA set against Danio rerio BVES (NM_001257163)	Inquiry
SHW014096	shRNA set against Danio rerio BVES (NM_001257164)	Inquiry

Cat.No.	Product Name	Price
CDCB175569	Danio rerio BVES ORF Clone (NM_001257162)	Inquiry
CDFR004981	Rat Bves cDNA Clone(NM_001077590.1)	Inquiry
MiUTR1M-02323	BVES miRNA 3'UTR clone	Inquiry
MiUTR1R-00630	BVES miRNA 3'UTR clone	Inquiry
MiUTR4H-TG00879	BVES miRNA 3'UTR clone	Inquiry
CDCB161501	Chicken BVES ORF Clone (NM_001001299)	Inquiry
CDCB167617	Danio rerio BVES ORF Clone (NM_001001847)	Inquiry
CDCB175570	Danio rerio BVES ORF Clone (NM_001257163)	Inquiry
CDCB175571	Danio rerio BVES ORF Clone (NM_001257164)	Inquiry
CDCB189938	Rabbit BVES ORF clone (XM_002714830.2)	Inquiry
CDCR035840	Mouse Bves ORF clone (NM_024285.2)	Inquiry
CDCR372057	Rat Bves ORF Clone(NM_001077590.1)	Inquiry
CDCS409466	Human BVES ORF Clone (BC034425)	Inquiry
CDCS409467	Human BVES ORF Clone (BC040502)	Inquiry

Detailed Information

Recent Research Progress

Blood vessel epicardial substance (BVES) is a tight junction-associated protein that was originally found in cDNA screening of developing hearts. Studies over the past few years have revealed that not only BVES is expressed in heart and bone tissue, but also that BVES is also expressed throughout the gastrointestinal epithelium. Mice lacking BVES maintain more severe intestinal damage and inflammation. Furthermore, BVES is inhibited in gastrointestinal cancer, and mouse models show that loss of BVES promotes tumor formation. Recent studies from multiple laboratories have shown that BVES can regulate several molecular pathways, including cyclic adenosine monophosphate (cAMP), WNT, and promote the degradation of the oncogene c-Myc.

The absence of BVES promotes CAC

BVES mRNA is reduced by hypermethylation of the promoter in tumors from colitis-associated cancer (CAC) patients. Importantly, the hypermethylation of the BVES promoter is concurrently present in the distant non-malignant appearance mucosa. As seen in human patients, BVES are under-expressed in experimental inflammatory carcinogenesis, and BVES-/- mice have increased tumor diversity and dysplasia after azoxymethane (AOM)/ dextran sodium sulfate (DSS) administration. Molecular analysis of BVES-/- tumors showed elevated Wnt activation and c-Myc levels. In terms of mechanism, Bobak Parang et al. identified a novel signaling pathway, namely the interaction of BVES with the protein phosphatase 2A (PP2A) regulatory subunit PR61α, which mediates the destruction of cMyc. In conclusion, deletion of BVES promotes inflammatory tumor genesis through Wnt signaling and dysregulation of the oncogene c-Myc (Figure 1). The BVES promoter methylation status can be used as a CAC biomarker.

Figure 1. Working model of the role of BVES in regulating c-Myc degradation and CAC development (Parang Bobak, et al. GUT, 2017)

BVES inhibition triggers human hepatocellular carcinoma EMT

Metastasis contributes to a poor prognosis of hepatocellular carcinoma (HCC). However, the mechanism by which primary HCC cells develop into a metastatic phenotype remains unclear. Recently, investigations have shown that BVES was down-regulated in human liver cancer tissues and HCC cell lines with high metastatic potential. Ping Han et al. selected Huh7 cells (BVES high-level expressing cells) to study the role of BVES in HCC. After BVES inhibition, Huh7 cells exhibited some morphological changes, including cytoskeletal rearrangement and ligation disruption. Cell migration and invasion were increased concomitant with increased expression of vimentin, IL-6, MMP2, MMP9 and decreased expression of E-cadherin. Finally, the expression of the epithelial-mesenchymal transition (EMT) transcription factors Snail1 and Twist1 was significantly increased in BVES knockdown cells. These findings suggest that down-regulation of BVES in HCC induces EMT, thereby promoting invasion and metastasis of HCC cells.

BVES may be a potential target for enhancing heart protection

BVES play a role in muscle regeneration, heart rate regulation, hypoxia tolerance, and ischemic preconditioning. Expression of BVES is elevated in cardiomyocytes maintained in serum-free defined medium. BVES deficiency caused by small interfering RNA (siRNA)-mediated gene silencing leads to myocardial cell injury and death, up-regulation of pro-apoptotic protein Bcl-2/adenovirus E1B 19-kDa interacting protein 3 (Bnip3), as well as reduction in Rac1-GTPase activity and in Akt phosphorylation. Binding to BVES and Bnip3 silencing attenuated cell damage and prevented up-regulation of Bnip3 induced by BVES silencing alone. Chromatin immunoprecipitation indicated increased binding of the transcription factor FoxO3 to the Bnip3 promoter, although augmentation of FoxO3 in the nuclei was not detected. In contrast, the transcription factor NF-kB was excluded from the nucleus of BVES -deficient cardiomyocytes and exhibited reduced binding to the Bnip3 promoter. The data suggests that BVES regulates Bnip3 expression by altering Rac1 activity and FoxO3 and NF-kB transcription factors, maintaining cardiomyocyte viability in the absence of serum, pointing to BVES as a potential target for enhanced cardioprotection.

In conclusion, BVES regulates a variety of intracellular signaling pathways and is closely related to a variety of disease mechanisms. Although recent studies have elucidated the in vivo function of BVES, it remains to be seen how BVES plays a role in other tissues such as the lungs or breast. The production of tissue-specific BVES knockout mice will be the key to revealing its function.

References:

Parang Bobak, et al. BVES regulates c-Myc stability via PP2A and suppresses colitisinduced tumorigenesis. GUT, 2017, 66(5):852-862
Ping Han, et al. BVES Inhibition Triggers Epithelial-Mesenchymal Transition in Human Hepatocellular Carcinoma. Dig Dis Sciences ,2014, 59:992–1000
Vitaly Kliminski, et al. Popdc1/Bves Functions in the Preservation of Cardiomyocyte Viability While Affecting Rac1 Activity and Bnip3 Expression. Journal of Cellular Biochemistry. 2017, 118:1505–1517
Schindler Roland F. R, et al. POPDC1S201F causes muscular dystrophy and arrhythmia by affecting protein trafficking. The Journal of Clinical Investigation, 2016, 126(1):239-253
Bobak Parang, et al. Blood Vessel Epicardial Substance (BVES) in junctional signaling and cancer. Tissue barriers, 2018, 1-12

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