Expression and Significance of BNIP3 in Clear Cell Renal Cell Carcinoma

HUANG Long, ZHAO Tao, TIAN Yi-yang.et al

Abstract

To investigate the expression of proapoptosis protein BNIP3 in clear cell renal cell carcinoma (ccRCC) and its clinical significance. Methods The RCC tumor tissue samples from 30 pathologically diagnosed ccRCC and their adjacent pericarcinous tissues were adopted to detect the mRNA and protein expressions of BNIP3, von Hippel-Lindau(VHL), hypoxia inducible factor (HIF)-1α and vascular enothelial growth factor (VEGF) by real-time quantitative PCR(real-time PCR) and Western blot. The correlations of these genes' expressions with clinicopathologic features were analyzed. Results The expression levels of BNIP3 and VHL were lower in ccRCC tissues than those in pericarcinous tissues (P<0.05), but the mRNA expression levels of HIF-1α and VEGF were higher in ccRCC tissues than those in pericarcinous tissues (P<0.05). The lower level expression of BNIP3 in ccRCC was not related with any clinicopathologic features. No significant correlation was observed between the BNIP3 mRNA and protein level with the expressions of VHL, HIF-1α and VEGF. Conclusion In ccRCC, the expression of BNIP3 is decreased, which not correlated with the expression levels of VHL, HIF-1α and VEGF.

 

Keywords: Clear cell renal cell carcinoma, BNIP3 HIF-1α VEGF, Real-time PCR, Western blot 

 

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References


Lewis RV, Stern AS. Biosynthesis of the enkephalins and enkephalin-containing polypeptides. Annu Rev Pharmacol Toxicol, 1983; 23:353-372.

Comb M. Rosen H. Seeburg P. et al. Primary structure of the human proenkephalin gene. DNA,1983;2(3);213-229.

Pittius CW. Seizinger HR. Mehraein P. et al. Proenkephalin- A-derived peptides are present in human brain. Life Sci,1983; 33( 1): 41 -44.

Imura H, Nakai Y, Nakao K. et al. Biosynthesis and distribution of opioid peptides. J Endocrinol Invest. 1983;6(2): 139-149.

Kojima K. Structure of proenkephalin. Tanpakushitsu Kakusan Koso,1983;28(6):815-833.

Gera G. Maremmani I.Capovani В, et al. Long-acting opioid- agonists in the treatment of heroin addiction: why should we call them, substitution’. Subst Use Misuse. 2009; 44 ( 5 ): 663- 671.

Glorioso JC, Fink DJ. Gene therapy for pain; introduction to the special issue. Gene Ther,2009; 16(4);453-454.

Federici T, Boulis N. Gene therapy for peripheral nervous systea diseases. Curr Gene Ther, 2007;7(4):239-248.

Pinto M, Castro AR.Tshudy F,et al. Opioids modulate pain facilitation from the dorsal reticular nucleus. Mol Cell Neu, 2008;39(4):50.

Xu W.Sanz A. Pardo L,et al. Activation of the mu opioid re¬ceptor involves conformational rearrangements of multiple transmembrane domains. Biochemistry, 2008; 47 (40 ); 10576 - 10586.

Lemos MV, Menezes H. The effect of an immune RNA (RNAi) against Trypanosoma Cruzi infection in mice. Trop Med Parasitol ,1978; 29(1); 119-126.

Gojobori T, Nei M. Inter-RNA homology and possible roles of small RNAs. J Mol Evol,1981; 17(4) :245-250.

Harp PA. RNAi and double-strand RNA. Genes Dev,1999;13 (2) : 139-141.

Artemova N, Bumagina Z. Opioid peptides derived from food proteins suppress aggregation and promote reactivation of partly unfolded stressed proteins. Peptides,2009? 11(25):332- 338.

Sarkar DK,Zhang CQ, Murugan S, et al. Transplantation of beta-endorphin neurons into the hypothalamus promotes immune function and restricts the growth and metastasis of mammary carcinoma. Cancer Res, 2001;71 (19);6282-6291.

Karayiannakis AJ, Zbar A, Makri, et al. Serum beta- endorphin levels in morbidly obese patients; the effect of vertical banded gastroplasty. Eur Surg Res, 1998;30(6): 409- 413.

Seaki T, Nishimura M, Sato N, et al. Electrophysiological demonstration and activation of mu-opioid receptors in the rabbit sinoatrial node. J Cardiovasc Pharmacol, 1995; 26( 1 ); 160-168.


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