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Deliang Cao, Medical Microbiology, Immunology and Cell Biology Faculty - SIU School of Medicine


Our Faculty

Delian Cao

Deliang Cao
Associate Professor
Cross Appointment with Simmons Cancer Institute


Dr. Cao is an Associate Professor in the Department of Medical Microbiology, Immunology and Cell Biology at SIU School of Medicine and a member of the Simmons Cancer Institute. Dr. Cao is a member of the American Association of Cancer Research and a member of the American Society for Biochemistry and Molecular Biology.

Dr. Cao was the recipient of AACR - Aventis Scholar-in-Training Award (2002) and AACR - AstraZeneca Scholar-in-Training Award (2003).


  • Bachelor in Medicine (1984), Nanhua University School of Medicine, China
  • Ph.D. in Molecular Biology (1996), University of Hong Kong, Hong Kong

Academic Appointments

2008-present Associate Professor (tenured), Department of Medical Microbiology, Immunology, and Cell Biology, Simmons Cancer Institute, Southern Illinois University School of Medicine, Springfield, IL 62794-9626

2005-2008 Assistant Professor (tenure track), Department of Medical Microbiology, Immunology, and Cell Biology, Simmons Cancer Institute, Southern Illinois University School of Medicine, Springfield, IL 62794-9626

2000-2005 Associate Research Scientist, Department of Internal Medicine (Oncology), Yale University School of Medicine. 333 Cedar Street, New Haven, CT 06520-8032

1997-2000 Postdoctoral Associate, Department of Pharmacology, Yale University School of Medicine. 333 Cedar Street, New Haven, CT 06520-8032

Research Focus:

Physiopathological Function of Aldo-Keto Reductase 1B10 (AKR1B10)
AKR1B10 is a main research project ongoing in my laboratory that has been supported by NCI and DoD Breast Cancer Research Program. We have published 16 peer-reviewed research articles plus several review article on AKR1B10, leading the AKR1B10 studies internationally.

AKR1B10 is a new member of aldo-keto reductase (AKR) superfamily that we first isolated in human hepatocellular carcinoma (HCC). In human normal tissues, AKR1B10 is specifically expressed in epithelial cells of the gastrointestinal tract (GT), with a detectable level in the liver. AKR1B10 is not expressed in the breast and lung. In diseased tissues, AKR1B10 is upregulated in breast, lung and colon cancers but oppositely, down regulated in ulcerative colitis (UC) and colitis-associated colorectal cancers. The essential biological functions of AKR1B10 described thus far include 1) a NADPH-dependent reductase, reducing carbonyl groups, and 2) a mediator of long chain fatty acid de novo synthesis. Our studies on AKR1B10 focus on two fields:

(a) AKR1B10 as a oncogenic promoter of breast cancer

We found that AKR1B10 is overexpressed in breast cancer and promotes growth and metastasis of breast cancers to lymph nodes. Through clearance of electrophilic carbonyls metabolically produced in tumor cells, AKR1B10 protects the host cells from carbonyl and subsequent oxidative damage. By promoting long chain fatty acid/lipid synthesis, AKR1B10 activates lipid second messenger-mediated PKC/ERK signaling pathway, promoting tumor cell proliferation, migration and invasion. We are currently digging the possibility of developing AKR1B10-target therapeutics or molecular diagnosis for breast cancer.

(b) AKR1B10 as a regulator of colonic epithelium

AKR1B10 is primarily expressed in colon epithelial cells, but its expression is diminished or lost in UC and UC-associated colorectal cancer. Colonic epithelium is featured with (1) constant self-renewal and (2) carbonyl stress derived from diets and luminal microbes. Our studies demonstrated that AKR1B10 specifically expressed in the epithelial cells of colon promotes their proliferation and migration, and protects them from carbonyl lesions. AKR1B8 (an ortholog of human AKR1B10 in the mouse) knockout leads to diminished epithelial proliferation and injury repair, as well as increased DNA damage of the colonic epithelium. The colonic mucosa of AKR1B8 mice was highly susceptible to dextran sodium sulfate (DSS)-induced colitis and colitis (inflammation)-associated cancer. We are currently digging the underlying mechanisms

Tumor suppressive role of NF-κB RelA/p65

NF-KB RelA/p65 has long been recognized as an oncogenic transcriptional factor and a target for anticancer therapy. Evidence is emerging recently that RelA/p65 functions as a tumor suppressor, but the underlying mechanisms are not well known. Studies in our laboratory have shown that phosphomimetic mutation at Ser536 of RelA/p65 gene induces dramatic apoptosis and senescence through changing the expression of a large group of cell death and survival genes. Our testing hypothesis is that phosphorylation and activation of specific sites in RelA/p65 may switch the face of RelA/p65 as an oncogene or a tumor suppressor.

Experimental therapeutics and drug resistance

Chemotherapy still stands for a main option for patients with late stage cancers when a targeted therapy is unavailable or becomes resistant. Using gene transfer, RNA interference, and gene knockout technologies, we investigate the metabolic pathways and molecular mechanisms affecting antitumor activity and tumor selectivity of cytotoxic agents, i.e., fluoropyrimidines and anthracyclines. For translations, we explore rapid, easy methods to monitor activity of the metabolic pathways and effectors. Our final goal is to provide evidence and methodologies for the individualization of the chemotherapeutic agents.


  1. ARL-1 SPECIFIC ANTIBODY (U.S. Application #: 12/032327; Patent #: 8114604,02/14/2012)
  2. METHODS FOR DIAGNOSING BOWEL DISEASE (U.S. Application #: 12/739371, 10/24/2008; Patent #: 8551720,10/08/2013)
  3. ARL-1 SPECIFIC ANTIBODIES AND USES THEREOF (U.S. Application #: 13/017618,01/31/2011; ; Patent #: 8685666,04/01/2014)

Selected Peer-Reviewed Papers within 10 years (* Corresponding author)

  1. Bu Y, Li X, He Y, Shen Y, Huang C, Cao Y, Huang D, Cai C, Wang Y, Wang Z, Liao DF, and *Cao D. A phosphomimetic mutant of RelA/p65 at Ser536 induces apoptosis and senescence: an implication for tumor-suppressive role of Ser536 phosphorylation. Int. J. Cancer. In Revision
  2. Shen, Y., Ma, J., Yan, R., Ling, H., Li, X., Yang, W., Gao, J., Huang, C., Bu, Y., He, Y., Wan, L., Huang, M. C., Stenson, W. F., Liao, D. F., *Cao D. Impaired self-renewal and increased colitis and dysplastic lesions in colonic mucosa of akr1b8 deficient mice. Clin. Cancer Res. 2014 Dec 23. pii: clincanres.2072.2014. [Epub ahead of print]
  3. Luo, D., Bu, Y., Ma, J., Rajput, S., He, Y., Cai, G., Liao, D, and *Cao, D. Heat shock protein 90-α mediates aldo-keto reductase 1 B10 (AKR1B10) protein secretion through secretory lysosomes. J. Biol. Chem. 288:36733-36740, 2013 (Featured online on Global Medical Discovery [ISSN 1929-8536])
  4. Ma, J., Luo, D.X., Huang, C., Shen, Y., Bu, Y., Markwell, S., Gao, J., Liu, J., Zu, X., Cao, Z., Gao, Z., Lu, F., Liao, D.F., *Cao, D. AKR1B10 overexpression in breast cancer: association with tumor size, lymph node metastasis and patient survival and its potential as a novel serum marker. Int. J. Cancer. 131(6):E862-871, 2012 (Reader Comment)
  5. Liu, Z., Yan, R., Al-Salman, A., Shen, Y., Bu, Y., Ma, J., Luo, D. X., Huang, C., Jiang, Y., Wilber, A., Mo, Y. Y., Huang, M., Zhao, Y., *Cao, D. Epidermal growth factor induces tumor marker AKR1B10 expression through activator protein-1 signaling in hepatocellular carcinoma cells. Biochem. J. 442(2):2732-82, 2012
  6. Cao, D., Ziemba, A. J., McCabe, J., Yan, R., Wan, L., Kim, B., Gach, H. M., Flynn, S., Pizzorno, G. Differential expression of uridine phosphorylase in tumors contributes to an improved fluoropyrimidines therapeutic activity. Mol. Cancer Ther. 10(12):2330-9, 2011
  7. Zhong, L., Shen, H., Huang, C., Jing, H., and *Cao, D. AKR1B10 induces cell resistance to daunorubicin and idarubicin by reducing C13 ketonic group. Toxicol. Appl. Pharmacol. 255(1):40-47, 2011
  8. Luo, D.X., Huang, M., Ma, J., Gao, Z., Liao, D.F., and *Cao, D. Aldo-keto reductase family 1 member B10 protein is secreted through a lysosome-mediated nonclassical pathway. Biochem. J. 438(1): 71-80, 2011
  9. Shen, Y., Zhong, L., Johnson, S., and *Cao, D. Human aldo-keto reductases 1B1 and 1B10: A comparative study on their enzyme activity toward electrophilic carbonyl compounds. Chem. Biol. Interact. 191: 192-198, 2011. PMID: 21329684
  10. Pandey, P.R., Okuda, H., Watabe, M., Pai, S.K., Liu, W., Kobayashi, A., Xing, F., Fukuda, K., Hirota, S., Sugai, T., Wakabayashi, G., Koeda, K., Kashiwaba, M., Suzuki, K., Chiba, T., Endo, M., Fujioka., T, Tanji, S., Mo, Y.Y., Cao, D., Wilber, A.C., and Watabe, K. Resveratrol suppresses growth of cancer stem-like cells by inhibiting fatty acid synthase. Breast Cancer Res. Treat. 130(2):387-98, 2011. PMID: 21188630
  11. Zu, X., Ma, j., Liu, X., Liu, F., Tan, C., Yu, L., Wang, J., Xie, Z., Cao, D., and Jiang, Y. Pro-oncogene Pokemon promotes breast cancer progression by upregulating survivin expression. Breast Cancer Res. 10;13(2):R26, 2011. PMID: 21392388
  12. Shen, Y., Zhong, L., Markwell, S., and *Cao, D. Thiol-disulfide exchanges modulate aldo-keto reductase family 1 member B10 activity and sensitivity to inhibitors. Biochimie. 92(5):530-7, 2010
  13. Joshi, A., Rajput, S., Wang, C., and *Cao, D. Murine aldo-keto reductase family 1 subfamily B: Identification of AKR1B8 as an ortholog of human AKR1B10. Biol. Chem. 391(12):1371-8, 2010. PMID: 21087085
  14. Wang, C., Yan, R., Luo, D., Watabe, K., Liao, D.L., and *Cao, D. Aldo-keto reductase family 1 member B10 promotes cell survival by regulating lipid synthesis and eliminating carbonyls. J. Biol. Chem. 284(39):26742-8, 2009
  15. Zhong, L., Liu, Z., Yan, R., Johnson, S., Fang, X., and *Cao, D. Aldo-Keto reductase family 1 B10 protein detoxifies alpha, beta-unsaturated carbonyls at physiological levels. Biochem. Biophys. Res. Commun. 387(2):245-250, 2009
  16. Liu, Z., Zhong, L., Krishack, P.A., Robbins, S., Cao, J.X., Zhao, Y., Chung, S.S., and *Cao, D. Structure and promoter characterization of aldo-keto reductase family 1 B10 gene. Gene. 437(1-2):39-44, 2009
  17. Wang, C., Xu, C., Sun, M., Liao, D.L., and *Cao, D. Acetyl-CoA carboxylase-α inhibitor TOFA induces human cancer cell apoptosis. Biochem. Biophys. Res. Commun. 385(3):302-306, 2009
  18. Ma, J., Yan, R., Zu, X., Cheng, J.M., Rao K., Liao, D.F., and *Cao, D. Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl-CoA carboxylase-alpha in breast cancer cells. J. Biol. Chem. 283(6):3418-3423, 2008
  19. Zu, X., Yan, R., Robbins, S., Krishack, P., Liao, D., and *Cao, D. Reduced 293T cell susceptibility to acrolein due to aldose reductase-like-1 protein expression. Toxicol. Sci. 97:562-568, 2007
  20. Yan, R., Zu, X., Ma, J. Liu, Z., Adeyanju, M., Liao, D. and *Cao, D. Aldo-keto reductase family 1B10 gene silencing results in growth inhibition of colorectal cancer cell: Implication for cancer intervention. Int. J. Cancer. 121: 2301-2306, 2007
  21. Cao, D., Leffert, J. J. McCabe, J., Kim, B., and Pizzorno, G. Abnormalities in uridine homeostatic regulation and pyrimidine nucleotide metabolism as a consequence of the deletion of the uridine phosphorylase gene. J. Biol. Chem. 280: 21169-21175, 2005
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