Shao Laboratory

Rong Shao, M.D., Ph.D.

Telephone: 413.794.9568
Fax: 413.794.0857
Email
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Scientist, PVLSI
Adjunct Research Assistant Professor, Veterinary & Animal Sciences, University of Massachusetts Amherst

Education

M.D., Shanghai Second Medical University
M.S., Shanghai Second Medical University
Ph.D., Philadelphia College of Pharmacy and Science

Postdoctoral Experience

Research Associate, Liver Center Laboratory, Duke University Medical Center, 1997-2000
Research Associate, Department of Pharmacology and Cancer Biology, Duke University Medical Center, 2000-2004

Activity of angiogenic factors in breast cancer development

Breast cancer is one of the most life-threatening diseases among women in this country and the incidence of the disease is still gradually increasing every year. Although early diagnosis and treatment of breast cancer have much improved, mortality at the later stage of the cancer remains static. In the better understanding of breast cancer progression, our lab focuses on the identification of molecular mechanisms in cancer angiogenesis and metastasis. Tumor angiogenesis, the new vasculature formation from pre-existing blood vessels, is a fundamental process required for tumor growth. The angiogenic switch is initially triggered by the ectopic production and elaboration of angiogenic factors that are mainly derived from tumor cells such as growth factors VEGF and bFGF. Those angiogenic molecules bind to specific membrane tyrosine kinase receptors to induce angiogenic signaling cascades in endothelial cells, a major component of the blood vasculature. The new vasculature developed by the endothelial cells in turn facilitates tumor growth and expansion. In addition, the tumor angiogenesis is frequently associated with tumor metastasis, a process that is mainly characterized by tumor cells. Metastatic tumor cells are capable of defying constrains of tissue boundaries and migrating into a new terrain to develop secondary colonies.

We have found that the molecules secreted from cancerous cells such as periostin are markedly elevated in cancer patients and they exert angiogenic and metastatic function in cancer progression. The increased levels of those factors in the blood will serve as biomarkers for the diagnosis and prognosis in the later stage of cancer development.

Working Groups:
Breast Cancer Working Group
Center of Excellence in Apoptosis Research

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Selected papers:

W. Yan and R. Shao. Transduction of a mesenchyme-specific gene periostin into 293T cells induces cell invasive activity through epithelial-mesenchymal transformation. J. Biol. Chem. 281: 19700-8, 2006.

R. Shao and Xing Guo. Human microvascular endothelial cells immortalized with hTERT: a model for the study of in vitro angiogenesis. Biochem. Bioph. Res. Co. 321, 788-794, 2004.

S. Bao, G. Ouyang, X. Bai, H. Zhi, C. Ma, M. Liu, R. Shao, R. Anderson, J. N. Rich and X-F. Wang. Periostin potently promotes metastatic growth of colon cancer by augmenting cell survival via the Akt/PKB pathway. Cancer Cell 5, 329-339, 2004.

R. Shao, S. Bao, X. Bai, C. Blanchette, R. Anderson, J. R. Mark and X-F. Wang. Acquired expression of periostin by breast cancers promotes tumor progression via enhancement of angiogenesis. Mol. Cell. Biol. 24, 3992-4003, 2004.

R. Shao, Z. Shi, P.J. Gotwals, V.E. Koteliansky and D.C.Rockey. Cell and molecular regulation of endothelin-1 production during hepatic wound healing. Mol. Biol. Cell 14,2327-2341, 2003.

C. Hubbert, A. Guardiola, R. Shao, Y. Kawaguchi, A. Ito, A. Nixon, M. Yoshida, X-F. Wang and T-P. Yao. HDAC6 is a microtubule-associated deacetylase. Nature 417 :455-458, 2002.

R. Shao and D.C. Rockey. Effects of endothelins on hepatic stallate cell synthesis of endothelin-1 during hepatic wound healing. J. Cell. Physiol. 191:342-350, 2002.

Q. Yu, R. Shao, H.S. Qian, S.E. George and D.C. Rockey. Gene transfer of the neuronal NO synthase isoform to cirrhotic rat liver ameliorates portal hypertension. J. Clin. Invest. 105:741-748,2000.

R. Shao, W. Yan and D. C. Rockey. Endothelin production is regulated by endothelin converting enzyme-1 in hepatic wound healing. J. Biol. Chem. 274: 3228-3234,1999.

R. Shao, S. Ring and J.B. Tarloff. Coincubation of rat renal proximal tubules with hepatic subcellular fractions potentiates the effects of para-aminophenol. Fund. Appl. Toxicol. 39:101-108, 1997.

R. Shao and J.B.Tarloff. Lack of correlation between para-aminophenol toxicity in vivo and in vitro in female Sprague-Dawley rats. Fund. Appl. Toxicol. 31:268-278, 1996.

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