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Faculty Detail    
Name YANG YANG
 
Campus Address WTI 320A Zip 3300
Phone  205-996-6228
E-mail  yangyang@uab.edu
Other websites
     

Education
Medical School  China Medical University, China    1982  M.D. 
Graduate  Third Military Medical University, China     1989  PhD 


Faculty Appointment(s)
Appointment Type Department Division Rank
Primary  Pathology   Molecular & Cellular Pathology Associate Professor
Center  Center for Metabolic Bone Disease  Center for Metabolic Bone Disease Associate Professor
Center  Comprehensive Cancer Center  Comprehensive Cancer Center Associate Professor
Center  General Clinical Research Center  Ctr for Clinical & Translational Sci Associate Professor

Graduate Biomedical Sciences Affiliations
Cancer Biology 
Cell, Molecular, & Developmental Biology 
Medical Scientist Training Program 
Pathobiology and Molecular Medicine 

Biographical Sketch 
Dr. Yang received her M.D. degree from China Medical University and PhD degree from Third Military Medical University, China. She completed postdoctoral training and was appointed as an Assistant Professor in the Department of Pathology, University of Arkansas for Medical Sciences. Dr. Yang joined the faculty of Department of Pathology at UAB in 2006. She is currently an Associate Professor and Principal Investigator in the Division of Molecular and Cellular Pathology.

Society Memberships
Organization Name Position Held Org Link
American Association for Cancer Research   Member   
American Association for Matrix   Member   
American Society for Bone and Mineral Research  Member   
American Society of Hematology   Member   
International Bone and Mineral Society   Member   
Metastasis Research Society   Member   

Research/Clinical Interest
Title
Multiple myeloma and tumor microenvironment
Description
My lab is focused on the role of tumor microenvironment in multiple myeloma (MM), cancer-related bone diseases and the translational research of MM. MM is a B-lymphoid malignancy characterized by tumor cell infiltration of the bone marrow, osteolytic lesions, and angiogenesis in the vicinity of the tumor cells. Although new treatments have improved the outlook for patients with MM, it remains an incurable disease. (1) Syndecan-1 in myeloma. Syndecan-1 is the dominant heparan sulfate (HS) proteoglycan expressed on the surface of MM cells and a marker of MM. Syndecam-1 can be shed from the MM cell surface and high levels of syndecan-1 in MM patient sera are an indicator of poor prognosis. We demonstrated that the shed syndecan-1 is not simply an indicator of poor prognosis, but it actively promotes the growth and dissemination of myeloma tumors. Moreover, we discovered that syndecan-1 shedding is stimulated by heparanase expressed in myeloma cells. These important discoveries have been published in Blood (2002) and JBC (2007), which have been cited numerous times in peer-reviewed journals. (2) Heparanase in MM and MM-related bone diseases. Heparanase-1 (heparanase) is an endo-beta-glucuronidase that specifically cleaves the saccharide chains of HS proteoglycans, and is upregulated in a variety of human tumors, including MM. In MM, We demonstrated that heparanase drives tumor growth, angiogenesis and metastasis and thus plays a major role in promoting the progression of this cancer. Recently, we discovered that heparanase promotes bone resorption and inhibits bone formation in MM through secreting soluble factors. Our work on heparanase has been published in high ranking journals (e.g., Blood, JBC, and Cancer Research) and presented orally at many international meetings. (3)The role of Runx2 in MM. This is a new research direction of my lab. Runx2, a member of the runt-related gene family, is well-known for its essential regulatory roles in the chondro-osteoblast lineage and bone formation. Accumulated evidence indicates that various cancer cells (e.g., breast, prostate, uterine, thyroid, colon and pancreatic cancers) also express Runx2 and that tumor-derived Runx2 is correlated with the aggressive tumor phenotype, including bone-metastasis and osteolysis. We currently study the role of both MM cell-derived Runx2 and Osteoblast-derived Runx2 in MM progression in bone. This study will provide novel insights into MM pathology and identify novel potential therapeutic targets.

Selected Publications 
Publication PUBMEDID
Adhami, M.D.; Rashid, H.; Chen, H; Yang, Y; Javed, A. Loss of Runx2 in committed osteoblasts impairs postnatal skeletogenesis. J Bone Miner Res. 2015 Jan; 30(1):71-82.   25079226 
Trotter, T.N., Li, M., Pan, Q., Li, J; Peker, D., Rowan P.D., Suva, L.J., Javed, A., and Yang, Y. Myeloma cell-derived Runx2 promotes myeloma progression in bone. Blood 2015 Apr 10. pii: blood-2014-12-613968. [Epub ahead of print]   
Daft, P.G., Yang, Y., and Zayzafoon, M. The growth and aggressive behavior of human osteosarcoma is regulated by a CaMKII-controlled autocrine VEGF signaling mechanism. PLOS ONE 2015 Apr 10; 10(4):e0121568. doi: 10.1371/journal.pone.0121568.    
Ruan, J., Trotter, T.N., Nan, L., Luo, R., Javed, A., Sanderson, R.D., Suva, L.J., Yang, Y. Heparanase inhibits osteoblastogenesis and shifts bone marrow progenitor cell fate in myeloma bone disease. Bone 2013, 57(1):10–17.   3786009 
Ritchie, J.P., Ramani, V.C., Naggi, A., Torri, G., Casu, B., Pisano, C., Carminati, P., Tortoreto, M., Zunino, F., Vlodavsky, I., Sanderson, R.D. and Yang, Y. SST0001, a chemically modified heparin, inhibits myeloma growth and angiogenesis via disruption of the heparanase/ syndecan-1 axis. Clinical Cancer Research 2011; 17(6):1382-93.  3060291 
Yang, Y., Ren, R., Ramani, V.C., Nan, L., Suva, L.J., and Sanderson, R.D. Heparanase enhances local and systemic osteolysis in multiple myeloma by upregulating the expression and secretion of RANKL. Cancer Res 2010; 70(21): 8329-38.  2970667 
Yang Y, MacLeod V, Dai Y, Khotskaya-Sample Y, Shriver Z, Venkataraman G, Sasisekharan R, Naggi A, Torri G, Casu B, Vlodavsky I, Suva, Epstein J, Yaccoby S, Shaughnessy JD, Barlogie B and Sanderson RD: The syndecan-1 heparan sulfate proteoglycan is a viable target for myeloma therapy. Blood 2007; 110(6): 2041-8.   1976367 
Yang, Y., Macleod, V., Bendre, M., Huang, Y., Theus, A.M, Miao, H.Q., Kussie, P., Yaccoby, S., Epstein, J., Suva, L.J., Kelly, T., and Sanderson, R.D. Heparanase promotes the spontaneous metastasis of myeloma cells to bone. Blood 2005; 105 (3): 1303-1309.   

Keywords
multiple myeloma, Runx2, tumor microenvironment, cancer-related bone diseases, syndecan-1, heparanase