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Faculty Detail    
Campus Address MCLM 350A Zip 0005
Phone  205-934-3441
Other websites

Faculty Appointment(s)
Appointment Type Department Division Rank
Primary  Cell, Developmntl, & Integrative Biology  Cell, Developmntl, & Integrative Biology Professor
Secondary  Biomedical Engineering  Biomedical Engineering Associate Professor
Secondary  Cell Biology (Org Ret)  Cell Biology (Org Ret) Associate Professor
Center  Arthritis & Musculoskeletal Diseases Center (Org Ret)  Arthritis & Musculoskeletal Diseases Center (Org Ret) Professor
Center  Biomedical Engineering  Biomatrix Eng Regen Med (BERM) Ctr Professor
Center  Pathology   Cell Adhesion & Matrix Research Center Professor
Center  Center for Biophysical Sciences/Engineering  Center for Biophysical Sciences/Engineering Professor
Center  Comp Arthritis, MSK, Bone & Autoimmunity Ctr  Comp Arthritis, MSK, Bone & Autoimmunity Ctr Professor
Center  Comprehensive Cancer Center  Comprehensive Cancer Center Professor
Center  General Clinical Research Center  Ctr for Clinical & Translational Sci Professor
Center  GL Ctr for Craniofacial, Oral, & Dental Disorders  GL Ctr for Craniofacial, Oral, & Dental Disorders Professor
Center  Medicine  Ctr Cardiovasc Bio (Org Ret) Professor
Center  Medicine  Gene Therapy Center Professor
Center  Neurology   Multiple Sclerosis Center Professor
Center  General Clinical Research Center  Nephrology Research & Training Center Professor

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

Biographical Sketch 
I received a Ph.D. in Biochemistry from the University of Rhode Island in 1993. My postdoctoral research, performed at the SUNY Health Science Center in Syracuse, NY, was centered on understanding cell/matrix interactions. Since my arrival at UAB in 1998, I have continued to focus my research in the general area of cell adhesion and matrix biology.

Society Memberships
Organization Name Position Held Org Link
American Association for Cancer Research     
American Society for Biochemistry and Molecular Biology     
American Society for Cell Biology     
American Society for Matrix Biology     
Society for Biomaterials     
Society for Glycobiology     

Research/Clinical Interest
Cell/matrix interactions in disease and tissue regeneration
There are two principal projects in the Bellis laboratory: (1) Role of receptor glycosylation in regulating cell migration and survival. The addition of the negatively-charged sugar, sialic acid, to selected cell surface receptors has a significant impact on receptor function. Our laboratory has determined that the ST6Gal-I glycosyltransferase adds sialic acids to selected integrin and death receptors and thereby regulates cell adhesion, migration and apoptosis. Using cell model systems and genetically engineered mice, we have shown that ST6Gal-I-mediated sialylation controls integrin preference for matrix molecules, and also blocks apoptotic signaling from the Fas and TNFR1 death receptors. Collectively these molecular pathways are hypothesized to regulate the migration and survival of both immune cells and epithelial tumor cells. The broad goal of our research is to elucidate the mechanistic basis for sialylation-dependent receptor signaling, and to determine whether manipulating sialylation levels can be used as a clinical treatment for pathologies such as autoimmune disorders and metastatic cancer. (2) Biomimetic electrospun matrices for bone repair. The goal of this project is to create bone-like synthetic matrices for bone repair and regeneration. Electrospinning technology is being used to generate composite nanoscale fibrous matrices that incorporate a synthetic polymer (to control tensile strength and degradation kinetics) and two natural bone matrix molecules, collagen I and hydroxyapatite (HA). These composite matrices support robust mesenchymal stem cell (MSC) survival and proliferation in vitro, and also stimulate substantial new bone formation when implanted into bone defects. To further enhance the osteogenic properties of the substrates, the matrices are being functionalized with bioactive factors such as PDGF-BB, a potent chemotactic and proliferative factor for MSCs, and BMP-2, which stimulates MSCs to undergo osteoblastic differentiation. In complementary studies, we are developing novel methods for improving the bonding of bioactive proteins and peptides to HA-containing electrospun substrates. Our broad objective is to synthesize bone-mimicking matrices that, when implanted, stimulate recruitment and osteoblastic differentiation of the patientís mesenchymal stem cells, leading to accelerated bone regeneration.

Selected Publications 
Publication PUBMEDID
Phipps, MC, Clem, WC, Grunda, JM, Clines, GA, and Bellis, SL (2012) Increasing the pore sizes of bone-mimetic electrospun scaffolds comprised of polycaprolactone, collagen I and hydroxyapatite to enhance cell infiltration. Biomaterials, 33: 524-34   
Liu, Z, Swindall, AF, Kesterson, RA, Schoeb, TR, Bullard, DC, and Bellis, SL (2011) ST6Gal-I regulates macrophage apoptosis via alpha2-6 sialylation of the TNFR1 death receptor, J Biol Chem 286: 39654-62   
Swindall, AF and Bellis, SL (2011) Sialylation of the Fas death receptor by ST6Gal-I provides protection against Fas-mediated apoptosis in colon carcinoma cells. J Biol Chem, 286: 22982-22990 (Selected as Editor's Choice manuscript, Science Signaling)   
Bellis, SL (2011) Advantages of RGD peptides for directing cell association with biomaterials, Biomaterials, 32: 4205-4210   
Phipps, MC, Clem WC, Catledge, SA, Xu, Y, Hennessy, KM, Thomas, V, Jablonsky, MJ, Chowdhury, S, Stanishevsky, AV, Vohra, YK and Bellis, SL (2011) Mesenchymal stem cell responses to bone-mimetic electrospun matrices composed of polycaprolactone, collagen I and nanoparticulate hydroxyapatite. PLoS One, 6: e16813   
Zhuo, Y and Bellis, SL (2011) Emerging role of alpha2-6 sialic acid as a negative regulator of galectin binding and function. J Biol Chem, 286: 5935-594   

integrin, death receptors, cell adhesion, apoptosis, signal transduction, glycosylation, extracellular matrix, bone, biomaterials, tissue engineering