BlalockBlalock    
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
   HomePagine personaliBlalock
William Blalock


 

Istituto di Genetica Molecolare - Sede di Bologna

c/o Istituto Ortopedico Rizzoli -via di Barbiano 1/10

40136 Bologna

 

Telefono: +39 051 6366769 

Email: william.blalockcnr.it

 

Education

1991:  Bachelor of Science (BS) in Biology from Wake Forest University, Winston-Salem, North Carolina 

1997: Master of Science (MS) in Biology from East Carolina University, Greenville, North Carolina.

2000: Doctor of Philosophy (PhD) in Microbiology and Immunology from Brody School of Medicine, East Carolina University, Greenville, North Carolina. 

 

Employment/ Training

2000-2005: Post-doctoral Research Associate, University of Florida Shands Cancer Center, Gainesville, Florida, USA.

2005-2007: Senior Scientist, Department of Innovative Therapy, Advanced Biotechnology Center/G. Gaslini Pediatric Institute, Genoa, Italy  

2007-2011: Senior Scientist, Cell Signaling Laboratory, Department of Human Anatomical Sciences, University of Bologna, Bologna, Italy.

2011-Present: Research Scientist, III Level, Institute of Molecular Genetics, National Research Council of Italy, UOS Bologna, Bologna, Italy.

 

Key Areas of Research

Inflammation, stress, nuclear signaling, acute leukemia, bone marrow failure disorders, osteosarcoma

 

 

Research Interests

My research is focused on inflammatory/stress-mediated signaling in the nucleus and how this signaling influences the progression of cancer and neuromuscular degeneration.  In particular, I am characterizing the role of the stress-activated kinase, PKR, in the nucleus.  Constitutive activation of PKR has been demonstrated in myelodysplastic syndromes, leukemia, breast cancer, melanoma, Alzheimer’s disease, Huntington’s corea and Creutzfeldt-Jakob syndrome.  In many of these diseases active PKR is localized exclusively to the nucleus.  PKR can influence diverse signaling pathways and thus multiple cellular functions, including eIF2a (translation), NF-kB (transcription/inflammation/angiogenesis), and p53 (DNA repair/transcription/cell cycle).  The majority of effort is being directed toward understanding the role of PKR signaling in the development and progression of cancer. Using proteomic methods (mass spectrometry, peptide arrays, HPLC, 2D electrophoresis), I am looking to identify the interactors and potentially novel substrates of PKR in the nucleus of cancer cells.  New interactors and substrates are to be validated by biological, molecular and cellular methods.  Moreover, as the kinases AKT and PKR are involved in converging signaling pathways which are induced by cytokines such as tumor necrosis factor (TNF)-a, insulin growth factor (IGF) and platelet derived growth factor (PDGF); and their signaling influences each other, we are examining proteins that serve as substrates and/or interactors of both kinases.

 

 

Recent Publications

  • Ramazzotti, G., Bavelloni, A., Blalock, W., Piazzi, M., Cocco, L. and Faenza, I.  BMP-2 Induced Expression of PLCβ1 That Is a Positive Regulator of Osteoblast Differentiation. (2015) J. Cell. Physiol. (In press).  doi: 10.1002/jcp.25107.
  • Bavelloni, A., Piazzi, M., Raffini, M., Faenza, I. and Blalock, WL.  Prohibitin 2: At a communications crossroads. (2015). IUBMB Life 67: 239-254.
  • Piazzi, M., Blalock, WL., Bavelloni, A., Faenza, I., Raffini, M., Tagliavini, F., Manzoli, L. and Cocco, L.  PI-PLCβ1b affects Akt activation, cyclin E expression, and caspase cleavage, promoting cell survival in pro-B-lymphoblastic cells exposed to oxidative stress. (2014). FASEB J. 
  • Bavelloni, A., Dmitrienko, GI., Goodfellow, VJ., Ghavami, A., Piazzi, M., Blalock, W., Chiarini, F., Cocco, L. and Faenza, I. PLCβ1a and PLCβ1b selective regulation and cyclin D3 modulation reduced by kinamycin F during k562 cell differentiation. (2015).  J. Cell. Physiol. 230: 587-594. 
  • Bavelloni, A., Poli, A., Fiume, R., Blalock, W., Matteucci, A., Ramazzotti, G., McCubrey, JA., Cocco, L. and Faenza, I.  PLC-beta 1 regulates the expression of miR-210 during mithramycin-mediated erythroid differentiation in K562 cells. (2014). Oncotarget 5: 4222-4231. 
  • Bavelloni, A., Piazzi, M., Faenza, I., Raffini, M., D'Angelo, A., Cattini, L., Cocco, L. and Blalock WL. Prohibitin 2 represents a novel nuclear AKT substrate during all-trans retinoic acid-induced differentiation of acute promyelocytic leukemia cells. (2014). FASEB J. 28: 2009-2019. 
  • Blalock, WL. (corresponding), Piazzi, M. (co-first author), Bavelloni, A., Raffini, M., Faenza, I., D'Angelo, A., and Cocco, L.  Identification of the PKR nuclear interactome reveals roles in ribosome biogenesis, mRNA processing and cell division. (2014). J. Cell. Physiol.  229: 1047-1060. 
  • Follo, MY., Faenza, I., Piazzi, M., Blalock, WL., Manzoli, L., McCubrey, JA. and Cocco, L.  Nuclear PI-PLCβ1: an appraisal on targets and pathology.  (2014). Adv. Biol. Regul. 54: 2-11. 
  • Piazzi, M., Blalock, WL., Bavelloni, A., Faenza, I., D'Angelo, A., Maraldi, NM. and Cocco, L. Phosphoinositide-specific phospholipase C β 1b (PI-PLCβ1b) interactome: affinity purification-mass spectrometry analysis of PI-PLCβ1b with nuclear protein. (2013). Mol. Cell. Proteomics 12: 2220-2235. 
  • Versura, P., Bavelloni, A., Blalock, W., Fresina, M. and Campos, EC.  A rapid standardized quantitative microfluidic system approach for evaluating human tear proteins. (2012). Mol. Vis. 18: 2526-2537. 
  • Faenza I, Blalock W., Bavelloni A, Shoser B, Fiume R, Pacella S, Piazzi M, D'Angelo A, and Cocco L.  A role for PLCβ1 in myotonic dystrophies type 1 and 2. (2012). FASEB J. 26: 3042-3048. 
  • Blalock,WL., Bavelloni,A., Piazzi,M., Tagliavini,F., Faenza,I., Martelli,AM., Follo,MY. and Cocco,L. Multiple forms of PKR present in the nuclei of acute leukemia cells represent an active kinase that is responsive to stress. (2011). Leukemia 25: 236-245. 

 


Copyright © 2014 Home