Cellular and Molecular Pathology (CMP)
Graduate Training Program
 

Faculty and Their Research Interests

   Faculty Index

  BulletDr. Badylak
  BulletDr. Becich
  BulletDr. D. Becker
  BulletDr. J. Becker
  BulletDr. Billiar
  BulletDr. Blair
  BulletDr. Bostwick
  BulletDr. Bowser
  BulletDr. Chaillet
  BulletDr. Chang
  BulletDr. Cheng
  BulletDr. Chu
  BulletDr. Clemens
  BulletDr. DeFrances
  BulletDr. Delude
  BulletDr. Demetris
  BulletDr. Dong
  BulletDr. Donnenberg
  BulletDr. Duensing
  BulletDr. Fox
  BulletDr. Gandhi
  BulletDr. Giannoukakis
  BulletDr. Gnarra
  BulletDr. Grandis
  BulletDr. Hackam
  BulletDr. Hebda
  BulletDr. Huard
  BulletDr. Kaminski
  BulletDr. Katyal
  BulletDr. Kelavkar
  BulletDr. Klunk
  BulletDr. Kulich
  BulletDr. Lagasse
  BulletDr. Latimer
  BulletDr. Luyuan Li
  BulletDr. Yong Li
  BulletDr. Youhua Liu
  BulletDr. Lokshin
  BulletDr. Lokshin
  BulletDr. Luo
  BulletDr. Lyons-Weiler
  BulletDr. Mars
  BulletDr. Michalopoulos
  BulletDr. Monga
  BulletDr. Nikiforov
  BulletDr. Ochoa
  BulletDr. O'Keefe
  BulletDr. Oltvai
  BulletDr. Oury
  BulletDr. Pflug
  BulletDr. Piganelli
  BulletDr. Robinson
  BulletDr. Saunders
  BulletDr. Shapiro
  BulletDr. Stolz
  BulletDr. Strom
  BulletDr. Surti
  BulletDr. Vodovotz
  BulletDr. Vorp
  BulletDr. Wang
  BulletDr. Wells
  BulletDr. Wenzel
  BulletDr. Wiley
  BulletDr. Wu, C
  BulletDr. Yin
  BulletDr. Yu
  BulletDr. Zarnegar


V-line Lisa J. Robinson, M.D.
Assistant Professor of Pathology
Email: robinsonlj@upmc.edu

Research Interest:

Dr. Robinson's laboratory investigates signaling mechanisms involved in the regulation of normal and abnormal myelopoiesis. A major focus of current work is the regulation of osteoclast formation from myeloid precursors and its modulation by steroid hormones. This work has identified a key role for scaffolding proteins that mediate crosstalk between signals from TNF family members such as RANKL and non-genomic effects of steroid hormone receptors. Other work examines how crosstalk between signaling pathways, dependent on scaffolding proteins, determines the balance of proliferative versus differentiative effects on hematopoietic cytokines on myeloid precursors.

Representative Publication

Robinson LJ, Yaroslavskiy BB, Griswold RD, Zadorozny EV, Guo L, Tourkova IL, Blair HC. Estrogen inhibits RANKL-stimulated osteoclastic differentiation of human monocytes through estrogen and RANKL-regulated interactions of estrogen receptor-alpha with BCAR1 and Traf6. Experimental Cell Research, 315; 2009: 1287-1301.

Wang L, Xue J, Zadorozny EV, Robinson LJ. G-CSF stimulates Jak2-dependent Gab2 phosphorylation leading to Erk1/2 activation and cell proliferation. Cellular Signalling, 20; 2008: 1890-1899.

Yaroslavskiy BB, Sharrow AC, Wells A, Robinson LJ, Blair HC. Necessity of inositol (1,4,5)-trisphosphate receptor 1 and mu-calpain in NO-induced osteoclast motility. Journal of Cell Science 120; 2007: 2884-94.

Robinson, LJ, Borysenko CW, Blair HC. Tumor Necrosis Factor Family Receptors Regulating Bone Turnover: New Observations in Osteoblastic and Osteoclastic Cell Lines. Annals of the New York Academy of Sciences 1116; 2007: 432-443.

Robinson LJ, Xue J, Corey SJ. Src tyrosine kinases are activated by Flt3 and are involved in the proliferative effects of leukemia-associated Flt3 mutations. Experimental Hematology, 33; 2005: 469-479.

Garcia-Palacios V, Robinson LJ, Borysenko CW, Kalla SE, Blair HC. Negative regulation of RANKL-induced osteoclastic differentiation in RAW264.7 cells by estrogen and phytoestrogens. Journal of Biological Chemistry, 280; 2005: 13720-13727.

Blair HC, Robinson LJ, Zaidi M. Osteoclast signaling pathways. Biochemical and Biophysical Research Communications 328; 2005: 728-738.

Zhu QS, Robinson LJ, Roginskaya V, Corey SJ. G-CSF-induced tyrosine phosphorylation of Gab2 is Lyn kinase dependent and associated with enhanced Akt and differentiative, not proliferative, responses. Blood 103; 2004: 3305-3312.

Shaul PW, Smart EJ, Robinson LJ, German Z, Yuhanna IS, Ying Y, Anderson RGW, Michel T. Acylation targets endothelial nitric oxide synthase to plasmalemmal caveolae. Journal of Biological Chemistry 271; 1996: 6518-6522.

Robinson LJ, Michel T. Mutagenesis of palmitoylation sites in endothelial nitric oxide synthase identifies a novel motif for dual acylation and subcellular targeting. Proceedings of the National Academy of Sciences USA 92; 1995: 11776-11780.

Robinson LJ, Busconi L and Michel T. Agonist-modulated palmitoylation of endothelial nitric oxide synthase. Journal of Biological Chemistry 270; 1995: 995-998.



 

University of Pittsburgh
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