Current Role at Stanford

Director, Translational Applications Service Center (TASC)

Co-Director and Scientific Program Manager, Translational Research and Applied Medicine (TRAM) Program

Senior Research Scientist, Stanford School of Medicine

Member, Stanford Cancer Institute

Honors & Awards

  • College of Letters and Science Dean's Honor List, University of California - Berkeley (1988)
  • NIH Tumor Immunology Institutional Training Grant (NIH CA - 09120), NIH (1996, 1997, 2000)
  • National Cancer Institute Research Training Grant (PHS Grant Number CA09302), DHHS, National Cancer Institute (2004-2009)

Education & Certifications

  • PhD, University of California - Los Angeles (2000)
  • BS, University of California - Berkeley (1988)


Professional Interests

The Translational Research and Applied Medicine (TRAM) Program is designed to focus on removing barriers and communication gaps between scientists and clinicians, and bridging clinical and basic research is paramount to our mission. TRAM initiatives include didactic lectures and symposia, research facilities and pilot grants that support translational medicine projects of faculty, clinical fellows, residents and students. Our program was established to provide an infrastructure to rapidly translate novel genomic/proteomic, nanoscale and imaging research discoveries from the laboratory to the clinic and facilitate bench-to-bedside development of cellular therapies. We support diverse translational research projects that lead to innovative approaches to the prevention, early detection, diagnosis and treatment of various human diseases.

Translational Applications Service Center (TASC) facility is a fee-for-service research laboratory serving the Stanford University scientific community, as well as outside investigators. It offers a variety of analytical services, technical and scientific consulting and training, as well as pay-per-use research equipment, which allow investigators shared access to technologies that support innovative research in translational medicine. By providing centralized oversight and infrastructure for conducting translational research studies, as well as access to high-quality, cost-efficient, state-of-the-art proteomic, molecular and genomic technologies, TASC's overall mission is to serve as a comprehensive resource for accelerating the pace of advances in patient therapy and diagnosis by enhancing basic research in the early stages of translation to the clinical setting.


All Publications

  • A distinct evolution of the T-cell repertoire categorizes treatment refractory gastrointestinal acute graft-versus-host disease. Blood Meyer, E. H., Hsu, A. R., Liliental, J., Löhr, A., Florek, M., Zehnder, J. L., Strober, S., Lavori, P., Miklos, D. B., Johnson, D. S., Negrin, R. S. 2013; 121 (24): 4955-4962


    Steroid refractory gastrointestinal (GI) acute graft versus host disease (aGVHD) is a major cause of mortality in hematopoietic stem cell transplantation (HCT) without immune markers to establish a diagnosis or guide therapy. We found that T cell receptor ? (TCR?) CDR3 repertoire sequencing reveals patterns that could eventually serve as a disease biomarker of T cell alloreactivity in aGVHD. We identified T cell clones in GI biopsies in a heterogeneous group of 15 allogeneic HCT patients with GI aGVHD symptoms. Seven steroid-refractory aGVHD patients showed a more conserved TCR? clonal structure between different biopsy sites in the GI tract than eight primary-therapy responsive patients. Tracking GI clones identified at endoscopy longitudinally in the blood also revealed an increased clonal expansion in patients with steroid-refractory disease. Immune repertoire sequencing-based methods could enable a novel personalized way to guide diagnosis and therapy in diseases where T cell activity is a major determinant.

    View details for DOI 10.1182/blood-2013-03-489757

    View details for PubMedID 23652802

  • A distinct evolution of the T-cell repertoire categorizes treatment refractory gastrointestinal acute graft-versus-host disease BLOOD Meyer, E. H., Hsu, A. R., Liliental, J., Loehr, A., Florek, M., Zehnder, J. L., Strober, S., Lavori, P., Miklos, D. B., Johnson, D. S., Negrin, R. S. 2013; 121 (24): 4955-4962
  • The Expansion of Gastrointestinal-Associated alpha beta T Cell Clones in Peripheral Blood Associates with Severe Steroid Refractory GVHD BMT Tandem Meetings Meyer, E. H., Liliental, J. A., Florek, M., Lohr, A., Hsu, A., Johnson, D., Lavori, P., Zehnder, J. L., Miklos, D. B., Strober, S., Negrin, R. ELSEVIER SCIENCE INC. 2013: S334?S335
  • The Expansion of Gastrointestinal-associated alpha beta T Cell Clones in Peripheral Blood Over Time Is a Disease Feature of Severe Acute Graft-Versus-Host Disease 54th Annual Meeting and Exposition of the American-Society-of-Hematology (ASH) Meyer, E. H., Liliental, J., Florek, M., Loehr, A., Hsu, A., Johnson, D. S., Miklos, D. B., Zehnder, J. L., Negrin, R. S. AMER SOC HEMATOLOGY. 2012
  • Regulation of transcription of hypoxia-inducible factor-1 alpha (HIF-1 alpha) by heat shock factors HSF2 and HSF4 ONCOGENE Chen, R., Liliental, J. E., Kowalski, P. E., Lu, Q., Cohen, S. N. 2011; 30 (22): 2570-2580


    Hypoxia-inducible factor-1? (HIF-1?) is a principal regulator of angiogenesis and other cellular responses to hypoxic stress in both normal and tumor cells. To identify novel mechanisms that regulate expression of HIF-1?, we designed a genome-wide screen for expressed sequence tags (ESTs) that when transcribed in the antisense direction increase production of the HIF-1? target, vascular endothelial growth factor (VEGF), in human breast cancer cells. We discovered that heat shock factor (HSF) proteins 2 and 4-which previously have been implicated in the control of multiple genes that modulate cell growth and differentiation and protect against effects of environmental and cellular stresses-function together to maintain a steady state level of HIF-1? transcription and VEGF production in these cells. We show both HSFs bind to discontinuous heat shock element (HSE) sequences we identified in the HIF-1? promoter region and that downregulation of either HSF activates transcription of HIF-1?. We further demonstrate that HSF2 and HSF4 displace each other from HSF/HSE complexes in the HIF-1? promoter so that HIF-1? transcription is also activated by overexpression of either HSFs. These results argue that HSF2 and HSF4 regulate transcription of HIF-1? and that a critical balance between these HSF is required to maintain HIF-? expression in a repressed state. Our findings reveal a previously unsuspected role for HSFs in control of VEGF and other genes activated by canonical HIF-1?-mediated signaling.

    View details for DOI 10.1038/onc.2010.623

    View details for Web of Science ID 000291198400008

    View details for PubMedID 21258402

  • Genetic deletion of the Pten tumor suppressor gene promotes cell motility by activation of Rac1 and Cdc42 GTPases CURRENT BIOLOGY Liliental, J., Moon, S. Y., Lesche, R., Mamillapalli, R., Li, D. M., Zheng, Y., Sun, H., Wu, H. 2000; 10 (7): 401-404


    Pten (Phosphatase and tensin homolog deleted on chromosome 10) is a recently identified tumor suppressor gene which is deleted or mutated in a variety of primary human cancers and in three cancer predisposition syndromes [1]. Pten regulates apoptosis and cell cycle progression through its phosphatase activity on phosphatidylinositol (PI) 3,4,5-trisphosphate (PI(3,4,5)P(3)), a product of PI 3-kinase [2-5]. Pten has also been implicated in controlling cell migration [6], but the exact mechanism is not very clear. Using the isogenic Pten(+/+) and Pten(-/-) mouse fibroblast lines, here we show that Pten deficiency led to increased cell motility. Reintroducing the wild-type Pten, but not the catalytically inactive Pten C124S or lipid-phosphatase-deficient Pten G129E mutant, reduced the enhanced cell motility of Pten-deficient cells. Moreover, phosphorylation of the focal adhesion kinase p125(FAK) was not changed in Pten(-/-) cells. Instead, significant increases in the endogenous activities of Rac1 and Cdc42, two small GTPases involved in regulating the actin cytoskeleton [7], were observed in Pten(-/-) cells. Overexpression of dominant-negative mutant forms of Rac1 and Cdc42 reversed the cell migration phenotype of Pten(-/-) cells. Thus, our studies suggest that Pten negatively controls cell motility through its lipid phosphatase activity by down-regulating Rac1 and Cdc42.

    View details for Web of Science ID 000088978000018

    View details for PubMedID 10753747

  • PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt protein kinase B signaling pathway PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Sun, H., Lesche, R., Li, D. M., Liliental, J., Zhang, H., Gao, J., Gavrilova, N., Mueller, B., Liu, X., Wu, H. 1999; 96 (11): 6199-6204


    To investigate the molecular basis of PTEN-mediated tumor suppression, we introduced a null mutation into the mouse Pten gene by homologous recombination in embryonic stem (ES) cells. Pten-/- ES cells exhibited an increased growth rate and proliferated even in the absence of serum. ES cells lacking PTEN function also displayed advanced entry into S phase. This accelerated G1/S transition was accompanied by down-regulation of p27(KIP1), a major inhibitor for G1 cyclin-dependent kinases. Inactivation of PTEN in ES cells and in embryonic fibroblasts resulted in elevated levels of phosphatidylinositol 3,4,5,-trisphosphate, a product of phosphatidylinositol 3 kinase. Consequently, PTEN deficiency led to dosage-dependent increases in phosphorylation and activation of Akt/protein kinase B, a well-characterized target of the phosphatidylinositol 3 kinase signaling pathway. Akt activation increased Bad phosphorylation and promoted Pten-/- cell survival. Our studies suggest that PTEN regulates the phosphatidylinositol 3,4, 5,-trisphosphate and Akt signaling pathway and consequently modulates two critical cellular processes: cell cycle progression and cell survival.

    View details for Web of Science ID 000080527100054

    View details for PubMedID 10339565

  • Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit JOURNAL OF BIOLOGICAL CHEMISTRY Liliental, J., Chang, D. D. 1998; 273 (4): 2379-2383


    The integrin beta subunit cytoplasmic domains are important for activation-dependent cell adhesion and adhesion-dependent signaling events. We report an interaction between integrin beta subunit cytoplasmic domain and Rack1, a Trp-Asp (WD) repeat protein that has been shown to bind activated protein kinase C. The Rack1-binding site on integrin beta 2 subunit resides within a conserved, membrane-proximal region. In the yeast two-hybrid assay, WD repeats five to seven of Rack1 (Rack1-WD5/7) interact with integrin beta 1, beta 2, and beta 5 cytoplasmic domain. In eukaryotic cells, Rack1 co-immunoprecipitates with at least two different beta integrins, beta 1 integrins in 293T cells and beta 2 integrins in JY lymphoblastoid cells. Whereas Rack1-WD5/7 binds integrins constitutively, the association of full-length Rack1 to integrins in vivo requires a treatment with phorbol esters, which promotes cell spreading and adhesion. These findings suggest that Rack1 may link protein kinase C directly to integrins and participate in the regulation of integrin functions.

    View details for Web of Science ID 000071595200074

    View details for PubMedID 9442085

  • Native gel analysis of ribonucleoprotein complexes from a Leishmania tarentolae mitochondrial extract MOLECULAR AND BIOCHEMICAL PARASITOLOGY Peris, M., Simpson, A. M., Grunstein, J., Liliental, J. E., Frech, G. C., Simpson, L. 1997; 85 (1): 9-24


    Two polypeptides of 50 and 45 kDa were adenylated by incubation of a mitochondrial extract from Leishmania tarentolae with [alpha-32P]ATP. These proteins were components of a complex that sedimented at 20S in glycerol gradients and migrated as a single band of approximately 1800 kDa in a native gel. The facts that RNA ligase activity cosedimented at 20S and that the ATP-labeled p45 and p50 polypeptides were deadenylated upon incubation with a ligatable RNA substrate suggested that these proteins may represent charged intermediates of a mitochondrial RNA ligase. Hybridization of native gel blots with guide RNA (gRNA) probes showed the presence of gRNA in the previously identified T-IV complexes that sedimented in glycerol at 10S and contained terminal uridylyl transferase (TUTase) activity, and also in a previously unidentified class of heterodisperse complexes that sedimented throughout the gradient. gRNAs were not detected in the p45 + p50-containing 1800 kDa complex. The heterodisperse gRNA-containing complexes were sensitive to incubation at 27 degrees C and appear to represent complexes of T-IV subunits with mRNA. Polyclonal antiserum to a 70 kDa protein that purified with terminal uridylyl transferase activity was generated, and the antiserum was used to show that this p70 polypeptide was a component of both the T-IV and the heterodisperse gRNA-containing complexes. We propose that the p45 + p50-containing 1800 kDa complex and the p70 + gRNA-containing heterodisperse complexes interact in the editing process. Further characterization of these various complexes should increase our knowledge of the biochemical mechanisms involved in RNA editing.

    View details for Web of Science ID A1997WR49200002

    View details for PubMedID 9108545

  • T cell receptor usage by cytotoxic T lymphocytes against autologous human melanoma ANTICANCER RESEARCH Leong, S. P., Liliental, J., Krams, S. M., Zhou, Y. M., GRANBERRY, M. E., Martinez, O. M. 1996; 16 (6B): 3355-3361


    T cell receptor (TCR) usage by tumor infiltrating lymphocytes (TIL) represents the host's response to autologous melanoma (AM). The goal of this study is it determine TCR usage by cytotoxic T lymphocytes (CTL) against AM.CTL were generated from three patients using lymphocytes from metastatic or tumor-draining lymph nodes by repeated in vitro sensitization (IVS). Total RNA was isolated from CTL and reverse-transcribed to cDNA. TCR usage was determined by polymerase chain reaction (PCR) using TCR primers.Cytolytic activity was non-specific within the first 2-4 weeks following IVS and TCR repertoire in these cultures revealed random V alpha and V beta gene usage. In contrast, by 6-10 weeks of culture, cytolysis was specifically directed against AM cells and such specific cytolysis was significantly correlated with TCR V alpha 1 (P < 0.001).TCR V alpha 1 is associated with a common restricted melanoma antigen.

    View details for Web of Science ID A1996WB83600001

    View details for PubMedID 9042192

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