Clinical Focus

  • Cardiovascular Disease
  • Heart Failure
  • Heart Transplantation
  • Advanced heart failure

Academic Appointments

Administrative Appointments

  • Medical Director, Heart Failure Disease Management Program, VA Palo Alto Health Care System, VAPHCS (2014 - 2016)

Honors & Awards

  • Cardiovascular Institute Postdoctoral Travel Award, Stanford University (2014)
  • T32 Training Grant- Mechanisms & Innovation in Vascular Disease, National Institutes of Health (2011)

Professional Education

  • Board Certification: Advanced Heart Failure and Transplant Cardiology, American Board of Internal Medicine (2014)
  • Fellowship:Stanford University (2013) CA
  • Board Certification: Cardiovascular Disease, American Board of Internal Medicine (2012)
  • Fellowship:Stanford University (2012) CA
  • Board Certification: Internal Medicine, American Board of Internal Medicine (2009)
  • Residency:Beth Israel Deaconess Medical Center (2009) MA
  • Medical Education:Georgetown University (2006) DC

Research & Scholarship

Clinical Trials

  • Efficacy, Safety and Tolerability of Serelaxin When Added to Standard Therapy in AHF Recruiting

    The purpose of the study to evaluate the efficacy, safety and tolerability of intravenous infusion of serelaxin, when added to standard therapy, in acute heart failure (AHF) patients.

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  • Left Atrial Pressure Monitoring to Optimize Heart Failure Therapy Not Recruiting

    The purpose of this clinical study is to evaluate the safety and clinical effectiveness of use of a physician-directed, patient self-management system, guided by left atrial pressure measurements, for use in patients with heart failure. The system allows patients to adjust their HF medications daily based on a physician-directed prescription plan and their current HF status, similar to the manner in which diabetes patients manage their insulin therapy. The goal of the LAPTOP-HF study is to demonstrate reductions in episodes of worsening heart failure (HF) and hospitalizations in patients who are managed with the left atrial pressure (LAP) management system (treatment group) versus those who receive only the current standard of care (control group).

    Stanford is currently not accepting patients for this trial.

    View full details


All Publications

  • Treatment of left ventricular assist device-associated arteriovenous malformations with thalidomide. ASAIO journal Ray, R., Kale, P. P., Ha, R., Banerjee, D. 2014; 60 (4): 482-483


    Gastrointestinal bleeding due to arteriovenous malformations (AVM) is an increasingly recognized complication of continuous flow left ventricular assist devices (LVAD). Currently, therapeutic options for LVAD-associated AVMs are limited and often require repeated endoscopic procedures and reduction or cessation of anticoagulation. Thalidomide has been utilized in the treatment of refractory bleeding due to gastrointestinal vascular malformations. Here we describe the case of a 66-year-old patient with severe ischemic cardiomyopathy implanted with a continuous flow Heartmate II. His post-operative course was complicated by multiple hospital admissions for gastrointestinal bleeding due to LVAD-associated AVMs refractory to repeated argon plasma laser coagulation (APC). Anticoagulation was discontinued with subsequent pump stoppage due to thrombus requiring urgent surgical pump exchange. Following this, thalidomide was initiated and anticoagulation with warfarin was continued. Since initiation of thalidomide, the patient has not had further gastrointestinal bleeding or evidence of pump thrombus in the subsequent 1 year.

    View details for DOI 10.1097/MAT.0000000000000087

    View details for PubMedID 24830804

  • Effects on neurite outgrowth and cell survival of a secreted fibroblast growth factor binding protein-upregulated during spinal cord injury AMERICAN JOURNAL OF PHYSIOLOGY-REGULATORY INTEGRATIVE AND COMPARATIVE PHYSIOLOGY Tassi, E., Walter, S., Aigner, A., Cabal-Manzano, R. H., Ray, R., Reier, P. J., Wellstein, A. 2007; 293 (2): R775-R783


    The fibroblast growth factor binding protein (FGF-BP; GenBank accession no. NP_005121) is a secreted protein that mobilizes FGFs from the extracellular matrix, protects them from degradation, and enhances their biological activity. Several previous studies reported that FGF-BP is an early response gene upregulated during tissue repair processes including wound healing and atherogenesis. In this study we analyzed whether FGF-BP expression was impacted by spinal cord injury and could have an effect on neuronal cell viability. Immunohistochemical and in situ hybridization studies revealed a dramatic upregulation of FGF-BP protein and mRNA levels following unilateral hemisection and contusion injury of adult rat spinal cord. In spinal cord sections of laminectomized rats, increased FGF-BP expression was observed in the fibers and cell bodies ipsilateral to the lesion site but was absent in the uninjured spinal cord tissue contralateral to the lesion. Increased expression of FGF-BP was observed at all postinjury time points, examined with peak levels occurring at day 4, a time when injury-induced increased levels of FGF2 have also been reported to be maximal. Moreover, using PC12 cells as a neuronal model, we observed that exogenous FGF-BP increased the capacity of FGF2 to stimulate neurite outgrowth and to increase cell survival. At the molecular level, FGF-BP enhanced FGF2-induced protein tyrosine phosphorylation and AKT/PKB activation. Collectively, these results suggest that FGF-BP is an early response gene after spinal cord injury and that its upregulation in regenerating spinal cord tissue may provide a molecular mechanism for enhancing the initial FGF2-mediated neurotrophic effects occurring after such tissue damage.

    View details for DOI 10.1152/ajpregu.00737.2006

    View details for Web of Science ID 000248726600030

    View details for PubMedID 17553847

  • Up-regulation of fibroblast growth factor-binding protein, by beta-catenin during colon carcinogenesis CANCER RESEARCH Ray, R., Cabal-Manzano, R., Moser, A. R., Waldman, T., Zipper, L. M., Aigner, A., BYERS, S. W., Riegel, A. T., Wellstein, A. 2003; 63 (23): 8085-8089


    Fibroblast growth factor-binding protein (FGF-BP) releases immobilized FGFs from the extracellular matrix and can function as an angiogenic switch molecule in cancer. Here we show that FGF-BP is up-regulated in early dysplastic lesions of the human colon that are typically associated with a loss of adenomatous polyposis coli and up-regulation of beta-catenin. In addition, FGF-BP expression is induced in dysplastic lesions in ApcMin/+ mice in parallel with the up-regulation of beta-catenin. Also, in cell culture studies FGF-BP is induced by beta-catenin through direct activation of the FGF-BP gene promoter. We conclude that FGF-BP is a target gene of beta-catenin.

    View details for Web of Science ID 000187450900003

    View details for PubMedID 14678957

  • Serum induction of the fibroblast growth factor-binding protein (FGF-BP) is mediated through ERK and p38 MAP kinase activation and C/EBP-regulated transcription ONCOGENE Harris, V. K., Kagan, B. L., Ray, R., Coticchia, C. M., Liaudet-Coopman, E. D., Wellstein, A., Riegel, A. T. 2001; 20 (14): 1730-1738


    The fibroblast growth factor-binding protein (FGF-BP) modulates FGF activity through binding and release from the extracellular matrix. Consequently, the expression of FGF-BP in certain tumor types is a rate-limiting regulator of FGF-mediated angiogenesis. FGF-BP is upregulated in squamous cell carcinoma by treatment with mitogens such as EGF or TPA. In this study, we investigated the regulation of FGF-BP gene expression by serum. Treatment of serum-starved ME-180 cells with fetal bovine serum (FBS) resulted in a rapid increase in steady-state levels of FGF-BP mRNA and in the rate of FGF-BP gene transcription. Serum induction of FGF-BP mRNA was not mediated through EGF receptor activation but was dependent on PKC, as well as ERK kinase (MEK) and p38 MAP kinase activation. Promoter analysis showed that C/EBP is the main promoter element required for the serum response. Unlike EGF-activation of FGF-BP, transcriptional induction by serum is not significantly regulated through the AP-1 or E-box sites in the promoter. These results illustrate differences between the mechanism of induction in response to serum and EGF.

    View details for Web of Science ID 000167750900006

    View details for PubMedID 11313920