Dr. Paul Pang is a postdoctoral fellow at the Stanford Cardiovascular Institute with research interests in disease modeling, clinical genomics, precision medicine, and drug discovery. Dr. Pang received his Ph.D. in Integrative Molecular and Biomedical Sciences studying the alternative splicing of SCN5A in the heart and the effects of its misregulation in diseases such as myotonic dystrophy. During his Ph.D. training, he was a recipient of the NIH T32 and F31 NRSA Predoctoral Fellowships, Claude W. Smith Fellowship Award, and Dean's Award of Excellence among numerous presentation and travel awards from the Muscular Dystrophy Association and the American Heart Association. During his postdoctoral training, Dr. Pang has been awarded NIH T32 and F32 NRSA Postdoctoral Fellowships to investigate muscular dystrophies with a focus on personalized medicine and drug discovery.

Honors & Awards

  • NIH Ruth L. Kirschstein F32 Postdoctoral Fellowship, National Institutes of Health/NHLBI (2020)
  • NIH NRSA T32 Postdoctoral Training Grant, National Institutes of Health/NHLBI, Stanford University (2019)
  • Best Platform Presentation, International Myotonic Dystrophy Consortium (2019)
  • Travel Award, International Myotonic Dystrophy Consortium, Muscular Dystrophy Association (2019)
  • Best Poster Presentation, Baylor College of Medicine, IMBS Graduate Program (2019)
  • Claude W. Smith Fellowship for Excellence in Research, Baylor College of Medicine (2018)
  • Best Seminar Presentation, Baylor College of Medicine, IMBS Graduate Program (2018)
  • Best Graduate Oral Presentation, Baylor College of Medicine, Dept of Molecular Physiology and Biophysics (2018)
  • NIH Ruth L. Kirschstein F31 Predoctoral Fellowship, National Institutes of Health/NHLBI (2018)
  • Top Abstract Award, Baylor College of Medicine, Cardiovascular Research Institute (2017)
  • Dean's Award of Excellence, Baylor College of Medicine (2017)
  • Abstract Travel Award, American Heart Association (2017)
  • Travel Award, International Myotonic Dystrophy Consortium, Muscular Dystrophy Association (2017)
  • NIH NRSA T32 Predoctoral Training Grant, National Institutes of Health/NHLBI, Baylor College of Medicine (2016)

Professional Education

  • Ph.D., Baylor College of Medicine (2019)
  • M.A., Harvard University (2015)
  • M.A., Boston University (2013)
  • B.S., University of Maryland, College Park (2011)

Stanford Advisors

Lab Affiliations

All Publications

  • miR-218 Expressed in Endothelial Progenitor Cells Contributes to the Development and Repair of the Kidney Microvasculature. The American journal of pathology Wang, X. n., Liu, J. n., Yin, W. n., Abdi, F. n., Pang, P. D., Fucci, Q. A., Abbott, M. n., Chang, S. L., Steele, G. n., Patel, A. n., Mori, Y. n., Zhang, A. n., Zhu, S. n., Lu, T. S., Kibel, A. S., Wang, B. n., Lim, K. n., Siedlecki, A. M. 2020; 190 (3): 642–59


    Ischemia due to hypoperfusion is one of the most common forms of acute kidney injury. We hypothesized that kidney hypoxia initiates the up-regulation of miR-218 expression in endothelial progenitor cells (EPCs) to guide endocapillary repair. Murine renal artery-derived EPCs (CD34+/CD105-) showed down-regulation of mmu-Mir218-5p/U6 RNA ratio after ischemic injury, while in human renal arteries, MIR218-5p expression was up-regulated after ischemic injury. MIR218 expression was clarified in cell culture experiments in which increases in both SLIT3 and MIR218-2-5p expressions were observed after 5 minutes of hypoxia. ROBO1 transcript, a downstream target of MIR218-2-5p, showed inverse expression to MIR218-2-5p. EPCs transfected with a MIR218-5p inhibitor in three-dimensional normoxic culture showed premature capillary formation. Organized progenitor cell movement was reconstituted when cells were co-transfected with Dicer siRNA and low-dose Mir218-5p mimic. A Mir218-2 knockout was generated to assess the significance of miR-218-2 in a mammalian model. Mir218-2-5p expression was decreased in Mir218-2-/- embryos at E16.5. Mir218-2-/- decreased CD34+ angioblasts in the ureteric bud at E16.5 and were nonviable. Mir218-2+/- decreased peritubular capillary density at postnatal day 14 and increased serum creatinine after ischemia in adult mice. Systemic injection of miR-218-5p decreased serum creatinine after injury. These experiments demonstrate that miR-218 expression can be triggered by hypoxia and modulates EPC migration in the kidney.

    View details for DOI 10.1016/j.ajpath.2019.11.014

    View details for PubMedID 31972158

  • KLF4 Represses DYRK2 Inhibition of Self-renewal and Survival Through c-Myc and p53 in Leukemia Stem/Progenitor Cells. Blood Park, C. S., Lewis, A. H., Chen, T. J., Bridges, C. S., Shen, Y. n., Suppipat, K. n., Puppi, M. n., Tomolonis, J. A., Pang, P. D., Mistretta, T. A., Ma, L. n., Green, M. R., Rau, R. n., Lacorazza, H. D. 2019


    Leukemia stem cells are a rare population with a primitive progenitor phenotype that can initiate, sustain, and recapitulate leukemia through a poorly understood mechanism of self-renewal. Here, we report that KLF4 promotes disease progression in a murine model of chronic myeloid leukemia (CML)-like myeloproliferative neoplasia by repressing an inhibitory mechanism of preservation in leukemia stem/progenitor cells with leukemia-initiating capacity. Deletion of the Klf4 gene severely abrogated the maintenance of BCR-ABL1(p210)-induced CML by impairing survival and self-renewal in BCR-ABL1+ CD150+ LSK leukemic cells. Mechanistically, KLF4 repressed the Dyrk2 gene in leukemic stem/progenitor cells; thus, loss of KLF4 resulted in elevated levels of DYRK2 kinase, which were associated with inhibition of survival and self-renewal via depletion of c-Myc protein and p53 activation. In addition to transcriptional regulation, stabilization of DYRK2 protein by inhibiting ubiquitin E3 ligase SIAH2 with vitamin K3 promoted apoptosis and abrogated self-renewal in murine and human CML stem/progenitor cells. Altogether, our results suggest that DYRK2 is a molecular checkpoint controlling both p53 and c-Myc-mediated regulation of survival and self-renewal in CML cells with leukemic-initiating capacity that can be targeted with small molecules.

    View details for DOI 10.1182/blood.2018875922

    View details for PubMedID 31515251

  • CRISPR -Mediated Expression of the Fetal Scn5a Isoform in Adult Mice Causes Conduction Defects and Arrhythmias. Journal of the American Heart Association Pang, P. D., Alsina, K. M., Cao, S. n., Koushik, A. B., Wehrens, X. H., Cooper, T. A. 2018; 7 (19): e010393


    Background The sodium channel, Nav1.5, encoded by SCN 5A, undergoes developmentally regulated splicing from inclusion of exon 6A in the fetal heart to exon 6B in adults. These mutually exclusive exons differ in 7 amino acids altering the electrophysiological properties of the Nav1.5 channel. In myotonic dystrophy type 1, SCN 5A is mis-spliced such that the fetal pattern of exon 6A inclusion is detected in adult hearts. Cardiac manifestations of myotonic dystrophy type 1 include conduction defects and arrhythmias and are the second-leading cause of death. Methods and Results This work aimed to determine the impact of SCN 5A mis-splicing on cardiac function. We used clustered regularly interspaced short palindromic repeat ( CRISPR) /CRISPR-associated protein 9 (Cas9) to delete Scn5a exon 6B in mice, thereby redirecting splicing toward exon 6A. These mice exhibit prolonged PR and QRS intervals, slowed conduction velocity, extended action potential duration, and are highly susceptible to arrhythmias. Conclusions Our findings highlight a nonmutational pathological mechanism of arrhythmias and conduction defects as a result of mis-splicing of the predominant cardiac sodium channel. Animals homozygous for the deleted exon express only the fetal isoform and have more-severe phenotypes than heterozygotes that also express the adult isoform. This observation is directly relevant to myotonic dystrophy type 1, and possibly pathological arrhythmias, in which individuals differ with regard to the ratios of the isoforms expressed.

    View details for DOI 10.1161/JAHA.118.010393

    View details for PubMedID 30371314

    View details for PubMedCentralID PMC6404881

  • Pre-clinical model of severe glutathione peroxidase-3 deficiency and chronic kidney disease results in coronary artery thrombosis and depressed left ventricular function. Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association Pang, P. n., Abbott, M. n., Abdi, M. n., Fucci, Q. A., Chauhan, N. n., Mistri, M. n., Proctor, B. n., Chin, M. n., Wang, B. n., Yin, W. n., Lu, T. S., Halim, A. n., Lim, K. n., Handy, D. E., Loscalzo, J. n., Siedlecki, A. M. 2018; 33 (6): 923–34


    Chronic kidney disease (CKD) patients have deficient levels of glutathione peroxidase-3 (GPx3). We hypothesized that GPx3 deficiency may lead to cardiovascular disease in the presence of chronic kidney disease due to an accumulation of reactive oxygen species and decreased microvascular perfusion of the myocardium. Methods. To isolate the exclusive effect of GPx3 deficiency in kidney disease-induced cardiac disease, we studied the GPx3 knockout mouse strain (GPx3-/-) in the setting of surgery-induced CKD. Results. Ribonucleic acid (RNA) microarray screening of non-stimulated GPx3-/- heart tissue show increased expression of genes associated with cardiomyopathy including myh7, plac9, serpine1 and cd74 compared with wild-type (WT) controls. GPx3-/- mice underwent surgically induced renal mass reduction to generate a model of CKD. GPx3-/- + CKD mice underwent echocardiography 4 weeks after injury. Fractional shortening (FS) was decreased to 32.9 ± 5.8% in GPx3-/- + CKD compared to 62.0% ± 10.3 in WT + CKD (P < 0.001). Platelet aggregates were increased in the myocardium of GPx3-/- + CKD. Asymmetric dimethylarginine (ADMA) levels were increased in both GPx3-/- + CKD and WT+ CKD. ADMA stimulated spontaneous platelet aggregation more quickly in washed platelets from GPx3-/-. In vitro platelet aggregation was enhanced in samples from GPx3-/- + CKD. Platelet aggregation in GPx3-/- + CKD samples was mitigated after in vivo administration of ebselen, a glutathione peroxidase mimetic. FS improved in GPx3-/- + CKD mice after ebselen treatment.These results suggest GPx3 deficiency is a substantive contributing factor to the development of kidney disease-induced cardiac disease.

    View details for DOI 10.1093/ndt/gfx304

    View details for PubMedID 29244159

    View details for PubMedCentralID PMC5982720

  • Human vascular progenitor cells derived from renal arteries are endothelial-like and assist in the repair of injured renal capillary networks. Kidney international Pang, P. n., Abbott, M. n., Chang, S. L., Abdi, M. n., Chauhan, N. n., Mistri, M. n., Ghofrani, J. n., Fucci, Q. A., Walker, C. n., Leonardi, C. n., Grady, S. n., Halim, A. n., Hoffman, R. n., Lu, T. n., Cao, H. n., Tullius, S. G., Malek, S. n., Kumar, S. n., Steele, G. n., Kibel, A. n., Freedman, B. S., Waikar, S. S., Siedlecki, A. M. 2017; 91 (1): 129–43


    Vascular progenitor cells show promise for the treatment of microvasculature endothelial injury. We investigated the function of renal artery progenitor cells derived from radical nephrectomy patients, in animal models of acute ischemic and hyperperfusion injuries. Present in human adventitia, CD34positive/CD105negative cells were clonal and expressed transcription factors Sox2/Oct4 as well as surface markers CXCR4 (CD184)/KDR(CD309) consistent with endothelial progenitor cells. Termed renal artery-derived vascular progenitor cells (RAPC), injected cells were associated with decreased serum creatinine after ischemia/reperfusion, reduced albuminuria after hyperperfusion, and improved blood flow in both models. A small population of RAPC integrated with the renal microvasculature following either experimental injury. At a cellular level, RAPC promoted local endothelial migration in co-culture. Profiling of RAPC microRNA identified high levels of miRNA 218; also found at high levels in exosomes isolated from RAPC conditioned media after cell contact for 24 hours. After hydrogen peroxide-induced endothelial injury, RAPC exosomes harbored Robo-1 transcript; a gene known to be regulated by mir218. Such exosomes enhanced endothelial cell migration in culture in the absence of RAPC. Thus, our work shows the feasibility of pre-emptive pro-angiogenic progenitor cell procurement from a targeted patient population and potential therapeutic use in the form of autologous cell transplantation.

    View details for DOI 10.1016/j.kint.2016.07.037

    View details for PubMedID 27692806

    View details for PubMedCentralID PMC5179298

  • RGS4 inhibits angiotensin II signaling and macrophage localization during renal reperfusion injury independent of vasospasm. Kidney international Pang, P. n., Jin, X. n., Proctor, B. M., Farley, M. n., Roy, N. n., Chin, M. S., von Andrian, U. H., Vollmann, E. n., Perro, M. n., Hoffman, R. J., Chung, J. n., Chauhan, N. n., Mistri, M. n., Muslin, A. J., Bonventre, J. V., Siedlecki, A. M. 2015; 87 (4): 771–83


    Vascular inflammation is a major contributor to the severity of acute kidney injury. In the context of vasospasm-independent reperfusion injury we studied the potential anti-inflammatory role of the Gα-related RGS protein, RGS4. Transgenic RGS4 mice were resistant to 25 min injury, although post-ischemic renal arteriolar diameter was equal to the wild type early after injury. A 10 min unilateral injury was performed to study reperfusion without vasospasm. Eighteen hours after injury, blood flow was decreased in the inner cortex of wild-type mice with preservation of tubular architecture. Angiotensin II levels in the kidneys of wild-type and transgenic mice were elevated in a sub-vasoconstrictive range 12 and 18 h after injury. Angiotensin II stimulated pre-glomerular vascular smooth muscle cells (VSMCs) to secrete the macrophage chemoattractant RANTES, a process decreased by angiotensin II R2 (AT2) inhibition. However, RANTES increased when RGS4 expression was suppressed implicating Gα protein activation in an AT2-RGS4-dependent pathway. RGS4 function, specific to VSMC, was tested in a conditional VSMC-specific RGS4 knockout showing high macrophage density by T2 MRI compared with transgenic and non-transgenic mice after the 10 min injury. Arteriolar diameter of this knockout was unchanged at successive time points after injury. Thus, RGS4 expression, specific to renal VSMC, inhibits angiotensin II-mediated cytokine signaling and macrophage recruitment during reperfusion, distinct from vasomotor regulation.

    View details for DOI 10.1038/ki.2014.364

    View details for PubMedID 25469849

    View details for PubMedCentralID PMC4382433

  • Sox9 Activation Highlights a Cellular Pathway of Renal Repair in the Acutely Injured Mammalian Kidney. Cell reports Kumar, S. n., Liu, J. n., Pang, P. n., Krautzberger, A. M., Reginensi, A. n., Akiyama, H. n., Schedl, A. n., Humphreys, B. D., McMahon, A. P. 2015; 12 (8): 1325–38


    After acute kidney injury (AKI), surviving cells within the nephron proliferate and repair. We identify Sox9 as an acute epithelial stress response in renal regeneration. Translational profiling after AKI revealed a rapid upregulation of Sox9 within proximal tubule (PT) cells, the nephron cell type most vulnerable to AKI. Descendants of Sox9(+) cells generate the bulk of the nephron during development and regenerate functional PT epithelium after AKI-induced reactivation of Sox9 after renal injury. After restoration of renal function post-AKI, persistent Sox9 expression highlights regions of unresolved damage within injured nephrons. Inactivation of Sox9 in PT cells pre-injury indicates that Sox9 is required for the normal course of post-AKI recovery. These findings link Sox9 to cell intrinsic mechanisms regulating development and repair of the mammalian nephron.

    View details for DOI 10.1016/j.celrep.2015.07.034

    View details for PubMedID 26279573