I grew up in a wonderful community in California, surrounded by old chicken farms and horses, living in the house that my great-grandfather built. I attended Lewis and Clark College in Portland, Oregon, a small liberal arts school where I became interested in the sciences and medicine. I then moved halfway across the country to St. Louis, Missouri, for a joint MD/PhD program with graduate training focused on the development and patterning of the fruit fly eye. Missing my family and California, I made my way back after graduation from medical school and completed my residency training at Stanford Children's Health/Lucile Packard Children's Hospital. I have been working as a hospitalist and pediatrician at Stanford Children's Health since graduating from residency.

I believe that pediatricians not only have the responsibility and privilege to care for children but also the opportunity to partner with parents in helping their children grow and develop over time. Parenthood can be incredibly rewarding and very challenging and every person's experience of being a parent is unique. I love working closely with families to promote their child's health, growth and development, whether that is while their baby is in the hospital after birth or as a pediatrician in the High Risk Infant Follow-Up Clinic at Stanford Children's Health. I also enjoy teaching and working with residents and medical students in both settings.

Academic Appointments

Honors & Awards

  • Resident as Teacher Award, Stanford Children's Hospital Residency Program (2012)
  • Alpha Omega Alpha, Alpha Omega Alpha Honor Medical Society (2009)
  • George F. Gill Prize in Pediatrics, Washington University in St. Louis (2009)
  • Glasgow-Rubin Memorial Achievement Citation, American Medical Women’s Association (2009)
  • Edmund V. Cowdry Prize in Histology, Washington University in St. Louis (2002)
  • Kehar S. Chouke-George Gill Prize in Anatomy, Washington University in St. Louis (2002)
  • Co-recipient of Senior Woman Award at Lewis and Clark College, American Association of University Women (1999)
  • Pamplin Society Fellow, Lewis and Clark College (1997)
  • Phi Beta Kappa, Phi Beta Kappa, Lewis and Clark College (1997)


All Publications

  • Epidemiology of Bacteremia in Previously Healthy Febrile Infants: A Follow-up Study. Hospital pediatrics Mischler, M., Ryan, M. S., Leyenaar, J. K., Markowsky, A., Seppa, M., Wood, K., Ren, J., Asche, C., Gigliotti, F., Biondi, E. 2015; 5 (6): 293-300


    Describe the etiology of bacteremia among a geographically diverse sample of previously well infants with fever admitted for general pediatric care and to characterize demographic and clinical characteristics of infants with bacteremia according to bacterial etiology. We hypothesized that the epidemiology of bacteremia in febrile infants from a geographically diverse cohort would show similar results to smaller or single-center cohorts previously reported.This was a retrospective review of positive, pathogenic blood cultures in previously healthy, febrile infants≤90 days old admitted to a general unit. In total, there were 17 participating sites from diverse geographic regions of the United States. Cultures were included if the results were positive for bacteria, obtained from an infant 90 days old or younger with a temperature≥38.0°C, analyzed using an automated detection system, and treated as pathogenic.Escherichia coli was the most prevalent species, followed by group B Streptococcus, Streptococcus viridans, and Staphylococcus aureus. Among the most prevalent bacteria, there was no association between gender and species (Ps>.05). Age at presentation was associated only with Streptococcus pneumoniae. There were no cases of Listeria monocytogenes.Our study confirms the data from smaller or single-center studies and suggests that the management of febrile well-appearing infants should change to reflect the current epidemiology of bacteremia. Further research is needed into the role of lumbar puncture, as well as the role of Listeria and Enterococcus species in infantile bacteremia.

    View details for DOI 10.1542/hpeds.2014-0121

    View details for PubMedID 26034160

  • Ajuba LIM Proteins Are Negative Regulators of the Hippo Signaling Pathway CURRENT BIOLOGY Das Thakur, M., Feng, Y., Jagannathan, R., Seppa, M. J., Skeath, J. B., Longmore, G. D. 2010; 20 (7): 657-662


    The mammalian Ajuba LIM proteins (Ajuba, LIMD1, and WTIP) are adaptor proteins that exhibit the potential to communicate cell adhesive events with nuclear responses to remodel epithelia. Determining their role in vivo, however, has been challenging due to overlapping tissue expression and functional redundancy. Thus, we turned to Drosophila, where a single gene, CG11063 or djub, exists. Drosophila lacking the djub gene or depleted of dJub by RNA interference identify djub as an essential gene for development and a novel regulator of epithelial organ size as a component of the conserved Hippo (Hpo) pathway, which has been implicated in both tissue size control and cancer development. djub-deficient tissues were small and had decreased cell numbers as a result of increased apoptosis and decreased proliferation, due to downregulation of DIAP1 and cyclin E. This phenocopies tissues deficient for Yorkie (Yki), the downstream target of the Hippo pathway. djub genetically interacts with the Hippo pathway, and epistasis suggests that djub lies downstream of hpo. In mammalian and Drosophila cells, Ajuba LIM proteins/dJub interact with LATS/Warts (Wts) and WW45/Sav to inhibit phosphorylation of YAP/Yki. This work describes a novel role for the Ajuba LIM proteins as negative regulators of the Hippo signaling pathway.

    View details for DOI 10.1016/j.cub.2010.02.035

    View details for Web of Science ID 000276753100031

    View details for PubMedID 20303269

  • Polychaetoid controls patterning by modulating adhesion in the Drosophila pupal retina DEVELOPMENTAL BIOLOGY Seppa, M. J., Johnson, R. I., Bao, S., Cagan, R. L. 2008; 318 (1): 1-16


    Correct cellular patterning is central to tissue morphogenesis, but the role of epithelial junctions in this process is not well-understood. The Drosophila pupal eye provides a sensitive and accessible model for testing the role of junction-associated proteins in cells that undergo dynamic and coordinated movements during development. Mutations in polychaetoid (pyd), the Drosophila homologue of Zonula Occludens-1, are characterized by two phenotypes visible in the adult fly: increased sensory bristle number and the formation of a rough eye produced by poorly arranged ommatidia. We found that Pyd was localized to the adherens junction in cells of the developing pupal retina. Reducing Pyd function in the pupal eye resulted in mis-patterning of the interommatidial cells and a failure to consistently switch cone cell contacts from an anterior-posterior to an equatorial-polar orientation. Levels of Roughest, DE-Cadherin and several other adherens junction-associated proteins were increased at the membrane when Pyd protein was reduced. Further, both over-expression and mutations in several junction-associated proteins greatly enhanced the patterning defects caused by reduction of Pyd. Our results suggest that Pyd modulates adherens junction strength and Roughest-mediated preferential cell adhesion.

    View details for DOI 10.1016/j.ydbio.2008.02.022

    View details for Web of Science ID 000256254200001

    View details for PubMedID 18423436

  • The Drosophila CD2AP/CIN85 orthologue cindr regulates junctions and cytoskeleton dynamics during tissue patterning JOURNAL OF CELL BIOLOGY Johnson, R. I., Seppa, M. J., Cagan, R. L. 2008; 180 (6): 1191-1204


    Developing tissues require cells to undergo intricate processes to shift into appropriate niches. This requires a functional connection between adhesion-mediating events at the cell surface and a cytoskeletal reorganization to permit directed movement. A small number of proteins are proposed to link these processes. Here, we identify one candidate, Cindr, the sole Drosophila melanogaster member of the CD2AP/CIN85 family (this family has been previously implicated in a variety of processes). Using D. melanogaster retina, we demonstrate that Cindr links cell surface junctions (E-cadherin) and adhesion (Roughest) with multiple components of the actin cytoskeleton. Reducing cindr activity leads to defects in local cell movement and, consequently, tissue patterning and cell death. Cindr activity is required for normal localization of Drosophila E-cadherin and Roughest, and we show additional physical and functional links to multiple components of the actin cytoskeleton, including the actin-capping proteins capping protein alpha and capping protein beta. Together, these data demonstrate that Cindr is involved in dynamic cell rearrangement in an emerging epithelium.

    View details for Web of Science ID 000254295400013

    View details for PubMedID 18362180

  • Chick ciliary neurotrophic factor is secreted via a nonclassical pathway MOLECULAR AND CELLULAR NEUROSCIENCE Reiness, C. G., Seppa, M. J., Dion, D. M., Sweeney, S., Foster, D. N., Nishi, R. 2001; 17 (6): 931-944


    In contrast to mammalian ciliary neurotrophic factors (CNTFs), chick CNTF is secreted, although it lacks an N-terminal signal. We determined that a 52 aa region of chick CNTF containing an internal hydrophobic domain could direct secretion of rat CNTF. Using a stable cell line that overexpressed chick CNTF, we found that chick CNTF immunoreactivity was punctate throughout the cytosol. Cellular fractionation confirmed chick CNTF to be protected by vesicles. Chick CNTF did not colocalize with fibronectin, calreticulin, wheat germ agglutinin binding sites, or with transferrin receptor. The distribution of chick CNTF was altered neither by brefeldin A nor by chloroquine treatment. Although the punctate pattern of chick CNTF immunoreactivity was not due to reuptake, chick CNTF could be found in a cellular compartment labeled after a brief incubation with dextran microbeads. When synthesized in vitro, chick CNTF did not translocate into microsomes. We conclude that chick CNTF is secreted via a nonclassical pathway.

    View details for DOI 10.1006/mcne.2001.0985

    View details for Web of Science ID 000169626800001

    View details for PubMedID 11414784