Internists, Nephrologist (kidney), Radiologist
14 years of experience
Video profile
Accepting new patients
3300 Providence Dr
Suite 02
University Area, Anchorage, AK 99508
Locations and availability (2)

Education ?

Medical School Score
West Virginia School of Osteopathic Medicine (1996)
  • Currently 1 of 4 apples

Awards & Distinctions ?

Certified in Diagnostic & Interventional Nephrology
Chief Nephrology Fellow
American College of Physicians
Fellow of American Society of Nephrology
Certified in Diagnostic & Interventional Nephrology
American College of Physicians
Chief Nephrology Fellow
Fellow of American Society of Nephrology
Medical University Of South Carolina College Of Medicine - Charleston Sc

Affiliations ?

Dr. Lefler is affiliated with 8 hospitals.

Hospital Affilations



  • Providence Alaska Medical Center
    PO Box 196604, Anchorage, AK 99519
    • Currently 1 of 4 crosses
  • Providence Extended Care Center
    4900 Eagle St, Anchorage, AK 99503
  • Memorial Hospital
  • Providence Valdez Medical Center
    Valdez, AK 99686
  • Pioneer Health Services of Patrick County,Inc
  • R. J. Reynolds Patrick Community Memorial Hospital
  • Straub Clinic
  • Kapi`olani Medical Center
  • Publications & Research

    Dr. Lefler has contributed to 2 publications.
    Title Ca2+-calmodulin and Janus Kinase 2 Are Required for Activation of Sodium-proton Exchange by the Gi-coupled 5-hydroxytryptamine 1a Receptor.
    Date February 2007
    Journal The Journal of Pharmacology and Experimental Therapeutics

    The type 1 sodium-proton exchanger (NHE-1) is expressed ubiquitously and regulates key cellular functions, including mitogenesis, cell volume, and intracellular pH. Despite its importance, the signaling pathways that regulate NHE-1 remain incompletely defined. In this work, we present evidence that stimulation of the 5-hydroxytryptamine 1A (5-HT1A) receptor results in the formation of a signaling complex that includes activated Janus kinase 2 (Jak2), Ca2+/calmodulin (CaM), and NHE-1, and which involves tyrosine phosphorylation of CaM. The signaling pathway also involves rapid agonist-induced association of CaM and NHE-1 as assessed by coimmunoprecipitation studies and by bioluminescence resonance energy transfer studies in living cells. We propose that NHE-1 is activated through this pathway: 5-HT1A receptor --> G(i2)alpha and/or G(i3)alpha --> Jak2 activation --> tyrosine phosphorylation of CaM --> increased binding of CaM to NHE-1 --> induction of a conformational change in NHE-1 that unmasks an obscured proton-sensing and/or proton-transporting region of NHE-1 --> activation of NHE-1. The G(i/o)-coupled 5-HT1A receptor now joins a handful of Gq-coupled receptors and hypertonic shock as upstream activators of this emerging pathway. In the course of this work, we have presented clear evidence that CaM can be activated through tyrosine phosphorylation in the absence of a significant role for elevated intracellular Ca2+. We have also shown for the first time that the association of CaM with NHE-1 in living cells is a dynamic process.

    Title Identification of Proteins in Slow Continuous Ultrafiltrate by Reversed-phase Chromatography and Proteomics.
    Date April 2005
    Journal Journal of Proteome Research

    Continuous modes of renal replacement therapy (CRRT) are increasingly being utilized in the intensive care unit. The removal of cytokines and other inflammatory proteins during ultrafiltration may be responsible for some of the beneficial effects of CRRT. We used proteomic tools to identify proteins found in the ultrafiltrate from a patient with acute renal failure. Identification of these proteins could help elucidate the mechanism(s) of improved outcome with continuous renal replacement therapy. Protein was loaded on a reversed-phase C4 column and eluted with stepwise isocratic flows starting with 0%, 5%, 10%, 25%, and 50% of acetonitrile. Effluent was collected, pooled, desalted, and separated by two-dimensional gel electrophoresis (2DE). Reversed-phase separation improved the resolution and the number of spots seen on the gels. Protein spots were digested with trypsin and spotted onto MALDI plates. Proteins were identified by either peptide mass fingerprinting using a MALDI-TOF mass spectrometer or by peptide sequencing using a MALDI-TOF/TOF tandem mass spectrometer. From 196 spots cut, 47 were identified, representing multiple charge forms of 10 different proteins. Proteins identified were albumin, apolipoprotein A-IV, beta-2-microglobulin, lithostathine, mannose-binding lectin associated serine protease 2 associated protein, plasma retinol-binding protein, transferrin, transthyretin, vitamin D-binding protein and Zn alpha-2 glycoprotein. Continuous renal replacement therapy is frequently used in acutely ill patients with renal failure. Removal of proteins occurs during this process. The physiological significance of this protein removal is unclear. Identification of these proteins will lead to better understanding of the role of protein removal in continuous renal replacement therapy.

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