Sando, Julianne J.
Primary Appointment
Associate Professor and Chair, Anesthesiology
Education
- BS, Biology and Chemistry, Indiana Univ. of Pennsylvania, Indiana, PA
- PhD, Pharmacology, Univ. of Michigan, Ann Arbol, MI
- Postdoc, Carcinogen and Immunology, Natl. Inst. of Health, Bethesda, MD
Contact Information
PO Box 800710
Old Med School, Room 3739A
Telephone: 924-5020/2494
Email: jjs@virginia.edu
Research Interests
Structure and Activation of Protein Kinase C (PKC) Isozymes and Roles of PKCs in Signal Transduction
Research Description
Signal Transduction through Protein Kinase C
The major interest of my laboratory is in activation of Protein Kinase C (PKC) isozymes and in roles of these enzymes in cellular signaling networks. PKC family members are activated by association with cell membranes and help to transduce a variety of extracellular signals. Most cells have several PKC isozymes. Alterations in isozyme expression or activation have been found in a number of diseases including some cancers and some endocrine, immunological, neurological, and cardiovascular diseases. Our goal is to understand the structure and activation of the enzymes and the role of individual isozymes in specific cellular processes. This understanding should facilitate design of more specific PKC activators and inhibitors for clinical use.
Properties of membrane lipids that activate PKC are studied using biochemical and biophysical techniques. Structural analysis of PKC is conducted in collaboration with Dr. Kretsinger (Biology) via generation of 2-dimensional crystals on defined lipid monolayers and with Drs. Grisham and Cafiso (Chemistry) using NMR and EPR. In a past collaboration with Drs. Steers and Tuttle (Urology), we started to examine the hypothesis that PKC may transduce physical stimuli such as cell stretch or pressure changes that occur in the urinary tract or the vasculature.
Among the proteins regulated by PKC are many ion channels and receptors that also are affected by anesthetics. We hypothesize that some anesthetic effects may be mediated via alterations in PKC activation, either via direct anesthetic-PKC binding or indirectly via anesthetic effects on membrane lipid domains that activate PKC. In collaboration with Drs. Lynch, Kamatchi, Patel, Zuo and Bayliss (Anesthesiology), we are analyzing the regulation by PKC of calcium, sodium, and potassium channels and of gluatamate transporters involved in anesthetic actions. In collaboration with Dr. Hussaini (Pathology), we have studied the role of PKC isozymes in development of invasive glioblastomas. A newer project involving collaborations with Drs. Gaylinn (Endocrinology), Patel (Anesthesiology), Cafiso (Chemistry) and Somlyo (Physiology) addresses regulation by PKC of the orexigenic peptide hormone ghrelin, which has effects on several ion channels and on lymphocyte, cardiovascular, adipocyte, and osteoblast function.