| Researcher | Lipidomics Research |
|---|---|
| Vytas Bankaitis E.L. Wehner-Welch Foundation Chair in Chemistry Professor of Molecular and Cellular Medicine and of Biochemistry and Biophysics 108 Reynolds Medical Bldg. Vytas@tamhsc.edu 979-862-3188 B.S., Edinboro University, 1978 M.S., Clemson University, 1980 Ph.D., UNC-Chapel Hill, 1984 Postdoc, California Institute of Technology, 1984-86 Professor, Univ. of N. Carolina |
Phosphatidylinositol is a metabolic precursor of phosphoinositides and soluble inositol phosphates. Both sets of molecules function as critical intracellular chemical signals in eukaryotes. While much effort has been invested in understanding the enzymes that produce and consume these molecules, central aspects for how phsophoinositide production is controlled remain unresolved, and largely unappreciated. The Bankaitis laboratory is interested in how lipid-mediated signal transduction circuits are wired to specific biological outcomes using phosphoinositide signaling as primary focus. The work primarily centers on the phosphatidylinositol transfer proteins (PITPs), a ubiquitous yet enigmatic class of proteins, that are key regulators of functionally channeled phosphoinositide signaling circuits. Their biological importance is reported by the physiological consequences that accompany deficits in individual PITPs. These include neurodegeneration, chylomicron retention disease, liver steatosis, and hypoglycemia in neonatal mice, failures in embryogenesis and retinal degeneration in zebrafish and flies, and striking developmental defects in fungi. Ongoing projects in the laboratory focus on how PITPs work as molecules, how PITPs are integrated into cellular physiology, and development of small molecule tools for intervening with PITP and phosphoinositide signaling in cells. Relevant approaches that the laboratory employs include: molecular biology, protein and lipid biochemistry, confocal and electron microscopy, mouse gene knockout technology, and classical and molecular genetics. |
| Robert S. Chapkin, Ph.D.Professor KL / Room 442 r-chapkin@tamu.edu 979-845-0419 B.Sc. University of Guelph, Canada (1981) M.Sc. University of Guelph, Canada (1983) Ph.D. University of California, Davis (1986)Postdoc. University of California, Davis School of Medicine (1986-88) |
Chemoprevention: Why membrane phospholipids matterDr. Robert S. Chapkin is an expert in bioactive lipids and cancer and has been continuously funded by NIH/NCI for the past 25 years. He has made highly significant contributions to cancer chemoprevention by examining the effects of amphiphilic dietary bioactive lipids on cell membrane biology and function, with particular attention to cells of the immune system and intestinal stem cells. This novel work has had a far-reaching impact on the prevention of cancer.Since membrane localization of soluble proteins is mediated by interactions between lipid anchors of proteins and cell membranes, Dr. Chapkin hypothesized that their membrane localization and function are sensitive to amphiphilic fatty acid-induced changes in the cellular phospholipid environment. His on-going experiments indicate that the targeting of membrane structure and function using diet may reduce colon cancer risk. In a highly novel finding, Chapkin lab recently demonstrated that polyphosphoinositide 4,5-bisphosphate (PI(4,5)P2) mass and downstream actin remodeling are directly suppressed by the incorporation of n-3 polyunsaturated fatty acids (PUFA) into CD4+ T cell membranes. This is consistent with the fact that many actin remodeling proteins are regulated by PI(4,5)P2, an n-6 PUFA (arachidonic acid) enriched phospholipid on the inner surface of the plasma membrane which accumulates at the margins of lipid raft clusters. Collectively, this body of work suggests that targeted modifications to plasma membrane (lipid raft-cytoskeletal) composition represent a novel mechanism to control cell function and plasticity, raising the possibility that therapeutic alteration of membrane lipid order could affect inflammatory cell activation and ameliorate pathology. |
| Vishal Gohil, Ph.D.Assistant Professor ILSB, Room 2146A vgohil@tamu.edu 979-847-6138 B.Sc. Mohan Lal Sukhadia University, India (1995) M.Sc. Maharaja Sayajirao University of Baroda, India (1997) Ph.D. Wayne State University, Detroit (2005) Postdoc. Massachusetts General Hospital, Boston (2005-2008)Instructor in Medicine, Harvard Medical School, Boston (2008-2011) |
Despite the fundamental role of the mitochondrial respiratory chain (MRC) in cellular energy production, many of the factors required for its formation are currently unknown. The Gohil lab is using an integrative approach utilizing tools of genomics, lipidomics, biochemistry, and mass spectrometry to discover novel lipids and proteins required for the function and formation of the MRC. The lab has recently identified an evolutionary conserved MRC complex IV assembly factor, Coa6, in which a pathogenic mutation has been shown to cause fatal hypertrophic cardiomyopathy. Dr. Gohil’s lab has also demonstrated that meclizine, an over-the-counter anti-nausea drug, perturbs MRC function by targeting cellular phospholipid metabolism. Current work in the lab is focused on elucidating the precise biochemical function of Coa6 in complex IV assembly, and illuminating the role of phospholipids in maintaining the structural and functional integrity of the MRC. With this work, we hope to advance the frontiers of mitochondrial bioenergetics, and also uncover pathologies associated with mitochondrial dysfunction. |
| David H. Russell, Ph.D.Head, Department of Chemistry Professor Ph. D., University of Nebraska Contact Information: Phone: (979) 845-3345 |
My research focuses on proteomics, lipidomics, biophysical chemistry and application and development of mass spectrometry, such as “label-free” nano-particle based biosensors and novel peptide/protein isolation and purification strategies. We are also investigating the structure(s) of model peptides in an effort to better describe folding/unfolding and structure of membrane and intrinsically disordered (IDP) proteins. Peptides take on very different 2°, 3° and 4° structure, which determine or influence bio-activity. In the presence of lipid vesicles peptides can exist as solution-phase species, “absorbed” on lipid bilayers or “inserted” (as a monomer or multimer) in lipid bilayers. By what mechanism do peptides interact with lipid membranes to affect these structural changes, how do peptide-lipid interactions promote self-assembly to form intermediates that eventually yield aggregates, i.e., amyloid fibrils, or how does metal ion coordination affect the structure of metalloproteins? Mass spectrometry-based experiments, hydrogen/deuterium (H/D) exchange, chemical ‘foot-printing’ and gas-phase (ion-molecule and ion-ion reaction chemistry) and solution-phase chemical modifications, have expanded our abilities to address such questions, and new instrumental approaches, esp. ion mobility spectrometry (IMS) combined with enhanced molecular dynamics simulations (MDS), have become standard tools for structural-mass spectrometry studies. Over the past several years we have either acquired or developed novel, next-generation IM-MS instruments that are redefining cutting-edge structural-mass spectrometry research as well as cutting-edge computational tools essential to carry out these studies. Our new laboratories in the Interdisciplinary Life Sciences Building (ILSB) provides exciting opportunities for collaborative, interdisciplinary research with chemical-biologists, biochemists and other chemists. |
