This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Meibomian lipids are the major component of the outermost layer of the tear film, the film that protects the surface of the eye. They are composed of a wide variety of lipid species, the majority of which are long chain wax esters, cholesterol esters and fatty acids. Because it forms the interface with air, the physical and chemical properties of the lipid layer are believed to be influential in tear film stability. We are interested in exploring the structure of Meibomian lipids from individuals with stable tear films and patients with dry eye disease (unstable tear films). Studies of Meibomian lipid monolayers have shown the mechanical properties of these lipids to be quite responsive to temperature. We would like to link these results to changes in the crystalline structure from 25?C through the melting transition, which will indicate the melt temperature of the lipids. In some forms of dry eye disease the composition of these lipids is different than asymptomatic individuals. If the melt temperature changes significantly compared to body temperature, the ability of the lipids to spread and the mechanical properties of the lipid layer may be modified in such a way that the tear film becomes unstable. The goal of this study is to understand the inherent crystalline structure of Meibum from ?normal? and dry eye subjects as a function of temperature using small angle x-ray scattering. We hope that such studies will contribute to an understanding of which properties promote stability in the tear film, how they change with disease, and how they can be restored for individuals suffering from dry eye.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR001209-31
Application #
8170363
Study Section
Special Emphasis Panel (ZRG1-BCMB-P (40))
Project Start
2010-05-01
Project End
2011-02-28
Budget Start
2010-05-01
Budget End
2011-02-28
Support Year
31
Fiscal Year
2010
Total Cost
$346
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305
Vickers, Chelsea; Liu, Feng; Abe, Kento et al. (2018) Endo-fucoidan hydrolases from glycoside hydrolase family 107 (GH107) display structural and mechanistic similarities to ?-l-fucosidases from GH29. J Biol Chem 293:18296-18308
Nguyen, Phong T; Lai, Jeffrey Y; Lee, Allen T et al. (2018) Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP Binding Cassette (ABC) transporter. Proc Natl Acad Sci U S A 115:E10596-E10604
Aleman, Fernando; Tzarum, Netanel; Kong, Leopold et al. (2018) Immunogenetic and structural analysis of a class of HCV broadly neutralizing antibodies and their precursors. Proc Natl Acad Sci U S A 115:7569-7574
Herrera, Nadia; Maksaev, Grigory; Haswell, Elizabeth S et al. (2018) Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance. Sci Rep 8:14566
Lal, Neeraj K; Nagalakshmi, Ugrappa; Hurlburt, Nicholas K et al. (2018) The Receptor-like Cytoplasmic Kinase BIK1 Localizes to the Nucleus and Regulates Defense Hormone Expression during Plant Innate Immunity. Cell Host Microbe 23:485-497.e5
Pluvinage, Benjamin; Grondin, Julie M; Amundsen, Carolyn et al. (2018) Molecular basis of an agarose metabolic pathway acquired by a human intestinal symbiont. Nat Commun 9:1043
Beyerlein, Kenneth R; Jönsson, H Olof; Alonso-Mori, Roberto et al. (2018) Ultrafast nonthermal heating of water initiated by an X-ray Free-Electron Laser. Proc Natl Acad Sci U S A 115:5652-5657
Yoshizawa, Takuya; Ali, Rustam; Jiou, Jenny et al. (2018) Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. Cell 173:693-705.e22
Dods, Robert; Båth, Petra; Arnlund, David et al. (2017) From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography. Structure 25:1461-1468.e2
de Vries, Robert P; Tzarum, Netanel; Peng, Wenjie et al. (2017) A single mutation in Taiwanese H6N1 influenza hemagglutinin switches binding to human-type receptors. EMBO Mol Med 9:1314-1325

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