rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Annexin A2 Controls Lipid Composition Necessary for Junctional Stability in Response to Sphingosine 1-Phosphate
  name:
    name part: Sveeggen, Timothy
    role:
      role term: creator
    role:
      role term: author.
  name:
    name part: Bayless, Kayla
    role:
      role term: thesis advisor.
  name:
    name part: Texas A&M University
    role:
      role term: degree granting institution.
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: txu
    date issued: 2023
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: remote
    extent: 1 online resource.
  abstract: The intersection of protein and lipid biology is of growing importance for understanding how cells respond to changes in structural needs during adhesion and migration. While protein complexes engaged with the cytoskeleton play a vital role, support from the phospholipid membrane is crucial for directing localization and ensuring proper assembly. During angiogenesis, the development of new blood vessels from pre-existing structures, it is well known that dramatic cellular remodeling between proteins and membranes is necessary as endothelial cells shift from a stable monolayer to invasive structures. We better characterized the role of annexin A2, a membrane binding protein that is known to help coordinate the actin cytoskeleton with the plasma membrane. Annexin A2 maintains organization of adherens junctions, focal adhesions, and F-actin in response to sphingosine 1-phosphate, which directly regulates the balance between sprout initiation and sprout maturation during angiogenesis. Further, lipidomic analysis revealed that annexin A2 modulates composition of specific membrane lipids upstream of cytoskeletal coordination with adherens junctions, including accumulation of phosphatidylcholine (16:0_16:0). Incorporation of excess phosphatidylcholine (16:0_16:0) in wild-type cells mimics the annexin A2 knock-down phenotype, indicating that annexin A2 regulates the phospholipid membrane upstream organization of F-actin and adherens junctions. Altogether these data present a novel function for annexin A2, and suggests proper lipid modulation is a critical component of endothelial function. The electronic version of this dissertation is accessible from https://hdl.handle.net/1969.1/198138
  note: by Timothy Sveeggen.
  note: "Major Subject: Genetics"
  note: Includes vita.
  note: Doctor of Philosophy Texas A&M University 2022 https://hdl.handle.net/1969.1/198138
  note: Includes bibliographical references.
  note: Text (Dissertation)
  subject:
    topic: Major Genetics
  subject:
    topic: Actin-Related Protein 2
  subject:
    topic: Adherens Junctions
  subject:
    topic: Annexin A2
  subject:
    topic: Cholesterol
  subject:
    topic: Cytoskeleton
  subject:
    topic: Endothelial Cells
  subject:
    topic: Lipidomics
  subject:
    topic: Membrane Lipids
  subject:
    topic: Phosphatidylcholines
  subject:
    topic: Phospholipids
  identifier: https://hdl.handle.net/1969.1/198138
  record info:
    record content source: TXA
    record creation date: 240828
    record change date: 20240829173519.5
    record identifier: in00005468676
    language of cataloging:
      language term: eng