title: Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae.
abstract: The gene Ag-Aper14 encodes a novel peritrophic matrix (or peritrophic membrane; PM) protein in the mosquito Anopheles gambiae. The Ag-Aper14 protein is merely 89 amino acids long and has a single putative chitin-binding domain. Prior to blood feeding, the Ag-Aper14 protein is stored in secretory vesicles next to the epithelial cell lumenal surface. Immunoelectron microscopy has revealed that Ag-Aper14 co-localizes to the same secretory vesicles as another PM protein, Ag-Aper1, indicating a common mode of regulated secretion. Conversely, Ag-Muc1, an epithelial cell-surface protein, does not co-localize to these secretory vesicles and is detected only on the cell surface. After blood feeding, Ag-Aper14 is secreted and incorporated into the PM that surrounds the ingested blood.
authors.affiliation: Department of Genetics, Case Western Reserve University, Cleveland, OH, USA.
authors.forename: M
authors.initials: M
authors.lastname: Devenport
authors.forename: H
authors.initials: H
authors.lastname: Fujioka
authors.forename: M
authors.initials: M
authors.lastname: Donnelly-Doman
authors.forename: Z
authors.initials: Z
authors.lastname: Shen
authors.forename: M
authors.initials: M
authors.lastname: Jacobs-Lorena
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000852:Anopheles / Q000378:metabolism*; D000906:Antibodies / Q000378:metabolism; D001483:Base Sequence; D004064:Digestive System / Q000378:metabolism / Q000648:ultrastructure; D004848:Epithelium / Q000378:metabolism; D005260:Female; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007814:Larva; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
chemical_list: D000906:Antibodies; D019476:Insect Proteins