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.
journal_name
Cell Tissue Resjournal_title
Cell and tissue researchauthors
Devenport M,Fujioka H,Donnelly-Doman M,Shen Z,Jacobs-Lorena Mdoi
10.1007/s00441-004-1067-3keywords:
subject
Has Abstractpub_date
2005-04-01 00:00:00pages
175-85issue
1eissn
0302-766Xissn
1432-0878journal_volume
320pub_type
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