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.
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Acknowledgements
We thank Minh Lam of the Case Western Reserve University, Ireland Comprehensive Cancer Center, Confocal Microscopy Facility for expert technical assistance.
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This work was supported by grants from the National Institutes of Health. Confocal microscopy research was supported by CWRU Ireland Comprehensive Cancer Center departmental grant P30 CA43703-12.
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Devenport, M., Fujioka, H., Donnelly-Doman, M. et al. Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae. Cell Tissue Res 320, 175–185 (2005). https://doi.org/10.1007/s00441-004-1067-3
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DOI: https://doi.org/10.1007/s00441-004-1067-3