Storage and secretion of the peritrophic matrix protein Ag-Aper1 and trypsin in the midgut of Anopheles gambiae

The gene Ag-Aper1 encodes a peritrophic matrix (PM) protein from the mosquito Anopheles gambiae. Ag-Aper1 gene expression and protein localization in the mosquito midgut were studied during the course of a blood meal. Ag-Aper1 mRNA abundance does not change appreciably during the course of blood ing...

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Bibliographic Details
Published in:Insect molecular biology 2004-08, Vol.13 (4), p.349-358
Main Authors: Devenport, M, Fujioka, H, Jacobs-Lorena, M
Format: Article
Language:English
Subjects:
Animals
Anopheles - metabolism
Anopheles gambiae
Antibodies - metabolism
Blood - metabolism
Blotting, Northern
Blotting, Western
Carrier Proteins - genetics
Carrier Proteins - metabolism
Carrier Proteins - secretion
Culicidae
Digestion - physiology
Digestive System - metabolism
Digestive System - secretion
epithelial cells
Epithelium - metabolism
Epithelium - secretion
Fluorescent Antibody Technique
Freshwater
gene expression
Gene Expression Profiling
Gene Expression Regulation
hematophagy
Insect Proteins - genetics
Insect Proteins - metabolism
Insect Proteins - secretion
intracellular protein storage
messenger RNA
Microscopy, Immunoelectron
midgut
mosquito
peritrophic matrix
peritrophic membrane
protein secretion
protein synthesis
proteins
RNA, Messenger - genetics
RNA, Messenger - metabolism
secretory vesicles
Time Factors
trypsin
Trypsin - secretion
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Summary:The gene Ag-Aper1 encodes a peritrophic matrix (PM) protein from the mosquito Anopheles gambiae. Ag-Aper1 gene expression and protein localization in the mosquito midgut were studied during the course of a blood meal. Ag-Aper1 mRNA abundance does not change appreciably during the course of blood ingestion and digestion. Prior to a blood meal, the protein is stored in secretory vesicles of midgut epithelial cells. Moreover, Ag-Aper1 colocalizes to the same secretory vesicles as trypsin, indicating that these proteins use a common secretory pathway. Blood feeding triggers the secretion of vesicle contents into the midgut lumen, after which Ag-Aper1 is incorporated into the PM. Newly synthesized Ag-Aper1 protein was again detected within the midgut epithelial cells at 60 h after blood ingestion.
ISSN:0962-1075
1365-2583
DOI:10.1111/j.0962-1075.2004.00488.x