Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae

M. Devenport; H. Fujioka; M. Donnelly-Doman; Z. Shen; M. Jacobs-Lorena

doi:10.1007/s00441-004-1067-3

Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae

M. Devenport, H. Fujioka, M. Donnelly-Doman, Z. Shen, M. Jacobs-Lorena

Bloomberg School of Public Health

Research output: Contribution to journal › Article › peer-review

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.

Original language	English (US)
Pages (from-to)	175-185
Number of pages	11
Journal	Cell and Tissue Research
Volume	320
Issue number	1
DOIs	https://doi.org/10.1007/s00441-004-1067-3
State	Published - Apr 2005

Keywords

Midgut
Mosquito Anopheles gambiae (Insecta)
Mucin
Peritrophic matrix

ASJC Scopus subject areas

Pathology and Forensic Medicine
Histology
Cell Biology

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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.",

keywords = "Midgut, Mosquito Anopheles gambiae (Insecta), Mucin, Peritrophic matrix",

author = "M. Devenport and H. Fujioka and M. Donnelly-Doman and Z. Shen and M. Jacobs-Lorena",

note = "Funding Information: 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. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.",

year = "2005",

month = apr,

doi = "10.1007/s00441-004-1067-3",

language = "English (US)",

volume = "320",

pages = "175--185",

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AU - Fujioka, H.

AU - Donnelly-Doman, M.

AU - Shen, Z.

AU - Jacobs-Lorena, M.

N1 - Funding Information: 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. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.

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N2 - 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.

AB - 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.

KW - Midgut

KW - Mosquito Anopheles gambiae (Insecta)

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KW - Peritrophic matrix

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Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae

Abstract

Keywords

ASJC Scopus subject areas

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