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Immunodetection of annexins 1 and 2 in ciliated cells from quail oviduct *
Author(s) -
Chailley Bernadette,
Pradel LouiseAnne
Publication year - 1992
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/0248-4900(92)90123-i
Subject(s) - biology , spectrin , cytoskeleton , microbiology and biotechnology , annexin a2 , actin , annexin , cell , biochemistry
Summary— Annexins I and 2 are Ca 2+ ‐binding proteins related to the cytoskeletal proteins which have been reported to bind in a calcium‐dependent manner to F‐actin and phospholipids in vitro . Proteins immunologically related to the brain 37‐kDa annexin I and 36‐kDa annexin 2 were characterized by immunoblotting epithelial ciliated cells from quail oviduct. They were detected by immunofluorescence in ciliated as well as glandular cells, using antisera and purified antibodies directed against pig brain annexins. The pattern of labeling was found in the apical part of both cell types, with close membrane association. However, a wider distribution was observed in mature ciliated cells: annexins were localized in the well developed cytoskeletal meshwork in which the ciliary apparatus is tightly anchored. After immunogold labeling, annexins 1 and 2 were located in the same area as spectrin 240/235 and at the connection sites of F‐actin; both these cytoskeletals proteins were associated with the appendages of the basal body. In contrast, annexins were not detected in immature epithelial cells, while actin and spectrin were present. During ciliogenesis, the staining gradually appeared associated with the lateral and apical membranes. In this cellular model, the annexins may function during exocytosis in gland epithelial cells, where a close cytoskeleton‐membrane association is observed; moreover, in ciliated cells, a relationship between cytoskeletal elements of the terminal web and annexins may exist.