QUANTIFICATION OF ANNEXIN I IN SUBCELLULAR FRACTIONS OF HUMAN NEUTROPHILS REVEALS AN EXCLUSIVE CYTOSOLIC LOCALISATION | Zendy

Movitz Charlotta | Zendy; Dahlgren Claes | Zendy

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QUANTIFICATION OF ANNEXIN I IN SUBCELLULAR FRACTIONS OF HUMAN NEUTROPHILS REVEALS AN EXCLUSIVE CYTOSOLIC LOCALISATION

Author(s) -

Movitz Charlotta,

Dahlgren Claes

Publication year - 2001

Publication title -

cell biology international

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.932

H-Index - 77

eISSN - 1095-8355

pISSN - 1065-6995

DOI - 10.1006/cbir.2001.0760

Subject(s) - cytosol , secretion , intracellular , extracellular , annexin a2 , microbiology and biotechnology , annexin , cell fractionation , subcellular localization , gelatinase , signal peptide , granule (geology) , secretory protein , biology , annexin a1 , biochemistry , cytoplasm , cell , peptide sequence , enzyme , gene , paleontology

Annexin I is an abundant cytosolic protein in human neutrophils. Besides its intracellular location, annexin I is found as an extracellular protein and the pathway for secretion has been of interest since the protein lacks a signal sequence for secretion. It was recently shown that annexin I is stored in the secretory gelatinase granules of human neutrophils, suggesting that the protein might be released through a granule mobilisation and fusion process resembling classical secretion. In this study we have determined the intracellular localisation of annexin I in human neutrophils using subcellular fractionation, protein separation by SDS‐PAGE and immunoblotting, and show that virtually all annexin I is localised in the cell cytosol.

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