Abstract

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.

Keywords

CytosolSecretionIntracellularExtracellularAnnexin A2Cell biologyAnnexinCell fractionationSubcellular localizationGelatinaseSignal peptideGranule (geology)Secretory proteinBiologyAnnexin A1BiochemistryCytoplasmCellPeptide sequenceEnzymeGene

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Publication Info

Year
2001
Type
article
Volume
25
Issue
10
Pages
963-969
Citations
7
Access
Closed

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Charlotta Movitz, Cláes Dahlgren (2001). QUANTIFICATION OF ANNEXIN I IN SUBCELLULAR FRACTIONS OF HUMAN NEUTROPHILS REVEALS AN EXCLUSIVE CYTOSOLIC LOCALISATION. Cell Biology International , 25 (10) , 963-969. https://doi.org/10.1006/cbir.2001.0760

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DOI
10.1006/cbir.2001.0760