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Vesicular Location and Transport of S100A8 and S100A9 Proteins in Monocytoid Cells.

Chakraborty, Paramita LU ; Bjork, Per; Källberg, Eva LU ; Olsson, Anders; Riva, Matteo; Mörgelin, Matthias LU ; Liberg, David; Ivars, Fredrik LU and Leanderson, Tomas LU (2015) In PLoS ONE 10(12).
Abstract
We show here, by using surface biotinylation, followed by Western blotting or surface plasmon resonance analysis, that very low levels of S100A8 and/or S100A9 can be detected on the surface of THP-1 cells or freshly isolated human monocytes. This was supported by immune-electron microscopy where we observed membrane-associated expression of the proteins restricted to small patches. By using confocal microscopy we could determine that S100A8 and S100A9 protein in THP-1 cells or freshly isolated human monocytes was mostly present in vesicular structures. This finding was confirmed using immune-electron microscopy. Subcellular fractionation and confocal microscopy showed that these vesicular structures are mainly early endosomes and... (More)
We show here, by using surface biotinylation, followed by Western blotting or surface plasmon resonance analysis, that very low levels of S100A8 and/or S100A9 can be detected on the surface of THP-1 cells or freshly isolated human monocytes. This was supported by immune-electron microscopy where we observed membrane-associated expression of the proteins restricted to small patches. By using confocal microscopy we could determine that S100A8 and S100A9 protein in THP-1 cells or freshly isolated human monocytes was mostly present in vesicular structures. This finding was confirmed using immune-electron microscopy. Subcellular fractionation and confocal microscopy showed that these vesicular structures are mainly early endosomes and endolysosomes. Our subsequent studies showed that accumulation of S100A8 and S100A9 in the endolysosomal compartment is associated with induction of their release from the cells. Furthermore, an inhibitor of lysosomal activity could modulate the release of S100A8 and S100A9 in the extracellular milieu. Our current results suggest that the S100A8 and S100A9 proteins are primarily associated with certain kinds of cytosolic vesicles and may be secreted via an endolysosomal pathway. (Less)
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organization
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publication status
published
subject
in
PLoS ONE
volume
10
issue
12
publisher
Public Library of Science
external identifiers
  • pmid:26661255
  • wos:000366715900193
  • scopus:84961351275
ISSN
1932-6203
DOI
10.1371/journal.pone.0145217
language
English
LU publication?
yes
id
407e59fa-2ece-4337-9c8f-996e91a129c9 (old id 8505015)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/26661255?dopt=Abstract
date added to LUP
2016-01-05 18:29:17
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2017-03-10 12:11:49
@article{407e59fa-2ece-4337-9c8f-996e91a129c9,
  abstract     = {We show here, by using surface biotinylation, followed by Western blotting or surface plasmon resonance analysis, that very low levels of S100A8 and/or S100A9 can be detected on the surface of THP-1 cells or freshly isolated human monocytes. This was supported by immune-electron microscopy where we observed membrane-associated expression of the proteins restricted to small patches. By using confocal microscopy we could determine that S100A8 and S100A9 protein in THP-1 cells or freshly isolated human monocytes was mostly present in vesicular structures. This finding was confirmed using immune-electron microscopy. Subcellular fractionation and confocal microscopy showed that these vesicular structures are mainly early endosomes and endolysosomes. Our subsequent studies showed that accumulation of S100A8 and S100A9 in the endolysosomal compartment is associated with induction of their release from the cells. Furthermore, an inhibitor of lysosomal activity could modulate the release of S100A8 and S100A9 in the extracellular milieu. Our current results suggest that the S100A8 and S100A9 proteins are primarily associated with certain kinds of cytosolic vesicles and may be secreted via an endolysosomal pathway.},
  articleno    = {e0145217},
  author       = {Chakraborty, Paramita and Bjork, Per and Källberg, Eva and Olsson, Anders and Riva, Matteo and Mörgelin, Matthias and Liberg, David and Ivars, Fredrik and Leanderson, Tomas},
  issn         = {1932-6203},
  language     = {eng},
  number       = {12},
  publisher    = {Public Library of Science},
  series       = {PLoS ONE},
  title        = {Vesicular Location and Transport of S100A8 and S100A9 Proteins in Monocytoid Cells.},
  url          = {http://dx.doi.org/10.1371/journal.pone.0145217},
  volume       = {10},
  year         = {2015},
}