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Pro-inflammatory LPS drives production and release of the chemokine MCP-1 in human coronary artery smooth muscle cells

Bankell, Elisabeth LU ; Gidlöf, Olof LU and Nilsson, Bengt-Olof LU orcid (2026) In Molecular and Cellular Biochemistry 481(5). p.2241-2249
Abstract
The chemokine monocyte chemoattractant protein-1 (MCP-1) plays an important role as chemoattractant for monocytes in atherosclerosis. It is established that MCP-1 is produced by vascular smooth muscle cells, but the underlying mechanisms for its release are not identified. Here, we investigate production and secretion of MCP-1 in primary human coronary artery smooth muscle cells. We demonstrate that the cells express MCP-1 using RT-qPCR, immunocytochemistry and ELISA, and the ELISA analysis shows that they contain high basal levels of MCP-1 compared to human THP-1 monocytes included as positive control representing an immune cell. Immunocytochemistry discloses co-staining for MCP-1 and the ER marker calreticulin, suggesting that they may... (More)
The chemokine monocyte chemoattractant protein-1 (MCP-1) plays an important role as chemoattractant for monocytes in atherosclerosis. It is established that MCP-1 is produced by vascular smooth muscle cells, but the underlying mechanisms for its release are not identified. Here, we investigate production and secretion of MCP-1 in primary human coronary artery smooth muscle cells. We demonstrate that the cells express MCP-1 using RT-qPCR, immunocytochemistry and ELISA, and the ELISA analysis shows that they contain high basal levels of MCP-1 compared to human THP-1 monocytes included as positive control representing an immune cell. Immunocytochemistry discloses co-staining for MCP-1 and the ER marker calreticulin, suggesting that they may co-exist. The cellular production of MCP-1 is stimulated by the bacterial endotoxin LPS demonstrated both on mRNA and protein levels. Conditioned medium contains higher amounts of MCP-1 than fresh medium, and pro-inflammatory LPS and TNF-α stimulate release of MCP-1 from the cells. LPS does not enhance the secretion of MCP-1 at an early time point (60 min) neither in the presence nor in the absence of protein synthesis inhibition with cycloheximide, and it has no effect on intracellular [Ca2+] within 0–60 min, suggesting that LPS has no direct effect on the secretory process of MCP-1. We conclude that human coronary artery smooth muscle cells contain high levels of MCP-1, and that pro-inflammatory stimulus triggers secretion of this important chemokine indirectly via activation of MCP-1 production. (Less)
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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Atherosclerosis, Chemoattractant, Inflammation, Protein synthesis, Secretion, Vascular smooth muscle cells
in
Molecular and Cellular Biochemistry
volume
481
issue
5
pages
2241 - 2249
publisher
Springer
external identifiers
  • pmid:41964752
  • scopus:105035410856
ISSN
0300-8177
DOI
10.1007/s11010-026-05532-y
language
English
LU publication?
yes
id
2948c036-aebe-4f1e-ae65-fcd651c1197e
date added to LUP
2026-05-07 11:57:05
date last changed
2026-06-08 07:38:08
@article{2948c036-aebe-4f1e-ae65-fcd651c1197e,
  abstract     = {{The chemokine monocyte chemoattractant protein-1 (MCP-1) plays an important role as chemoattractant for monocytes in atherosclerosis. It is established that MCP-1 is produced by vascular smooth muscle cells, but the underlying mechanisms for its release are not identified. Here, we investigate production and secretion of MCP-1 in primary human coronary artery smooth muscle cells. We demonstrate that the cells express MCP-1 using RT-qPCR, immunocytochemistry and ELISA, and the ELISA analysis shows that they contain high basal levels of MCP-1 compared to human THP-1 monocytes included as positive control representing an immune cell. Immunocytochemistry discloses co-staining for MCP-1 and the ER marker calreticulin, suggesting that they may co-exist. The cellular production of MCP-1 is stimulated by the bacterial endotoxin LPS demonstrated both on mRNA and protein levels. Conditioned medium contains higher amounts of MCP-1 than fresh medium, and pro-inflammatory LPS and TNF-α stimulate release of MCP-1 from the cells. LPS does not enhance the secretion of MCP-1 at an early time point (60 min) neither in the presence nor in the absence of protein synthesis inhibition with cycloheximide, and it has no effect on intracellular [Ca2+] within 0–60 min, suggesting that LPS has no direct effect on the secretory process of MCP-1. We conclude that human coronary artery smooth muscle cells contain high levels of MCP-1, and that pro-inflammatory stimulus triggers secretion of this important chemokine indirectly via activation of MCP-1 production.}},
  author       = {{Bankell, Elisabeth and Gidlöf, Olof and Nilsson, Bengt-Olof}},
  issn         = {{0300-8177}},
  keywords     = {{Atherosclerosis; Chemoattractant; Inflammation; Protein synthesis; Secretion; Vascular smooth muscle cells}},
  language     = {{eng}},
  month        = {{04}},
  number       = {{5}},
  pages        = {{2241--2249}},
  publisher    = {{Springer}},
  series       = {{Molecular and Cellular Biochemistry}},
  title        = {{Pro-inflammatory LPS drives production and release of the chemokine MCP-1 in human coronary artery smooth muscle cells}},
  url          = {{http://dx.doi.org/10.1007/s11010-026-05532-y}},
  doi          = {{10.1007/s11010-026-05532-y}},
  volume       = {{481}},
  year         = {{2026}},
}