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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
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
epub
subject
keywords
Atherosclerosis, Chemoattractant, Inflammation, Protein synthesis, Secretion, Vascular smooth muscle cells
in
Molecular and Cellular Biochemistry
pages
9 pages
publisher
Springer
external identifiers
  • scopus:105035410856
  • pmid:41964752
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
2026-06-05 05:57:10
@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}},
  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}},
  year         = {{2026}},
}