Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells

Research output: Contribution to journalJournal articlepeer-review

Standard

Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells. / He, Jianfei; Steffen, Jonas Hyld; Thulstrup, Peter Waaben; Pedersen, Jannik Nedergaard; Sauerland, Max B.; Otzen, Daniel E.; Hawkins, Clare L.; Gourdon, Pontus; Davies, Michael J.; Hägglund, Per.

In: Scientific Reports, Vol. 12, No. 1, 22051, 2022.

Research output: Contribution to journalJournal articlepeer-review

Harvard

He, J, Steffen, JH, Thulstrup, PW, Pedersen, JN, Sauerland, MB, Otzen, DE, Hawkins, CL, Gourdon, P, Davies, MJ & Hägglund, P 2022, 'Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells', Scientific Reports, vol. 12, no. 1, 22051. https://doi.org/10.1038/s41598-022-26359-9

APA

He, J., Steffen, J. H., Thulstrup, P. W., Pedersen, J. N., Sauerland, M. B., Otzen, D. E., Hawkins, C. L., Gourdon, P., Davies, M. J., & Hägglund, P. (2022). Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells. Scientific Reports, 12(1), [22051]. https://doi.org/10.1038/s41598-022-26359-9

Vancouver

He J, Steffen JH, Thulstrup PW, Pedersen JN, Sauerland MB, Otzen DE et al. Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells. Scientific Reports. 2022;12(1). 22051. https://doi.org/10.1038/s41598-022-26359-9

Author

He, Jianfei ; Steffen, Jonas Hyld ; Thulstrup, Peter Waaben ; Pedersen, Jannik Nedergaard ; Sauerland, Max B. ; Otzen, Daniel E. ; Hawkins, Clare L. ; Gourdon, Pontus ; Davies, Michael J. ; Hägglund, Per. / Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells. In: Scientific Reports. 2022 ; Vol. 12, No. 1.

Bibtex

@article{4ff1c15f1d7c48a28050cf3d312d2eae,
title = "Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells",
abstract = "Anastellin, a recombinant protein fragment from the first type III module of fibronectin, mimics a partially unfolded intermediate implicated in the assembly of fibronectin fibrils. Anastellin influences the structure of fibronectin and initiates in vitro fibrillation, yielding “superfibronectin”, a polymer with enhanced cell-adhesive properties. This ability is absent in an anastellin double mutant, L37AY40A. Here we demonstrate that both wild-type and L37AY40A anastellin affect fibronectin processing within the extracellular matrix (ECM) of smooth muscle cells. Fibronectin fibrils are diminished in the ECM from cells treated with anastellin, but are partially rescued by supplementation with plasma fibronectin in cell media. Proteomic analyses reveal that anastellin also impacts on the processing of other ECM proteins, with increased collagen and decreased laminin detected in media from cells exposed to wild-type anastellin. Moreover, both anastellin forms stimulate release of inflammatory cytokines, including interleukin 6. At the molecular level, L37AY40A does not exhibit major perturbations of structural features relative to wild-type anastellin, though the mutant showed differences in heparin binding characteristics. These findings indicate that wild-type and L37AY40A anastellin share similar molecular features but elicit slightly different, but partially overlapping, responses in smooth muscle cells resulting in altered secretion of cytokines and proteins involved in ECM processing.",
author = "Jianfei He and Steffen, {Jonas Hyld} and Thulstrup, {Peter Waaben} and Pedersen, {Jannik Nedergaard} and Sauerland, {Max B.} and Otzen, {Daniel E.} and Hawkins, {Clare L.} and Pontus Gourdon and Davies, {Michael J.} and Per H{\"a}gglund",
note = "Publisher Copyright: {\textcopyright} 2022, The Author(s).",
year = "2022",
doi = "10.1038/s41598-022-26359-9",
language = "English",
volume = "12",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Anastellin impacts on the processing of extracellular matrix fibronectin and stimulates release of cytokines from coronary artery smooth muscle cells

AU - He, Jianfei

AU - Steffen, Jonas Hyld

AU - Thulstrup, Peter Waaben

AU - Pedersen, Jannik Nedergaard

AU - Sauerland, Max B.

AU - Otzen, Daniel E.

AU - Hawkins, Clare L.

AU - Gourdon, Pontus

AU - Davies, Michael J.

AU - Hägglund, Per

N1 - Publisher Copyright: © 2022, The Author(s).

PY - 2022

Y1 - 2022

N2 - Anastellin, a recombinant protein fragment from the first type III module of fibronectin, mimics a partially unfolded intermediate implicated in the assembly of fibronectin fibrils. Anastellin influences the structure of fibronectin and initiates in vitro fibrillation, yielding “superfibronectin”, a polymer with enhanced cell-adhesive properties. This ability is absent in an anastellin double mutant, L37AY40A. Here we demonstrate that both wild-type and L37AY40A anastellin affect fibronectin processing within the extracellular matrix (ECM) of smooth muscle cells. Fibronectin fibrils are diminished in the ECM from cells treated with anastellin, but are partially rescued by supplementation with plasma fibronectin in cell media. Proteomic analyses reveal that anastellin also impacts on the processing of other ECM proteins, with increased collagen and decreased laminin detected in media from cells exposed to wild-type anastellin. Moreover, both anastellin forms stimulate release of inflammatory cytokines, including interleukin 6. At the molecular level, L37AY40A does not exhibit major perturbations of structural features relative to wild-type anastellin, though the mutant showed differences in heparin binding characteristics. These findings indicate that wild-type and L37AY40A anastellin share similar molecular features but elicit slightly different, but partially overlapping, responses in smooth muscle cells resulting in altered secretion of cytokines and proteins involved in ECM processing.

AB - Anastellin, a recombinant protein fragment from the first type III module of fibronectin, mimics a partially unfolded intermediate implicated in the assembly of fibronectin fibrils. Anastellin influences the structure of fibronectin and initiates in vitro fibrillation, yielding “superfibronectin”, a polymer with enhanced cell-adhesive properties. This ability is absent in an anastellin double mutant, L37AY40A. Here we demonstrate that both wild-type and L37AY40A anastellin affect fibronectin processing within the extracellular matrix (ECM) of smooth muscle cells. Fibronectin fibrils are diminished in the ECM from cells treated with anastellin, but are partially rescued by supplementation with plasma fibronectin in cell media. Proteomic analyses reveal that anastellin also impacts on the processing of other ECM proteins, with increased collagen and decreased laminin detected in media from cells exposed to wild-type anastellin. Moreover, both anastellin forms stimulate release of inflammatory cytokines, including interleukin 6. At the molecular level, L37AY40A does not exhibit major perturbations of structural features relative to wild-type anastellin, though the mutant showed differences in heparin binding characteristics. These findings indicate that wild-type and L37AY40A anastellin share similar molecular features but elicit slightly different, but partially overlapping, responses in smooth muscle cells resulting in altered secretion of cytokines and proteins involved in ECM processing.

UR - http://www.scopus.com/inward/record.url?scp=85144507966&partnerID=8YFLogxK

U2 - 10.1038/s41598-022-26359-9

DO - 10.1038/s41598-022-26359-9

M3 - Journal article

C2 - 36543832

AN - SCOPUS:85144507966

VL - 12

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 22051

ER -

ID: 333345542