Publication

alpha II-spectrin and beta II-spectrin do not affect TGF beta 1-induced myofibroblast differentiation

Piersma, B., Wouters, O. Y. & Bank, R. A., Oct-2018, In : Cell and Tissue Research. 374, 1, p. 165-175 11 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Piersma, B., Wouters, O. Y., & Bank, R. A. (2018). alpha II-spectrin and beta II-spectrin do not affect TGF beta 1-induced myofibroblast differentiation. Cell and Tissue Research, 374(1), 165-175. https://doi.org/10.1007/s00441-018-2842-x

Author

Piersma, Bram ; Wouters, Olaf Y. ; Bank, Ruud A. / alpha II-spectrin and beta II-spectrin do not affect TGF beta 1-induced myofibroblast differentiation. In: Cell and Tissue Research. 2018 ; Vol. 374, No. 1. pp. 165-175.

Harvard

Piersma, B, Wouters, OY & Bank, RA 2018, 'alpha II-spectrin and beta II-spectrin do not affect TGF beta 1-induced myofibroblast differentiation', Cell and Tissue Research, vol. 374, no. 1, pp. 165-175. https://doi.org/10.1007/s00441-018-2842-x

Standard

alpha II-spectrin and beta II-spectrin do not affect TGF beta 1-induced myofibroblast differentiation. / Piersma, Bram; Wouters, Olaf Y.; Bank, Ruud A.

In: Cell and Tissue Research, Vol. 374, No. 1, 10.2018, p. 165-175.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Piersma B, Wouters OY, Bank RA. alpha II-spectrin and beta II-spectrin do not affect TGF beta 1-induced myofibroblast differentiation. Cell and Tissue Research. 2018 Oct;374(1):165-175. https://doi.org/10.1007/s00441-018-2842-x


BibTeX

@article{8864b1c615474b29ab257390bb08538c,
title = "alpha II-spectrin and beta II-spectrin do not affect TGF beta 1-induced myofibroblast differentiation",
abstract = "Mechanosensing of fibroblasts plays a key role in the development of fibrosis. So far, no effective treatments are available to treat this devastating disorder. Spectrins regulate cell morphology and are potential mechanosensors in a variety of non-erythroid cells, but little is known about the role of spectrins in fibroblasts. We investigate whether II- and II-spectrin are required for the phenotypic properties of adult human dermal (myo)fibroblasts. Knockdown of II- or II-spectrin in fibroblasts did not affect cell adhesion, cell size and YAP nuclear/cytosolic localization. We further investigated whether II- and II-spectrin play a role in the phenotypical switch from fibroblasts to myofibroblasts under the influence of the pro-fibrotic cytokine TGF1. Knockdown of spectrins did not affect myofibroblast formation, nor did we observe changes in the organization of SMA stress fibers. Focal adhesion assembly was unaffected by spectrin deficiency, as was collagen type I mRNA expression and protein deposition. Wound closure was unaffected as well, showing that important functional properties of myofibroblasts are unchanged without II- or II-spectrin. In fact, fibroblasts stimulated with TGF1 demonstrated significantly lower endogenous mRNA levels of II- and II-spectrin. Taken together, despite the diverse roles of spectrins in a variety of other cells, II- and II-spectrin do not regulate cell adhesion, cell size and YAP localization in human dermal fibroblasts and are not required for the dermal myofibroblast phenotypical switch.",
keywords = "Spectrin, Fibroblast, TGF beta 1, Physiological stiffness, Mechanosensing, HIPPO SIGNALING PATHWAY, EMBRYONIC LIVER FODRIN, FIBROBLAST ACTIVATION, SUBSTRATE STIFFNESS, PLASMA-MEMBRANE, CELL CONTACT, SH3 DOMAIN, GROWTH, YAP, FIBROSIS",
author = "Bram Piersma and Wouters, {Olaf Y.} and Bank, {Ruud A.}",
year = "2018",
month = "10",
doi = "10.1007/s00441-018-2842-x",
language = "English",
volume = "374",
pages = "165--175",
journal = "Cell and Tissue Research",
issn = "1432-0878",
publisher = "SPRINGER",
number = "1",

}

RIS

TY - JOUR

T1 - alpha II-spectrin and beta II-spectrin do not affect TGF beta 1-induced myofibroblast differentiation

AU - Piersma, Bram

AU - Wouters, Olaf Y.

AU - Bank, Ruud A.

PY - 2018/10

Y1 - 2018/10

N2 - Mechanosensing of fibroblasts plays a key role in the development of fibrosis. So far, no effective treatments are available to treat this devastating disorder. Spectrins regulate cell morphology and are potential mechanosensors in a variety of non-erythroid cells, but little is known about the role of spectrins in fibroblasts. We investigate whether II- and II-spectrin are required for the phenotypic properties of adult human dermal (myo)fibroblasts. Knockdown of II- or II-spectrin in fibroblasts did not affect cell adhesion, cell size and YAP nuclear/cytosolic localization. We further investigated whether II- and II-spectrin play a role in the phenotypical switch from fibroblasts to myofibroblasts under the influence of the pro-fibrotic cytokine TGF1. Knockdown of spectrins did not affect myofibroblast formation, nor did we observe changes in the organization of SMA stress fibers. Focal adhesion assembly was unaffected by spectrin deficiency, as was collagen type I mRNA expression and protein deposition. Wound closure was unaffected as well, showing that important functional properties of myofibroblasts are unchanged without II- or II-spectrin. In fact, fibroblasts stimulated with TGF1 demonstrated significantly lower endogenous mRNA levels of II- and II-spectrin. Taken together, despite the diverse roles of spectrins in a variety of other cells, II- and II-spectrin do not regulate cell adhesion, cell size and YAP localization in human dermal fibroblasts and are not required for the dermal myofibroblast phenotypical switch.

AB - Mechanosensing of fibroblasts plays a key role in the development of fibrosis. So far, no effective treatments are available to treat this devastating disorder. Spectrins regulate cell morphology and are potential mechanosensors in a variety of non-erythroid cells, but little is known about the role of spectrins in fibroblasts. We investigate whether II- and II-spectrin are required for the phenotypic properties of adult human dermal (myo)fibroblasts. Knockdown of II- or II-spectrin in fibroblasts did not affect cell adhesion, cell size and YAP nuclear/cytosolic localization. We further investigated whether II- and II-spectrin play a role in the phenotypical switch from fibroblasts to myofibroblasts under the influence of the pro-fibrotic cytokine TGF1. Knockdown of spectrins did not affect myofibroblast formation, nor did we observe changes in the organization of SMA stress fibers. Focal adhesion assembly was unaffected by spectrin deficiency, as was collagen type I mRNA expression and protein deposition. Wound closure was unaffected as well, showing that important functional properties of myofibroblasts are unchanged without II- or II-spectrin. In fact, fibroblasts stimulated with TGF1 demonstrated significantly lower endogenous mRNA levels of II- and II-spectrin. Taken together, despite the diverse roles of spectrins in a variety of other cells, II- and II-spectrin do not regulate cell adhesion, cell size and YAP localization in human dermal fibroblasts and are not required for the dermal myofibroblast phenotypical switch.

KW - Spectrin

KW - Fibroblast

KW - TGF beta 1

KW - Physiological stiffness

KW - Mechanosensing

KW - HIPPO SIGNALING PATHWAY

KW - EMBRYONIC LIVER FODRIN

KW - FIBROBLAST ACTIVATION

KW - SUBSTRATE STIFFNESS

KW - PLASMA-MEMBRANE

KW - CELL CONTACT

KW - SH3 DOMAIN

KW - GROWTH

KW - YAP

KW - FIBROSIS

U2 - 10.1007/s00441-018-2842-x

DO - 10.1007/s00441-018-2842-x

M3 - Article

VL - 374

SP - 165

EP - 175

JO - Cell and Tissue Research

JF - Cell and Tissue Research

SN - 1432-0878

IS - 1

ER -

ID: 65264026