The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling. / Lord, Megan S; Chuang, Christine Y; Melrose, James; Davies, Michael Jonathan; Iozzo, Renato V; Whitelock, John M.

In: Matrix Biology, Vol. 35, 04.2014, p. 112-22.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Lord, MS, Chuang, CY, Melrose, J, Davies, MJ, Iozzo, RV & Whitelock, JM 2014, 'The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling', Matrix Biology, vol. 35, pp. 112-22. https://doi.org/10.1016/j.matbio.2014.01.016

APA

Lord, M. S., Chuang, C. Y., Melrose, J., Davies, M. J., Iozzo, R. V., & Whitelock, J. M. (2014). The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling. Matrix Biology, 35, 112-22. https://doi.org/10.1016/j.matbio.2014.01.016

Vancouver

Lord MS, Chuang CY, Melrose J, Davies MJ, Iozzo RV, Whitelock JM. The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling. Matrix Biology. 2014 Apr;35:112-22. https://doi.org/10.1016/j.matbio.2014.01.016

Author

Lord, Megan S ; Chuang, Christine Y ; Melrose, James ; Davies, Michael Jonathan ; Iozzo, Renato V ; Whitelock, John M. / The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling. In: Matrix Biology. 2014 ; Vol. 35. pp. 112-22.

Bibtex

@article{e7985b9c6c7a4ffdae7d4035ae571c6d,
title = "The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling",
abstract = "Smooth muscle cell proliferation can be inhibited by heparan sulfate proteoglycans whereas the removal or digestion of heparan sulfate from perlecan promotes their proliferation. In this study we characterized the glycosaminoglycan side chains of perlecan isolated from either primary human coronary artery smooth muscle or endothelial cells and determined their roles in mediating cell adhesion and proliferation, and in fibroblast growth factor (FGF) binding and signaling. Smooth muscle cell perlecan was decorated with both heparan sulfate and chondroitin sulfate, whereas endothelial perlecan contained exclusively heparan sulfate chains. Smooth muscle cells bound to the protein core of perlecan only when the glycosaminoglycans were removed, and this binding involved a novel site in domain III as well as domain V/endorepellin and the α2β1 integrin. In contrast, endothelial cells adhered to the protein core of perlecan in the presence of glycosaminoglycans. Smooth muscle cell perlecan bound both FGF1 and FGF2 via its heparan sulfate chains and promoted the signaling of FGF2 but not FGF1. Also endothelial cell perlecan bound both FGF1 and FGF2 via its heparan sulfate chains, but in contrast, promoted the signaling of both growth factors. Based on this differential bioactivity, we propose that perlecan synthesized by smooth muscle cells differs from that synthesized by endothelial cells by possessing different signaling capabilities, primarily, but not exclusively, due to a differential glycanation. The end result is a differential modulation of cell adhesion, proliferation and growth factor signaling in these two key cellular constituents of blood vessels.",
author = "Lord, {Megan S} and Chuang, {Christine Y} and James Melrose and Davies, {Michael Jonathan} and Iozzo, {Renato V} and Whitelock, {John M}",
note = "Copyright {\circledC} 2014 International Society of Matrix Biology. Published by Elsevier B.V. All rights reserved.",
year = "2014",
month = "4",
doi = "10.1016/j.matbio.2014.01.016",
language = "English",
volume = "35",
pages = "112--22",
journal = "Matrix Biology",
issn = "0945-053X",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - The role of vascular-derived perlecan in modulating cell adhesion, proliferation and growth factor signaling

AU - Lord, Megan S

AU - Chuang, Christine Y

AU - Melrose, James

AU - Davies, Michael Jonathan

AU - Iozzo, Renato V

AU - Whitelock, John M

N1 - Copyright © 2014 International Society of Matrix Biology. Published by Elsevier B.V. All rights reserved.

PY - 2014/4

Y1 - 2014/4

N2 - Smooth muscle cell proliferation can be inhibited by heparan sulfate proteoglycans whereas the removal or digestion of heparan sulfate from perlecan promotes their proliferation. In this study we characterized the glycosaminoglycan side chains of perlecan isolated from either primary human coronary artery smooth muscle or endothelial cells and determined their roles in mediating cell adhesion and proliferation, and in fibroblast growth factor (FGF) binding and signaling. Smooth muscle cell perlecan was decorated with both heparan sulfate and chondroitin sulfate, whereas endothelial perlecan contained exclusively heparan sulfate chains. Smooth muscle cells bound to the protein core of perlecan only when the glycosaminoglycans were removed, and this binding involved a novel site in domain III as well as domain V/endorepellin and the α2β1 integrin. In contrast, endothelial cells adhered to the protein core of perlecan in the presence of glycosaminoglycans. Smooth muscle cell perlecan bound both FGF1 and FGF2 via its heparan sulfate chains and promoted the signaling of FGF2 but not FGF1. Also endothelial cell perlecan bound both FGF1 and FGF2 via its heparan sulfate chains, but in contrast, promoted the signaling of both growth factors. Based on this differential bioactivity, we propose that perlecan synthesized by smooth muscle cells differs from that synthesized by endothelial cells by possessing different signaling capabilities, primarily, but not exclusively, due to a differential glycanation. The end result is a differential modulation of cell adhesion, proliferation and growth factor signaling in these two key cellular constituents of blood vessels.

AB - Smooth muscle cell proliferation can be inhibited by heparan sulfate proteoglycans whereas the removal or digestion of heparan sulfate from perlecan promotes their proliferation. In this study we characterized the glycosaminoglycan side chains of perlecan isolated from either primary human coronary artery smooth muscle or endothelial cells and determined their roles in mediating cell adhesion and proliferation, and in fibroblast growth factor (FGF) binding and signaling. Smooth muscle cell perlecan was decorated with both heparan sulfate and chondroitin sulfate, whereas endothelial perlecan contained exclusively heparan sulfate chains. Smooth muscle cells bound to the protein core of perlecan only when the glycosaminoglycans were removed, and this binding involved a novel site in domain III as well as domain V/endorepellin and the α2β1 integrin. In contrast, endothelial cells adhered to the protein core of perlecan in the presence of glycosaminoglycans. Smooth muscle cell perlecan bound both FGF1 and FGF2 via its heparan sulfate chains and promoted the signaling of FGF2 but not FGF1. Also endothelial cell perlecan bound both FGF1 and FGF2 via its heparan sulfate chains, but in contrast, promoted the signaling of both growth factors. Based on this differential bioactivity, we propose that perlecan synthesized by smooth muscle cells differs from that synthesized by endothelial cells by possessing different signaling capabilities, primarily, but not exclusively, due to a differential glycanation. The end result is a differential modulation of cell adhesion, proliferation and growth factor signaling in these two key cellular constituents of blood vessels.

U2 - 10.1016/j.matbio.2014.01.016

DO - 10.1016/j.matbio.2014.01.016

M3 - Journal article

C2 - 24509440

VL - 35

SP - 112

EP - 122

JO - Matrix Biology

JF - Matrix Biology

SN - 0945-053X

ER -

ID: 128973757