Angiogenic activity of an enamel matrix derivative (EMD) and EMD-derived proteins: An experimental study in mice

Daniel S. Thoma, Cristina C. Villar, David L. Carnes, Michel Dard, Yong-hee P Chun, David L Cochran

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Objectives: To determine whether all or only certain proteins in an enamel matrix derivative (EMD) are angiogenic. Materials and Methods: The angiogenic effect was analysed using an in vivo angiogenesis assay. Silicon tubes were filled with or without potential and known angiogenic-modulating factors: (i) an EMD parent, (ii) nine pools of EMD proteins, (iii) fibroblast growth factor/vascular endothelial growth factor and (iv) amelogenin. Silicon tubes were implanted subcutaneously in mice. Dextran-fluorescein isothiocyanate (FITC) was injected via the tail vein, mice were euthanized and tubes were retrieved. Neovascularization was determined by measuring the amount of dextran-FITC within the tubes. Results: The greatest angiogenic potential of the EMD parent was at a weight of 125 ng, resulting in a 4.3-fold increase compared with the negative control. Five pools of EMD proteins showed a stronger angiogenic activity than the EMD parent. Pool 5 showed the greatest angiogenic activity, when compared with the negative control (8.1-fold increase) and with 125 ng of the EMD parent (4.2-fold increase). Amelogenin demonstrated a significantly higher angiogenic activity than the negative control (increase up to 4.0-fold) and the EMD parent (increase up to 1.6-fold). Conclusions: EMD parent, recombinant porcine amelogenin and certain pools of EMD proteins induced significant angiogenesis compared with the controls using a standardized in vivo assay.

Original languageEnglish (US)
Pages (from-to)253-260
Number of pages8
JournalJournal of Clinical Periodontology
Volume38
Issue number3
DOIs
StatePublished - Mar 2011

Fingerprint

Dental Enamel
Amelogenin
Proteins
Silicon
Fibroblast Growth Factors
Angiogenesis Inducing Agents
Vascular Endothelial Growth Factor A
Tail
Veins
Swine
Weights and Measures
enamel matrix proteins

Keywords

  • amelogenin
  • angiogenesis
  • enamel matrix proteins
  • fibroblast growth factor
  • periodontal regeneration
  • vascular endothelial growth factor

ASJC Scopus subject areas

  • Periodontics

Cite this

Angiogenic activity of an enamel matrix derivative (EMD) and EMD-derived proteins : An experimental study in mice. / Thoma, Daniel S.; Villar, Cristina C.; Carnes, David L.; Dard, Michel; Chun, Yong-hee P; Cochran, David L.

In: Journal of Clinical Periodontology, Vol. 38, No. 3, 03.2011, p. 253-260.

Research output: Contribution to journalArticle

@article{33ced0e693c34fc48a5e740f86217c21,
title = "Angiogenic activity of an enamel matrix derivative (EMD) and EMD-derived proteins: An experimental study in mice",
abstract = "Objectives: To determine whether all or only certain proteins in an enamel matrix derivative (EMD) are angiogenic. Materials and Methods: The angiogenic effect was analysed using an in vivo angiogenesis assay. Silicon tubes were filled with or without potential and known angiogenic-modulating factors: (i) an EMD parent, (ii) nine pools of EMD proteins, (iii) fibroblast growth factor/vascular endothelial growth factor and (iv) amelogenin. Silicon tubes were implanted subcutaneously in mice. Dextran-fluorescein isothiocyanate (FITC) was injected via the tail vein, mice were euthanized and tubes were retrieved. Neovascularization was determined by measuring the amount of dextran-FITC within the tubes. Results: The greatest angiogenic potential of the EMD parent was at a weight of 125 ng, resulting in a 4.3-fold increase compared with the negative control. Five pools of EMD proteins showed a stronger angiogenic activity than the EMD parent. Pool 5 showed the greatest angiogenic activity, when compared with the negative control (8.1-fold increase) and with 125 ng of the EMD parent (4.2-fold increase). Amelogenin demonstrated a significantly higher angiogenic activity than the negative control (increase up to 4.0-fold) and the EMD parent (increase up to 1.6-fold). Conclusions: EMD parent, recombinant porcine amelogenin and certain pools of EMD proteins induced significant angiogenesis compared with the controls using a standardized in vivo assay.",
keywords = "amelogenin, angiogenesis, enamel matrix proteins, fibroblast growth factor, periodontal regeneration, vascular endothelial growth factor",
author = "Thoma, {Daniel S.} and Villar, {Cristina C.} and Carnes, {David L.} and Michel Dard and Chun, {Yong-hee P} and Cochran, {David L}",
year = "2011",
month = "3",
doi = "10.1111/j.1600-051X.2010.01656.x",
language = "English (US)",
volume = "38",
pages = "253--260",
journal = "Journal of Clinical Periodontology",
issn = "0303-6979",
publisher = "Blackwell Munksgaard",
number = "3",

}

TY - JOUR

T1 - Angiogenic activity of an enamel matrix derivative (EMD) and EMD-derived proteins

T2 - An experimental study in mice

AU - Thoma, Daniel S.

AU - Villar, Cristina C.

AU - Carnes, David L.

AU - Dard, Michel

AU - Chun, Yong-hee P

AU - Cochran, David L

PY - 2011/3

Y1 - 2011/3

N2 - Objectives: To determine whether all or only certain proteins in an enamel matrix derivative (EMD) are angiogenic. Materials and Methods: The angiogenic effect was analysed using an in vivo angiogenesis assay. Silicon tubes were filled with or without potential and known angiogenic-modulating factors: (i) an EMD parent, (ii) nine pools of EMD proteins, (iii) fibroblast growth factor/vascular endothelial growth factor and (iv) amelogenin. Silicon tubes were implanted subcutaneously in mice. Dextran-fluorescein isothiocyanate (FITC) was injected via the tail vein, mice were euthanized and tubes were retrieved. Neovascularization was determined by measuring the amount of dextran-FITC within the tubes. Results: The greatest angiogenic potential of the EMD parent was at a weight of 125 ng, resulting in a 4.3-fold increase compared with the negative control. Five pools of EMD proteins showed a stronger angiogenic activity than the EMD parent. Pool 5 showed the greatest angiogenic activity, when compared with the negative control (8.1-fold increase) and with 125 ng of the EMD parent (4.2-fold increase). Amelogenin demonstrated a significantly higher angiogenic activity than the negative control (increase up to 4.0-fold) and the EMD parent (increase up to 1.6-fold). Conclusions: EMD parent, recombinant porcine amelogenin and certain pools of EMD proteins induced significant angiogenesis compared with the controls using a standardized in vivo assay.

AB - Objectives: To determine whether all or only certain proteins in an enamel matrix derivative (EMD) are angiogenic. Materials and Methods: The angiogenic effect was analysed using an in vivo angiogenesis assay. Silicon tubes were filled with or without potential and known angiogenic-modulating factors: (i) an EMD parent, (ii) nine pools of EMD proteins, (iii) fibroblast growth factor/vascular endothelial growth factor and (iv) amelogenin. Silicon tubes were implanted subcutaneously in mice. Dextran-fluorescein isothiocyanate (FITC) was injected via the tail vein, mice were euthanized and tubes were retrieved. Neovascularization was determined by measuring the amount of dextran-FITC within the tubes. Results: The greatest angiogenic potential of the EMD parent was at a weight of 125 ng, resulting in a 4.3-fold increase compared with the negative control. Five pools of EMD proteins showed a stronger angiogenic activity than the EMD parent. Pool 5 showed the greatest angiogenic activity, when compared with the negative control (8.1-fold increase) and with 125 ng of the EMD parent (4.2-fold increase). Amelogenin demonstrated a significantly higher angiogenic activity than the negative control (increase up to 4.0-fold) and the EMD parent (increase up to 1.6-fold). Conclusions: EMD parent, recombinant porcine amelogenin and certain pools of EMD proteins induced significant angiogenesis compared with the controls using a standardized in vivo assay.

KW - amelogenin

KW - angiogenesis

KW - enamel matrix proteins

KW - fibroblast growth factor

KW - periodontal regeneration

KW - vascular endothelial growth factor

UR - http://www.scopus.com/inward/record.url?scp=79551663351&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79551663351&partnerID=8YFLogxK

U2 - 10.1111/j.1600-051X.2010.01656.x

DO - 10.1111/j.1600-051X.2010.01656.x

M3 - Article

C2 - 21198764

AN - SCOPUS:79551663351

VL - 38

SP - 253

EP - 260

JO - Journal of Clinical Periodontology

JF - Journal of Clinical Periodontology

SN - 0303-6979

IS - 3

ER -