Advanced glycation of type i collagen and fibronectin modifies periodontal cell behavior

Jesse Murillo, Yao Wang, Xiaoping Xu, Robert J. Klebe, Zhihua Chen, Gustavo Zardeneta, Sanjay Pal, Margarita Mikhailova, Bjorn Steffensen

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Background: Advanced glycation end products (AGEs) have been linked to pathogenic mechanisms of diabetes mellitus. However, little is known about the contribution of protein glycation to periodontal disease in patients with diabetes. Therefore, this study investigated whether glycation of type I collagen (COLI) and fibronectin (FN) modified the behavior of human gingival fibroblasts (hGFs) and periodontal ligament fibroblasts (hPDLs). Methods: Procedures for rapid in vitro glycation of COLI and FN used methylglyoxal (MG). Formation of AGEs was analyzed by changes in protein migration using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting with antibodies specific for MG-glycated proteins. Experiments then characterized the effects of glycated FN and COLI on the behavior of hGFs and hPDLs. Results: MG glycated COLI and FN in <6 hours. Confirming the specificity of the reactions, antibodies specific for MG-induced AGEs reacted with glycated FN and COLI but not with control proteins. In cell culture experiments, glycated FN was significantly less efficient in supporting the attachment of hGFs and hPDLs (P <0.05). Moreover, the morphologic parameters, including length, area, perimeter, and shape factor, were altered (P <0.001) for cells on both glycated proteins. Finally, cell migration was reduced on glycated FN and COLI (P <0.001). Conclusions: MG treatment efficiently glycated COLI and FN, providing a new tool to study the effects of diabetes on periodontal disease. The substantial effects of glycated COLI and FN on hGF and hPDL behavior indicated that protein glycation contributed to the pathogenesis and altered periodontal wound healing observed in patients with diabetes.

Original languageEnglish (US)
Pages (from-to)2190-2199
Number of pages10
JournalJournal of Periodontology
Volume79
Issue number11
DOIs
StatePublished - Nov 2008

Fingerprint

Fibronectins
Pyruvaldehyde
Collagen
Fibroblasts
Periodontal Ligament
Proteins
Periodontal Diseases
Advanced Glycosylation End Products
Antibody Specificity
Collagen Type I
glycosylated fibronectin
Sodium Dodecyl Sulfate
Wound Healing
Cell Movement
Polyacrylamide Gel Electrophoresis
Diabetes Mellitus
Cell Culture Techniques
Western Blotting
Antibodies

Keywords

  • Advanced glycation end products
  • Diabetes mellitus
  • Fibronectin
  • Methylglyoxal
  • Periodontal disease
  • Type I collagen

ASJC Scopus subject areas

  • Periodontics

Cite this

Murillo, J., Wang, Y., Xu, X., Klebe, R. J., Chen, Z., Zardeneta, G., ... Steffensen, B. (2008). Advanced glycation of type i collagen and fibronectin modifies periodontal cell behavior. Journal of Periodontology, 79(11), 2190-2199. https://doi.org/10.1902/jop.2008.080210

Advanced glycation of type i collagen and fibronectin modifies periodontal cell behavior. / Murillo, Jesse; Wang, Yao; Xu, Xiaoping; Klebe, Robert J.; Chen, Zhihua; Zardeneta, Gustavo; Pal, Sanjay; Mikhailova, Margarita; Steffensen, Bjorn.

In: Journal of Periodontology, Vol. 79, No. 11, 11.2008, p. 2190-2199.

Research output: Contribution to journalArticle

Murillo, J, Wang, Y, Xu, X, Klebe, RJ, Chen, Z, Zardeneta, G, Pal, S, Mikhailova, M & Steffensen, B 2008, 'Advanced glycation of type i collagen and fibronectin modifies periodontal cell behavior', Journal of Periodontology, vol. 79, no. 11, pp. 2190-2199. https://doi.org/10.1902/jop.2008.080210
Murillo, Jesse ; Wang, Yao ; Xu, Xiaoping ; Klebe, Robert J. ; Chen, Zhihua ; Zardeneta, Gustavo ; Pal, Sanjay ; Mikhailova, Margarita ; Steffensen, Bjorn. / Advanced glycation of type i collagen and fibronectin modifies periodontal cell behavior. In: Journal of Periodontology. 2008 ; Vol. 79, No. 11. pp. 2190-2199.
@article{65b1cfda77674009afb52f4d6a901509,
title = "Advanced glycation of type i collagen and fibronectin modifies periodontal cell behavior",
abstract = "Background: Advanced glycation end products (AGEs) have been linked to pathogenic mechanisms of diabetes mellitus. However, little is known about the contribution of protein glycation to periodontal disease in patients with diabetes. Therefore, this study investigated whether glycation of type I collagen (COLI) and fibronectin (FN) modified the behavior of human gingival fibroblasts (hGFs) and periodontal ligament fibroblasts (hPDLs). Methods: Procedures for rapid in vitro glycation of COLI and FN used methylglyoxal (MG). Formation of AGEs was analyzed by changes in protein migration using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting with antibodies specific for MG-glycated proteins. Experiments then characterized the effects of glycated FN and COLI on the behavior of hGFs and hPDLs. Results: MG glycated COLI and FN in <6 hours. Confirming the specificity of the reactions, antibodies specific for MG-induced AGEs reacted with glycated FN and COLI but not with control proteins. In cell culture experiments, glycated FN was significantly less efficient in supporting the attachment of hGFs and hPDLs (P <0.05). Moreover, the morphologic parameters, including length, area, perimeter, and shape factor, were altered (P <0.001) for cells on both glycated proteins. Finally, cell migration was reduced on glycated FN and COLI (P <0.001). Conclusions: MG treatment efficiently glycated COLI and FN, providing a new tool to study the effects of diabetes on periodontal disease. The substantial effects of glycated COLI and FN on hGF and hPDL behavior indicated that protein glycation contributed to the pathogenesis and altered periodontal wound healing observed in patients with diabetes.",
keywords = "Advanced glycation end products, Diabetes mellitus, Fibronectin, Methylglyoxal, Periodontal disease, Type I collagen",
author = "Jesse Murillo and Yao Wang and Xiaoping Xu and Klebe, {Robert J.} and Zhihua Chen and Gustavo Zardeneta and Sanjay Pal and Margarita Mikhailova and Bjorn Steffensen",
year = "2008",
month = "11",
doi = "10.1902/jop.2008.080210",
language = "English (US)",
volume = "79",
pages = "2190--2199",
journal = "Journal of Periodontology",
issn = "0022-3492",
publisher = "American Academy of Periodontology",
number = "11",

}

TY - JOUR

T1 - Advanced glycation of type i collagen and fibronectin modifies periodontal cell behavior

AU - Murillo, Jesse

AU - Wang, Yao

AU - Xu, Xiaoping

AU - Klebe, Robert J.

AU - Chen, Zhihua

AU - Zardeneta, Gustavo

AU - Pal, Sanjay

AU - Mikhailova, Margarita

AU - Steffensen, Bjorn

PY - 2008/11

Y1 - 2008/11

N2 - Background: Advanced glycation end products (AGEs) have been linked to pathogenic mechanisms of diabetes mellitus. However, little is known about the contribution of protein glycation to periodontal disease in patients with diabetes. Therefore, this study investigated whether glycation of type I collagen (COLI) and fibronectin (FN) modified the behavior of human gingival fibroblasts (hGFs) and periodontal ligament fibroblasts (hPDLs). Methods: Procedures for rapid in vitro glycation of COLI and FN used methylglyoxal (MG). Formation of AGEs was analyzed by changes in protein migration using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting with antibodies specific for MG-glycated proteins. Experiments then characterized the effects of glycated FN and COLI on the behavior of hGFs and hPDLs. Results: MG glycated COLI and FN in <6 hours. Confirming the specificity of the reactions, antibodies specific for MG-induced AGEs reacted with glycated FN and COLI but not with control proteins. In cell culture experiments, glycated FN was significantly less efficient in supporting the attachment of hGFs and hPDLs (P <0.05). Moreover, the morphologic parameters, including length, area, perimeter, and shape factor, were altered (P <0.001) for cells on both glycated proteins. Finally, cell migration was reduced on glycated FN and COLI (P <0.001). Conclusions: MG treatment efficiently glycated COLI and FN, providing a new tool to study the effects of diabetes on periodontal disease. The substantial effects of glycated COLI and FN on hGF and hPDL behavior indicated that protein glycation contributed to the pathogenesis and altered periodontal wound healing observed in patients with diabetes.

AB - Background: Advanced glycation end products (AGEs) have been linked to pathogenic mechanisms of diabetes mellitus. However, little is known about the contribution of protein glycation to periodontal disease in patients with diabetes. Therefore, this study investigated whether glycation of type I collagen (COLI) and fibronectin (FN) modified the behavior of human gingival fibroblasts (hGFs) and periodontal ligament fibroblasts (hPDLs). Methods: Procedures for rapid in vitro glycation of COLI and FN used methylglyoxal (MG). Formation of AGEs was analyzed by changes in protein migration using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting with antibodies specific for MG-glycated proteins. Experiments then characterized the effects of glycated FN and COLI on the behavior of hGFs and hPDLs. Results: MG glycated COLI and FN in <6 hours. Confirming the specificity of the reactions, antibodies specific for MG-induced AGEs reacted with glycated FN and COLI but not with control proteins. In cell culture experiments, glycated FN was significantly less efficient in supporting the attachment of hGFs and hPDLs (P <0.05). Moreover, the morphologic parameters, including length, area, perimeter, and shape factor, were altered (P <0.001) for cells on both glycated proteins. Finally, cell migration was reduced on glycated FN and COLI (P <0.001). Conclusions: MG treatment efficiently glycated COLI and FN, providing a new tool to study the effects of diabetes on periodontal disease. The substantial effects of glycated COLI and FN on hGF and hPDL behavior indicated that protein glycation contributed to the pathogenesis and altered periodontal wound healing observed in patients with diabetes.

KW - Advanced glycation end products

KW - Diabetes mellitus

KW - Fibronectin

KW - Methylglyoxal

KW - Periodontal disease

KW - Type I collagen

UR - http://www.scopus.com/inward/record.url?scp=55749086406&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=55749086406&partnerID=8YFLogxK

U2 - 10.1902/jop.2008.080210

DO - 10.1902/jop.2008.080210

M3 - Article

C2 - 18980529

AN - SCOPUS:55749086406

VL - 79

SP - 2190

EP - 2199

JO - Journal of Periodontology

JF - Journal of Periodontology

SN - 0022-3492

IS - 11

ER -